cysteine has been researched along with mycothiol in 156 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 11 (7.05) | 18.2507 |
| 2000's | 68 (43.59) | 29.6817 |
| 2010's | 69 (44.23) | 24.3611 |
| 2020's | 8 (5.13) | 2.80 |
| Authors | Studies |
|---|---|
| Aharonowitz, Y; Bewley, CA; Cohen, G; Davies, J; Dwyer, TJ; Fahey, RC; Faulkner, DJ; Horn, R; Newton, GL | 1 |
| Spies, HS; Steenkamp, DJ | 1 |
| Aharonowitz, Y; Arnold, K; Cohen, G; Davies, J; Davis, C; Delcardayre, SB; Fahey, RC; Newton, GL; Price, MS; Sherrill, C | 1 |
| Duine, JA; Misset-Smits, M; Sakuda, S; van Ophem, PW | 1 |
| Bornemann, C; Jardine, MA; Spies, HS; Steenkamp, DJ | 1 |
| Duine, JA; Jörnvall, H; Norin, A; Persson, B; Piersma, SR; Van Ophem, PW | 1 |
| Davis, C; Fahey, RC; Newton, GL; Unson, MD | 1 |
| Anderberg, SJ; Fahey, RC; Newton, GL | 1 |
| Aguilera, JA; Anderberg, SJ; Av-Gay, Y; delCardayre, SB; Fahey, RC; Newton, GL; Oh, NN; Unson, MD | 1 |
| Arnold, KF; Davis, CE; Fahey, RC; Newton, GL; Unson, MD | 1 |
| Duine, JA | 1 |
| Av-Gay, Y; Fahey, RC; Newton, GL | 2 |
| Fahey, RC | 2 |
| Aharonowitz, Y; Buttner, MJ; Cohen, G; Molle, V; Paget, MS | 1 |
| Gammon, DW; Jardine, MA; Nkambule, CM; Spies, HS; Steenkamp, DJ | 1 |
| Bewley, CA; Kovác, P; Nicholas, GM | 1 |
| Fahey, RC; Newton, GL; Sareen, D; Steffek, M | 1 |
| Vorholt, JA | 1 |
| Fahey, RC; Koledin, T; Newton, GL | 1 |
| Av-Gay, Y; Fahey, RC; Ko, M; Martinez, GJ; Newton, GL; Rawat, M | 1 |
| Fahey, RC; Newton, GL | 2 |
| Bewley, CA; Eckman, LL; Gonzalez, S; Knapp, S; Myers, DS | 1 |
| Bertozzi, CR; Leary, JA; Leavell, MD; Leigh, CD; Mougous, JD; Riley, LW; Senaratne, RH; Williams, SJ | 1 |
| Buchmeier, NA; Fahey, RC; Koledin, T; Newton, GL | 1 |
| Bewley, CA; Mahadevan, J; Nicholas, GM | 1 |
| Av-Gay, Y; Billman-Jacobe, H; Kovacevic, S; Rawat, M | 1 |
| Av-Gay, Y; Fahey, RC; Gorovitz, B; Koledin, T; Newton, GL; Rawat, M | 1 |
| Bewley, CA; Eckman, LL; Kovác, P; Nicholas, GM; Otero-Quintero, S | 1 |
| Gammon, DW; Hunter, R; Mudzunga, TT; Steenkamp, DJ | 1 |
| Blanchard, JS; Steenkamp, DJ; Vogt, RN; Zheng, R | 1 |
| Blanchard, JS; Roderick, SL; Vetting, MW; Yu, M | 1 |
| Av-Gay, Y; Fahey, RC; Newton, GL; Steffek, M | 1 |
| Buchmeier, NA; Fahey, RC; Newton, GL; Sareen, D | 1 |
| Baker, EN; Knijff, R; McCarthy, AA; Peterson, NA | 1 |
| Steenkamp, DJ; Vogt, RN | 1 |
| Lee, S; Rosazza, JP | 1 |
| Av-Gay, Y; Bancroft, GJ; Daffe, M; Dinadayala, P; Kendall, SL; McAlister, MS; McDonald, NQ; Movahedzadeh, F; Murray-Rust, J; Norman, RA; Rison, SC; Russell, DG; Smith, DA; Stoker, NG | 1 |
| Hayward, D; van Helden, P; Wiid, I | 1 |
| Av-Gay, Y; Fahey, RC; Newton, G; Rawat, M; Steffek, M; Uppal, M | 1 |
| Coldham, NG; Gordon, SV; Hewinson, RG; Keating, L; Parish, T; Wheeler, PR; Wooff, EE | 1 |
| Fahey, RC; Newton, GL; Ta, P | 1 |
| Blanchard, JS; Rendle, PM; Vetting, MW; Yu, M | 1 |
| Che, Y; Feng, J; Kalinowski, J; Liu, L; Liu, SJ; Milse, J; Qi, SW; Rückert, C; Shen, XH; Yin, YJ | 1 |
| Cha, CJ; Park, JH; Roe, JH | 1 |
| Auzanneau, FI; Hand, CE; Honek, JF | 1 |
| Av-Gay, Y; Fahey, RC; Ko, M; Newton, GL; Ta, P | 1 |
| Av-Gay, Y; Ung, KS | 1 |
| Fahey, RC; Newton, GL; Sareen, D; Ta, P | 1 |
| Nguyen, L; Thompson, CJ | 1 |
| Bewley, CA; Fahey, RC; Gutierrez-Lugo, MT; Newton, GL | 1 |
| Bzymek, KP; Fahey, RC; Newton, GL; Ta, P | 2 |
| Buchmeier, N; Fahey, RC | 1 |
| Bewley, CA; Metaferia, BB; Ray, S; Smith, JA | 1 |
| Chen, Z; Huang, Q; Li, X; Li, Y; Xu, S; Zhang, H; Zhang, Y | 1 |
| Av-Gay, Y; Rawat, M | 1 |
| Bergeron, H; Lau, PC; Lee, S; Rosazza, JP | 1 |
| Chang, WR; Feng, J; Li, M; Liu, SJ; Wang, F; Wang, R; Yin, YJ; Zhang, HM; Zhang, JP | 1 |
| Gammon, DW; Oscarson, S; Slättegård, R | 1 |
| Av-Gay, Y; Johnson, T; Miller, CC; Rawat, M | 1 |
| Av-Gay, Y; Cadiz, V; Johnson, C; Rawat, M | 1 |
| Blanchard, JS; Fan, F; Luxenburger, A; Painter, GF | 1 |
| Bhave, DP; Carroll, KS; Muse, WB | 1 |
| Bewley, CA; Fetterolf, BJ; Gutierrez-Lugo, MT; Metaferia, BB; Moravec, M; Ray, S; Shazad-Ul-Hussan, S; Smith, JA | 1 |
| Hamilton, CJ; Jothivasan, VK; Rowan, AS; Stewart, MJ; Wagg, J | 1 |
| Park, JH; Roe, JH | 1 |
| Fahey, RC; Fenical, W; Jensen, PR; Macmillan, JB; Newton, GL | 1 |
| Alland, D; Attarian, R; Av-Gay, Y; Chen, B; Colangeli, R; Hazbón, MH; Jacobs, WR; Liu, W; Liu, Z; Sacchettini, JC; Vilchèze, C | 1 |
| Fahey, RC; Johnson, T; Newton, GL; Rawat, M | 1 |
| Buchmeier, N; Fahey, RC; Newton, GL | 1 |
| Hamilton, CJ; Jothivasan, VK | 1 |
| Blanchard, JS; Fan, F; Tremblay, LW; Vetting, MW | 1 |
| Bonner, A; Finlay, RM; Hamilton, CJ; Stewart, MJ | 1 |
| De Galan, S; Gil, JA; Letek, M; Mateos, LM; Messens, J; Ordóñez, E; Roos, G; Van Belle, K; Wyns, L | 1 |
| Blanchard, JS; Fan, F | 1 |
| Baker, H; Bewley, CA; Boshoff, H; Gutierrez-Lugo, MT; Shiloach, J | 1 |
| Blanchard, JS; Fan, F; Frantom, PA; Vetting, MW | 1 |
| Gammon, DW; Hunter, R; Marakalala, MJ; Mavumengwana, V; Mudzunga, TT; Munyololo, M; Steenkamp, DJ | 1 |
| Ajayi, K; Knapp, S; Lapo, RC; Thakur, VV | 1 |
| Claiborne, A; Dos Santos, PC; Hamilton, CJ; Holder, RC; Newton, GL; Paige, C; Parsonage, D; Redinbo, MR; Reid, SD; Wallace, BD | 1 |
| Jiang, CY; Jin, JH; Liu, SJ; Luo, YM; Wang, BJ; Yin, YJ | 1 |
| Buchmeier, N; Fahey, RC; Newton, GL; Rawat, M; Ta, P | 1 |
| Av-Gay, Y; Gómez-Velasco, A; Jacobs, WR; Vilchèze, C; Xu, X | 1 |
| Hernick, M; Huang, X; Kocabas, E | 1 |
| Buchmeier, N; Fahey, RC; La Clair, JJ; Newton, GL | 1 |
| Av-Gay, Y; Barnes, SW; Glynne, RJ; Jacobs, WR; Larsen, MH; Vilchèze, C; Walker, JR | 1 |
| Chung, CC; Hung, SC; Padiyar, LT; Zulueta, MM | 1 |
| Fahey, RC; Leung, SS; Newton, GL; Rawat, M; Wakabayashi, JI | 1 |
| Chi, HW; Chin, DH; Huang, CC | 1 |
| Fahey, RC; Gushiken, M; Holden, D; Lo, K; Newton, GL; Rawat, M; Upton, H | 1 |
| Eastwood, H; Jardine, A; Lamprecht, DA; Muneri, NO; Naidoo, KJ; Strauss, E | 1 |
| Buts, L; Foloppe, N; Mateos, LM; Messens, J; Nilsson, L; Rawat, M; Roos, G; Van Belle, K; Van Laer, K; van Nuland, NA; Vertommen, D; Wahni, K | 1 |
| McConnell, MS; Nguyen, HM; Yu, F | 1 |
| Antelmann, H; Hamilton, CJ | 1 |
| Collet, JF; Dziewulska, AM; Fislage, M; Hbeddou, A; Mateos, LM; Messens, J; Tamu Dufe, V; Van Laer, K; Versées, W; Wahni, K | 1 |
| Hernick, M | 1 |
| Gammon, DW; Naidoo, KJ; Rogers, IL | 1 |
| Liu, YB; Long, MX; Lu, ZQ; Shen, XH; Si, MR; Wang, Y; Yin, YJ; Zhang, L | 1 |
| Baker, B; Hiten, NF; Pietersen, RD; Sao Emani, C; van Helden, PD; Viljoen, AJ; Wiid, IJ; Williams, MJ | 1 |
| Hartman, T; Jacobs, WR; Vilchèze, C; Weinrick, B | 1 |
| Antelmann, H; Bäsell, K; Becher, D; Busche, T; Chi, BK; Clermont, L; Kalinowski, J; Messens, J; Persicke, M; Seibold, GM; Van Laer, K | 1 |
| Hernick, M; Huang, X | 1 |
| Kathiravan, MK; Nilewar, SS | 1 |
| Hugo, M; Messens, J; Radi, R; Reyes, AM; Trujillo, M; Van Laer, K; Vertommen, D | 1 |
| Bhaskar, A; Bhave, D; Carroll, KS; Chandra, P; Chawla, M; Kumar, D; Mehta, M; Parikh, P; Singh, A | 1 |
| Chaudhry, MT; Chen, C; Liu, YB; Shen, XH; Si, MR; Wang, Y; Zhang, L | 1 |
| Liu, W; Wang, M; Xu, D; Zhang, Q; Zhao, Q | 1 |
| Melançon, CE | 1 |
| Dairi, T; Matsui, T; Nakajima, S; Satoh, Y; Yanashima, K | 1 |
| Gazak, R; Janata, J; Kadlcik, S; Kamenik, Z; Koberska, M; Kopecky, J; Najmanova, L; Novak, P; Novotna, J; Plhackova, K; Radojevic, B; Ulanova, D | 1 |
| Erdogan, H; Messens, J; Pedre, B; Tossounian, MA; Van Molle, I; Vertommen, D; Wahni, K | 1 |
| Erdogan, H; Mateos, LM; Messens, J; Pedre, B; Turell, L; Van Molle, I; Vertommen, D; Villadangos, AF; Wahni, K | 1 |
| Corkran, HM; Dasyam, N; Field, JJ; Harvey, JE; Riordan, SW; Stocker, BL; Teesdale-Spittle, PH; Timmer, MS | 1 |
| Ikeda, H; Nagamitsu, T; Shin-Ya, K; Tomoda, H | 1 |
| Liu, W; Wang, M; Zhao, Q | 1 |
| Mehta, M; Rajmani, RS; Singh, A | 1 |
| Adamson, JH; Av-Gay, Y; Bach, H; Chinta, KC; Cumming, BM; Eoh, H; Glasgow, JN; Gomez-Velasco, A; Guidry, L; Lamprecht, DA; Mazorodze, JH; Reddy, VP; Rhee, K; Richard-Greenblatt, M; Saini, V; Steyn, AJC | 1 |
| Lawrence, R; Patel, ND; Peteroy-Kelly, MA | 1 |
| Gao, F; Kang, Y; Li, M; Shen, X; Si, M; Su, T; Wang, T; Zhao, C | 1 |
| Chen, C; Lin, J; Liu, Y; Pan, J; Shen, X; Si, M; Yang, X; Yin, Y | 1 |
| Gulati, M; Hageman, S; Nobile, CJ; Rawat, M; Vargas, D | 1 |
| Hamilton, CJ; Messens, J; Sharma, SV; Van Laer, K | 1 |
| Chen, K; Shen, X; Si, M; Wei, D; Xiao, H; Yang, X; Zhang, B; Zhao, C | 1 |
| Balakrishna, AM; Grüber, G; Kumar, A; Manimekalai, MSS; Nartey, W | 1 |
| Blanco Capurro, JI; González Lebrero, MC; Hopkins, CW; Marti, MA; Pierdominici Sottile, G; Roitberg, AE | 1 |
| Alvarez, HM; Dávila Costa, JS; Leichert, L; Silva, RA | 1 |
| De Armas, MI; Messens, J; Pedre, B; Radi, R; Reyes, AM; Tossounian, MA; Trujillo, M | 1 |
| Gu, G; Guo, J; Guo, Y; Guo, Z; Wang, L | 1 |
| Antelmann, H; Becher, D; Bernhardt, J; Busche, T; Hell, R; Hillion, M; Kalinowski, J; Maaß, S; Rawat, M; Rossius, M; Rückert, C; Wirtz, M | 1 |
| Adrian, L; Antelmann, H; Astolfi Rosado, L; Becher, D; Bernhardt, J; Hell, R; Hillion, M; Imber, M; Loi, VV; Maaß, S; Messens, J; Pedre, B; Saleh, M; Weise, C; Wirtz, M | 1 |
| Aboushleib, HM; Bahey-El-Din, M; Kassem, MA; Zeitoun, H | 1 |
| Baker, B; Sao Emani, C; Taylor, MJC; Van Helden, PD; Wiid, IJ; Williams, MJ | 1 |
| Andreana, PR; Patel, K; Song, F | 1 |
| Comini, MA; Salinas, G | 1 |
| Grüber, G; Kumar, A; Subramanian Manimekalai, MS | 1 |
| Antelmann, H; Linzner, N; Loi, VV; Tung, QN | 1 |
| Barman, D; Beuming, T; Burns-Huang, K; Gold, B; Ioerger, T; Javidnia, P; Jiang, X; Li, H; Ling, Y; Liu, G; Mu, R; Nathan, CF; Negri, A; Oren, DA; Rhee, KY; Roberts, J; Sacchettini, JC; Somersan-Karakaya, S; Vendome, J; Wang, H; Warren, JD; Warrier, T; Wu, J; Zhang, X | 1 |
| Gazak, R; Janata, J; Kadlcik, S; Kamenik, Z; Najmanova, L | 1 |
| Baker, B; Sao Emani, C; Wiid, IJ; Williams, MJ | 1 |
| Baker, B; Carolis, C; Sao Emani, C; Taylor, MJC; Van Helden, PD; Wiid, IJ; Williams, MJ | 1 |
| Chen, C; Chen, K; Li, G; Pan, J; Si, M; Su, T; Zhang, B | 1 |
| Antelmann, H; Imber, M; Pietrzyk-Brzezinska, AJ | 1 |
| Baker, B; Gallant, JL; Sao Emani, C; Wiid, IJ | 1 |
| Liu, HH; Liu, YJ; Ren, YH; Sun, WJ; Wang, FQ; Wang, L; Wei, DZ | 1 |
| Che, C; Chen, C; Gong, Z; Li, G; Li, X; Liu, J; Si, M; Yang, G | 1 |
| Buts, L; Khanh Truong, AC; Leermakers, M; Mateos, LM; Messens, J; Mourenza, Á; Tossounian, MA; Vertommen, D; Volkov, AN; Wahni, K | 1 |
| Heine, T; Lienkamp, AC; Tischler, D | 1 |
| Che, C; Gong, Z; Li, X; Liu, Y; Si, M; Yang, G; Zhong, J | 1 |
| Aung, HL; Cook, GM; Dickerhof, N; Forrester, L; Hampton, MB; Kettle, AJ; Messens, J; Parker, HA; Ryburn, H; Smyth, L | 1 |
| Al-Nayal, A; Carapito, C; Dahl, C; Heintz, D; Hirschler, A; Ismail, W; Mahmoud, H; Maurer, L; Sangal, V; Van Dorsselaer, A; Villette, C; Zumsteg, J | 1 |
| Chen, K; Li, X; Liu, Y; Si, M; Su, T; Yu, X; Zhang, X | 1 |
| Castillo Arteaga, RD; Garrido, LM; Gross, H; Gust, B; Helmle, I; Padilla, G; Pedre, B | 1 |
| Honma, S; Ito, S; Kogo, M; Sasaki, Y; Shibui, Y; Yajima, S; Yoshizumi, T | 1 |
17 review(s) available for cysteine and mycothiol
| Article | Year |
|---|---|
Thiols in formaldehyde dissimilation and detoxification.
Topics: Aldehyde Oxidoreductases; Cysteine; Disaccharides; Formaldehyde; Glutathione; Glycopeptides; Gram-Positive Bacteria; Inactivation, Metabolic; Inositol; Mycobacterium; Pyrazoles; Sulfhydryl Compounds | 1999 |
Novel thiols of prokaryotes.
Topics: Cysteine; Disaccharides; Ergothioneine; Glutathione; Glycopeptides; Inositol; Mesna; Models, Chemical; Phosphothreonine; Prokaryotic Cells; Pyrazoles; Sulfhydryl Compounds | 2001 |
Cofactor-dependent pathways of formaldehyde oxidation in methylotrophic bacteria.
Topics: Cysteine; Disaccharides; Formaldehyde; Glutathione; Glycopeptides; Inositol; Methanol; Oxidation-Reduction; Proteobacteria; Pyrazoles; Sulfhydryl Compounds; Tetrahydrofolates | 2002 |
Mycothiol biochemistry.
Topics: Aldehyde Oxidoreductases; Amidohydrolases; Cysteine; Disaccharides; Glycopeptides; Inactivation, Metabolic; Inositol; Mycobacterium tuberculosis; Oxidation-Reduction; Pyrazoles; Sulfhydryl Compounds | 2002 |
Mycothiol-dependent proteins in actinomycetes.
Topics: Actinobacteria; Amidohydrolases; Biosynthetic Pathways; Coenzymes; Cysteine; Glycopeptides; Inactivation, Metabolic; Inositol; Molecular Sequence Data; Mycobacterium tuberculosis; NADH, NADPH Oxidoreductases; Oxidation-Reduction | 2007 |
Drug targets in mycobacterial sulfur metabolism.
Topics: Antitubercular Agents; Biological Transport; Cysteine; Glutathione; Glycopeptides; Inositol; Methionine; Mycobacterium tuberculosis; NADPH Oxidases; Sulfates; Sulfotransferases; Sulfur | 2007 |
Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria.
Topics: Actinobacteria; Bacterial Proteins; Cysteine; Gene Expression Regulation, Bacterial; Glycopeptides; Inositol; Mutation | 2008 |
Mycothiol: synthesis, biosynthesis and biological functions of the major low molecular weight thiol in actinomycetes.
Topics: Actinobacteria; Cysteine; Glycopeptides; Inositol; Molecular Structure; Molecular Weight; Sulfhydryl Compounds | 2008 |
Structures and mechanisms of the mycothiol biosynthetic enzymes.
Topics: Acetylesterase; Amidohydrolases; Bacterial Proteins; Cysteine; Glycopeptides; Glycosyltransferases; Inositol; Ligases; Models, Molecular; Mycobacterium tuberculosis | 2009 |
Glutathione analogs in prokaryotes.
Topics: Bacteria; Cysteine; Glutathione; Glycopeptides; Humans; Inositol; Molecular Weight; Oxygen; Prokaryotic Cells | 2013 |
Mycothiol: a target for potentiation of rifampin and other antibiotics against Mycobacterium tuberculosis.
Topics: Animals; Anti-Bacterial Agents; Antitubercular Agents; Cysteine; Drug Delivery Systems; Drug Synergism; Enzyme Inhibitors; Glycopeptides; Humans; Inositol; Mycobacterium tuberculosis; Rifampin | 2013 |
Mycothiol: a promising antitubercular target.
Topics: Antitubercular Agents; Cysteine; Glycopeptides; Inositol; Molecular Targeted Therapy; Mycobacterium tuberculosis | 2014 |
Chemistry and Redox Biology of Mycothiol.
Topics: Cysteine; Glycopeptides; Inositol; Mycobacterium tuberculosis; Oxidants; Oxidation-Reduction; Oxidative Stress; Peroxidases; Sulfhydryl Compounds | 2018 |
Application of genetically encoded redox biosensors to measure dynamic changes in the glutathione, bacillithiol and mycothiol redox potentials in pathogenic bacteria.
Topics: Biosensing Techniques; Cysteine; Glucosamine; Glutathione; Glycopeptides; Green Fluorescent Proteins; Humans; Inositol; Mycobacterium tuberculosis; Oxidation-Reduction; Recombinant Fusion Proteins; Staphylococcus aureus | 2018 |
Biosynthesis and incorporation of an alkylproline-derivative (APD) precursor into complex natural products.
Topics: Anti-Bacterial Agents; Antineoplastic Agents; Benzodiazepines; Biological Products; Cysteine; Depsipeptides; Ergothioneine; Evolution, Molecular; Glycopeptides; Humans; Inositol; Lincomycin; Lincosamides; Molecular Structure | 2018 |
Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.
Topics: Animals; Cysteine; Glucosamine; Glycopeptides; Gram-Positive Bacteria; Humans; Inositol; Models, Biological; Oxidation-Reduction; Protein Processing, Post-Translational; Structure-Activity Relationship; Sulfhydryl Compounds | 2019 |
The role of low molecular weight thiols in Mycobacterium tuberculosis.
Topics: Animals; Antitubercular Agents; Cysteine; Dipeptides; Enzyme Inhibitors; Enzymes; Ergothioneine; Glycopeptides; Humans; Inositol; Molecular Targeted Therapy; Molecular Weight; Mycobacterium tuberculosis; Sulfhydryl Compounds; Tuberculosis | 2019 |
139 other study(ies) available for cysteine and mycothiol
| Article | Year |
|---|---|
The structure of U17 isolated from Streptomyces clavuligerus and its properties as an antioxidant thiol.
Topics: Antioxidants; Carbohydrate Sequence; Chromatography, High Pressure Liquid; Cysteine; Disaccharides; Glycopeptides; Inositol; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Molecular Structure; Pyrazoles; Streptomyces; Sulfhydryl Compounds | 1995 |
Thiols of intracellular pathogens. Identification of ovothiol A in Leishmania donovani and structural analysis of a novel thiol from Mycobacterium bovis.
Topics: Animals; Chromatography, High Pressure Liquid; Cysteine; Disaccharides; Glycopeptides; Hydrolysis; Inositol; Leishmania donovani; Magnetic Resonance Spectroscopy; Mass Spectrometry; Methylhistidines; Molecular Weight; Mycobacterium bovis; Mycobacterium tuberculosis; NADH, NADPH Oxidoreductases; Pyrazoles; Sulfhydryl Compounds | 1994 |
Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes.
Topics: Actinomycetales; Coenzyme A; Cysteine; Disaccharides; Glycopeptides; Inositol; Molecular Structure; Pyrazoles; Sulfhydryl Compounds | 1996 |
Mycothiol, 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D- myo-inositol, is the factor of NAD/factor-dependent formaldehyde dehydrogenase.
Topics: Aldehyde Oxidoreductases; Bacterial Proteins; Chromatography, High Pressure Liquid; Cysteine; Disaccharides; Glycopeptides; Inositol; NAD; Pyrazoles; Streptomyces; Sulfhydryl Compounds | 1997 |
Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis.
Topics: Acetates; Carbohydrate Conformation; Cysteine; Disaccharides; Glycopeptides; Inositol; Magnetic Resonance Spectroscopy; Mycobacterium; Pyrazoles; Substrate Specificity; Sulfhydryl Compounds | 1997 |
Mycothiol-dependent formaldehyde dehydrogenase, a prokaryotic medium-chain dehydrogenase/reductase, phylogenetically links different eukaroytic alcohol dehydrogenases--primary structure, conformational modelling and functional correlations.
Topics: Actinomycetales; Aldehyde Oxidoreductases; Amino Acid Sequence; Cysteine; Disaccharides; Fatty Acid Desaturases; Glycopeptides; Humans; Inositol; Models, Molecular; Molecular Sequence Data; Phylogeny; Protein Conformation; Pyrazoles; Sequence Homology, Amino Acid; Sulfhydryl Compounds | 1997 |
An immunoassay for the detection and quantitative determination of mycothiol.
Topics: Animals; Antibodies; Chromatography, High Pressure Liquid; Cysteine; Disaccharides; Enterococcus faecalis; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Female; Glycopeptides; Hemocyanins; Immunoglobulin G; Immunohistochemistry; Inositol; Mycobacterium; Pyrazoles; Rabbits; Sensitivity and Specificity; Serum Albumin, Bovine; Streptococcus mutans; Sulfhydryl Compounds | 1998 |
Mycothiol biosynthesis and metabolism. Cellular levels of potential intermediates in the biosynthesis and degradation of mycothiol in mycobacterium smegmatis.
Topics: Chromatography, High Pressure Liquid; Cysteine; Disaccharides; Glycopeptides; Inositol; Models, Chemical; Mycobacterium smegmatis; Pyrazoles; Sulfhydryl Compounds | 1998 |
Characterization of Mycobacterium smegmatis mutants defective in 1-d-myo-inosityl-2-amino-2-deoxy-alpha-d-glucopyranoside and mycothiol biosynthesis.
Topics: Culture Media; Cysteine; Disaccharides; Drug Resistance, Microbial; Genetic Complementation Test; Glucosides; Glycopeptides; Hydrogen Peroxide; Inositol; Isoniazid; Mutagenesis; Mycobacterium smegmatis; Pyrazoles; Rifampin; Sulfhydryl Compounds | 1999 |
Improved methods for immunoassay of mycothiol.
Topics: Animals; Antibodies; Antibody Specificity; Biotinylation; Cerebrospinal Fluid; Cysteine; Disaccharides; Enzyme-Linked Immunosorbent Assay; Glycopeptides; Humans; Indicators and Reagents; Inositol; Mycobacterium Infections, Nontuberculous; Mycobacterium smegmatis; Pyrazoles; Rabbits; Sensitivity and Specificity; Sulfhydryl Compounds; Urine | 1999 |
A novel mycothiol-dependent detoxification pathway in mycobacteria involving mycothiol S-conjugate amidase.
Topics: Aldehyde Oxidoreductases; Alkylation; Amidohydrolases; Amino Acid Sequence; Bacterial Proteins; Cysteine; Disaccharides; Escherichia coli; Glycopeptides; Hydrolysis; Inactivation, Metabolic; Inositol; Molecular Sequence Data; Mycobacterium smegmatis; Mycobacterium tuberculosis; Pyrazoles; Sequence Homology, Amino Acid; Sulfhydryl Compounds | 2000 |
N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) is a key enzyme in mycothiol biosynthesis.
Topics: Acetylation; Acetylglucosamine; Amidohydrolases; Bacterial Proteins; Cysteine; Disaccharides; Glycopeptides; Inositol; Mutation; Mycobacterium smegmatis; Mycobacterium tuberculosis; Pyrazoles; Sulfhydryl Compounds | 2000 |
Defining the disulphide stress response in Streptomyces coelicolor A3(2): identification of the sigmaR regulon.
Topics: Amino Acid Sequence; Bacterial Proteins; Consensus Sequence; Cysteine; Databases, Genetic; Disaccharides; Disulfides; DNA-Directed RNA Polymerases; Gene Expression Regulation, Bacterial; Genes, Bacterial; Glutaredoxins; Glycopeptides; Inositol; Molecular Sequence Data; Operon; Oxidoreductases; Promoter Regions, Genetic; Proteins; Pyrazoles; Regulon; Ribosomes; RNA, Bacterial; Sequence Alignment; Sigma Factor; Streptomyces; Sulfhydryl Compounds | 2001 |
Synthesis of mycothiol, 1D-1-O-(2-[N-acetyl-L-cysteinyl]amino-2-deoxy-alpha-D-glucopyranosyl)-myo-inositol, principal low molecular mass thiol in the actinomycetes.
Topics: Actinomycetales; Cysteine; Disaccharides; Glycopeptides; Inositol; Molecular Weight; Mycobacterium smegmatis; Nuclear Magnetic Resonance, Biomolecular; Pyrazoles; Sulfhydryl Compounds | 2002 |
Total synthesis and proof of structure of mycothiol bimane.
Topics: Bridged Bicyclo Compounds, Heterocyclic; Circular Dichroism; Cysteine; Disaccharides; Glycopeptides; Inositol; Pyrazoles; Sulfhydryl Compounds | 2002 |
ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases.
Topics: Adenosine Triphosphate; Amino Acyl-tRNA Synthetases; Base Sequence; Cysteine; Databases, Nucleic Acid; Disaccharides; Glycopeptides; Inositol; Ligases; Molecular Sequence Data; Mycobacterium smegmatis; Mycobacterium tuberculosis; Pyrazoles; Sulfhydryl Compounds | 2002 |
Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes.
Topics: Acetyltransferases; Amidohydrolases; Amino Acid Sequence; Bacterial Proteins; Cloning, Molecular; Cosmids; Cysteine; Disaccharides; DNA Transposable Elements; Glycopeptides; Inositol; Molecular Sequence Data; Mutagenesis, Insertional; Mutation; Mycobacterium smegmatis; Pyrazoles; Sequence Homology, Amino Acid; Sulfhydryl Compounds | 2002 |
Mycothiol-deficient Mycobacterium smegmatis mutants are hypersensitive to alkylating agents, free radicals, and antibiotics.
Topics: Alkylating Agents; Amino Acid Sequence; Amino Acid Substitution; Anti-Bacterial Agents; Cysteine; Disaccharides; DNA Transposable Elements; DNA, Bacterial; Free Radicals; Genetic Complementation Test; Glycopeptides; Inositol; Ligases; Microbial Sensitivity Tests; Molecular Sequence Data; Mutation; Mycobacterium smegmatis; Oxidative Stress; Phenotype; Pyrazoles; Sulfhydryl Compounds | 2002 |
Shortcut to mycothiol analogues.
Topics: Amidohydrolases; Antitubercular Agents; Cysteine; Disaccharides; Drug Design; Glycopeptides; Inositol; Molecular Structure; Mycobacterium tuberculosis; Pyrazoles; Sulfhydryl Compounds | 2002 |
Discovery of sulfated metabolites in mycobacteria with a genetic and mass spectrometric approach.
Topics: Cysteine; Disaccharides; Genetic Engineering; Glycopeptides; Inositol; Mass Spectrometry; Mycobacterium smegmatis; Mycobacterium tuberculosis; Pyrazoles; Sulfates; Sulfhydryl Compounds; Sulfoglycosphingolipids; Sulfur Isotopes | 2002 |
Association of mycothiol with protection of Mycobacterium tuberculosis from toxic oxidants and antibiotics.
Topics: Amidohydrolases; Anti-Bacterial Agents; Antitubercular Agents; Bacterial Proteins; Benzene Derivatives; Catalase; Cell Division; Culture Media; Cysteine; Disaccharides; Drug Resistance, Multiple, Bacterial; Glycopeptides; Inositol; Isoniazid; Microbial Sensitivity Tests; Mutation; Mycobacterium smegmatis; Mycobacterium tuberculosis; Oleic Acid; Oxidants; Pyrazoles; Rifampin; Sulfhydryl Compounds | 2003 |
Solution conformations of mycothiol bimane, 1-D-GlcNAc-alpha-(1 --> 1)-D-myo-Ins and 1-D-GlcNAc-alpha-(1 --> 1)-L-myo-Ins.
Topics: Actinomyces; Amidohydrolases; Cyclization; Cysteine; Disaccharides; Glycopeptides; Inositol; Molecular Conformation; Molecular Structure; Nuclear Magnetic Resonance, Biomolecular; Pyrazoles; Stereoisomerism; Structure-Activity Relationship; Sulfhydryl Compounds | 2003 |
Inactivation of mshB, a key gene in the mycothiol biosynthesis pathway in Mycobacterium smegmatis.
Topics: Amidohydrolases; Amino Acid Sequence; Bacterial Proteins; Cysteine; Disaccharides; Ethionamide; Genetic Complementation Test; Glycopeptides; Inositol; Microbial Sensitivity Tests; Molecular Sequence Data; Mutation; Mycobacterium smegmatis; Oxidative Stress; Pyrazoles; Recombination, Genetic; Sequence Analysis, DNA; Sulfhydryl Compounds | 2003 |
The glycosyltransferase gene encoding the enzyme catalyzing the first step of mycothiol biosynthesis (mshA).
Topics: Amino Acid Sequence; Bacterial Proteins; Cysteine; Disaccharides; DNA Transposable Elements; Glycopeptides; Glycosyltransferases; Inositol; Molecular Sequence Data; Mutation; Mycobacterium smegmatis; Mycobacterium tuberculosis; Pyrazoles; Sequence Alignment; Sulfhydryl Compounds | 2003 |
Synthesis of 1-D- and 1-L-myo-inosityl 2-N-acetamido-2-deoxy-alpha-D-glucopyranoside establishes substrate specificity of the Mycobacterium tuberculosis enzyme AcGI deacetylase.
Topics: Amidohydrolases; Bacterial Proteins; Cysteine; Disaccharides; Glycopeptides; Inositol; Mycobacterium tuberculosis; Pyrazoles; Recombinant Fusion Proteins; Stereoisomerism; Substrate Specificity; Sulfhydryl Compounds | 2003 |
Synthesis of 2-deoxy-2-C-alkylglucosides of myo-inositol as possible inhibitors of a N-deacetylase enzyme in the biosynthesis of mycothiol.
Topics: Amidohydrolases; Cysteine; Disaccharides; Enzyme Inhibitors; Glucosides; Glycopeptides; Inositol; Mycobacterium smegmatis; Pyrazoles; Sulfhydryl Compounds; Tritium | 2003 |
The metabolism of nitrosothiols in the Mycobacteria: identification and characterization of S-nitrosomycothiol reductase.
Topics: Aldehyde Oxidoreductases; Bacterial Proteins; Carbohydrate Sequence; Cloning, Molecular; Cysteine; Disaccharides; Enzyme Stability; Glycopeptides; Hydrogen-Ion Concentration; Inositol; Mycobacterium smegmatis; Mycobacterium tuberculosis; NADH, NADPH Oxidoreductases; Pyrazoles; Recombinant Proteins; S-Nitrosoglutathione; Spectrometry, Mass, Electrospray Ionization; Sulfhydryl Compounds | 2003 |
Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.
Topics: Acetyltransferases; Amino Acid Motifs; Binding Sites; Crystallography, X-Ray; Cysteine; Databases as Topic; Disaccharides; Glycopeptides; Inositol; Models, Molecular; Multigene Family; Mycobacterium tuberculosis; Plasmids; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Pyrazoles; Sulfhydryl Compounds | 2003 |
Characterization of Mycobacterium tuberculosis mycothiol S-conjugate amidase.
Topics: Amidohydrolases; Amino Acid Sequence; Cloning, Molecular; Cysteine; Disaccharides; Enzyme Inhibitors; Glycopeptides; Hydrolysis; Inositol; Kinetics; Metals, Heavy; Molecular Sequence Data; Mycobacterium tuberculosis; Pyrazoles; Recombinant Proteins; Rifamycins; Substrate Specificity; Sulfhydryl Compounds | 2003 |
Mycothiol is essential for growth of Mycobacterium tuberculosis Erdman.
Topics: Adenosine Triphosphate; Bacterial Proteins; Culture Media; Cysteine; Disaccharides; Genes, Bacterial; Genes, Essential; Glycopeptides; Inositol; Ligases; Mycobacteriophages; Mycobacterium tuberculosis; Pyrazoles; Sulfhydryl Compounds | 2003 |
Crystal structure of MshB from Mycobacterium tuberculosis, a deacetylase involved in mycothiol biosynthesis.
Topics: Amidohydrolases; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Cysteine; Disaccharides; Glycopeptides; Hydrogen Bonding; Inositol; Ligands; Metals; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis; Protein Structure, Secondary; Pyrazoles; Sequence Alignment; Sulfhydryl Compounds | 2004 |
Preparation and utilization of a reagent for the isolation and purification of low-molecular-mass thiols.
Topics: Chromatography, High Pressure Liquid; Chromatography, Thin Layer; Cysteine; Disaccharides; Dithiothreitol; Glutathione; Glycopeptides; Inositol; Mycobacterium smegmatis; Naphthalenes; Pyrazoles; Sulfhydryl Compounds; Sulfhydryl Reagents | 2004 |
First total synthesis of mycothiol and mycothiol disulfide.
Topics: Cysteine; Disaccharides; Glucosamine; Glycopeptides; Inositol; Molecular Structure; Pyrazoles; Sulfhydryl Compounds | 2004 |
The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cysteine; Disaccharides; DNA Mutational Analysis; Gene Deletion; Genes, Bacterial; Genes, Essential; Glycopeptides; Inositol; Lipopolysaccharides; Macrophages; Mice; Mice, SCID; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Mycobacterium tuberculosis; Myo-Inositol-1-Phosphate Synthase; Phosphatidylinositols; Pyrazoles; Sulfhydryl Compounds; Tuberculosis; Virulence | 2004 |
Differential expression of mycothiol pathway genes: are they affected by antituberculosis drugs?
Topics: Acetylglucosamine; Animals; Antitubercular Agents; Chromosome Mapping; Computational Biology; Cysteine; Disaccharides; Enzymes; Glycopeptides; Growth Inhibitors; Humans; Inositol; Oxidoreductases; Polymorphism, Restriction Fragment Length; Pyrazoles; RNA, Antisense; Sulfhydryl Compounds | 2004 |
Targeted mutagenesis of the Mycobacterium smegmatis mca gene, encoding a mycothiol-dependent detoxification protein.
Topics: Amidohydrolases; Anti-Bacterial Agents; Bridged Bicyclo Compounds; Cysteine; Dinitrochlorobenzene; Disaccharides; Enzyme Inhibitors; Ethylmaleimide; Gene Deletion; Genes, Bacterial; Genetic Complementation Test; Glycopeptides; Inositol; Iodoacetamide; Mutagenesis, Insertional; Mycobacterium smegmatis; Mycobacterium tuberculosis; Naphthoquinones; Oxidants; Pyrazoles; Rifamycins; Streptomycin; Sulfhydryl Compounds; Vitamin K 3 | 2004 |
Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic Mycobacteria.
Topics: Alkynes; Amino Acids; Biological Transport; Carbon-Oxygen Lyases; Cell-Free System; Chromatography, High Pressure Liquid; Cloning, Molecular; Cystathionine gamma-Lyase; Cysteine; Disaccharides; DNA Mutational Analysis; Escherichia coli; Genetic Complementation Test; Genome; Genome, Bacterial; Glycine; Glycopeptides; Homoserine; Inositol; Ions; Kinetics; Methionine; Models, Chemical; Mutation; Mycobacterium bovis; Mycobacterium tuberculosis; Plasmids; Protein Structure, Tertiary; Pyrazoles; Sulfhydryl Compounds; Sulfur; Time Factors; Ultracentrifugation; Ultraviolet Rays | 2005 |
A mycothiol synthase mutant of Mycobacterium smegmatis produces novel thiols and has an altered thiol redox status.
Topics: Acetyl Coenzyme A; Acetyltransferases; Acyl Coenzyme A; Benzene Derivatives; Cysteine; Disaccharides; DNA Transposable Elements; Glycopeptides; Hydrogen Peroxide; Inositol; Mutagenesis, Insertional; Mycobacterium smegmatis; Oxidants; Oxidation-Reduction; Pyrazoles; Sulfhydryl Compounds; tert-Butylhydroperoxide | 2005 |
The substrate-induced conformational change of Mycobacterium tuberculosis mycothiol synthase.
Topics: Acetyltransferases; Binding Sites; Coenzyme A; Crystallography, X-Ray; Cysteine; Disaccharides; Glycopeptides; Inositol; Mycobacterium tuberculosis; Protein Binding; Protein Conformation; Pyrazoles; Substrate Specificity; Sulfhydryl Compounds | 2006 |
The gene ncgl2918 encodes a novel maleylpyruvate isomerase that needs mycothiol as cofactor and links mycothiol biosynthesis and gentisate assimilation in Corynebacterium glutamicum.
Topics: Amino Acid Sequence; Bacterial Proteins; Carbon; Chromatography, High Pressure Liquid; cis-trans-Isomerases; Corynebacterium glutamicum; Cysteine; Disaccharides; DNA Primers; Escherichia coli; Gene Deletion; Gene Expression Regulation, Bacterial; Genes, Bacterial; Gentisates; Glycopeptides; Hydroxybenzoates; Inositol; Ions; Kinetics; Mass Spectrometry; Models, Chemical; Molecular Sequence Data; Molecular Weight; Mutation; Phenotype; Pimelic Acids; Plasmids; Pyrazoles; Spectrometry, Mass, Electrospray Ionization; Sulfhydryl Compounds; Time Factors | 2006 |
Identification of genes for mycothiol biosynthesis in Streptomyces coelicolor A3(2).
Topics: Acetylesterase; Acetyltransferases; Bacterial Proteins; Culture Media; Cysteine; Disaccharides; Gene Expression Regulation, Bacterial; Glycopeptides; Informatics; Inositol; Mutation; Pyrazoles; Streptomyces coelicolor; Sulfhydryl Compounds | 2006 |
Conformational analyses of mycothiol, a critical intracellular glycothiol in Mycobacteria.
Topics: Carbohydrate Conformation; Cysteine; Disaccharides; Glycopeptides; Inositol; Intracellular Fluid; Mycobacterium; Pyrazoles; Sulfhydryl Compounds | 2006 |
Purification and characterization of Mycobacterium tuberculosis 1D-myo-inosityl-2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase, MshB, a mycothiol biosynthetic enzyme.
Topics: Amidohydrolases; Bacterial Proteins; Cysteine; Disaccharides; Glycopeptides; Inositol; Metalloproteins; Mycobacterium tuberculosis; Pyrazoles; Recombinant Proteins; Sulfhydryl Compounds | 2006 |
Mycothiol-dependent mycobacterial response to oxidative stress.
Topics: Cysteine; Disaccharides; Glycopeptides; Inositol; Mycobacterium bovis; Mycobacterium smegmatis; Oxidation-Reduction; Oxidative Stress; Pyrazoles; Reactive Oxygen Species; Sulfhydryl Compounds; Water | 2006 |
A coupled spectrophotometric assay for l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase and its application for inhibitor screening.
Topics: Antitubercular Agents; Colorimetry; Cysteine; Disaccharides; Enzyme Inhibitors; Glycopeptides; Inositol; Ligases; Molybdenum; Mycobacterium smegmatis; Mycobacterium tuberculosis; Phosphates; Phosphoric Acids; Pyrazoles; Pyrophosphatases; Rosaniline Dyes; Spectrophotometry; Sulfhydryl Compounds | 2006 |
Foundations of antibiotic resistance in bacterial physiology: the mycobacterial paradigm.
Topics: Anti-Bacterial Agents; Bacterial Proteins; Cell Wall; Cysteine; Disaccharides; Drug Resistance, Multiple, Bacterial; Glycopeptides; Inositol; Membrane Transport Proteins; Models, Biological; Mycobacterium; Mycobacterium tuberculosis; Permeability; Porins; Pyrazoles; Sulfhydryl Compounds; Transcription Factors | 2006 |
Cloning, expression and rapid purification of active recombinant mycothiol ligase as B1 immunoglobulin binding domain of streptococcal protein G, glutathione-S-transferase and maltose binding protein fusion proteins in Mycobacterium smegmatis.
Topics: Bacterial Proteins; Carbohydrate Conformation; Carrier Proteins; Cloning, Molecular; Cysteine; Glutathione Transferase; Glycopeptides; Immunoglobulins; Inositol; Ligases; Maltose-Binding Proteins; Mycobacterium smegmatis; Protein Binding; Recombinant Proteins; Time Factors | 2006 |
Biochemistry of the initial steps of mycothiol biosynthesis.
Topics: Acetylation; Acetylglucosamine; Biochemical Phenomena; Biochemistry; Chromatography, High Pressure Liquid; Cysteine; Disaccharides; Glycopeptides; Glycosyltransferases; Inositol; Inositol Phosphates; Mass Spectrometry; Mycobacterium smegmatis; Uridine Diphosphate | 2006 |
The mshA gene encoding the glycosyltransferase of mycothiol biosynthesis is essential in Mycobacterium tuberculosis Erdman.
Topics: Bacterial Proteins; Cysteine; Gene Dosage; Glycopeptides; Glycosyltransferases; Inositol; Mutagenesis, Site-Directed; Mycobacterium tuberculosis; Transduction, Genetic | 2006 |
Design and synthesis of substrate-mimic inhibitors of mycothiol-S-conjugate amidase from Mycobacterium tuberculosis.
Topics: Amidohydrolases; Chromatography, High Pressure Liquid; Cysteine; Drug Design; Enzyme Inhibitors; Glycopeptides; Glycosylation; Inositol; Mycobacterium tuberculosis; Spectrometry, Fluorescence; Structure-Activity Relationship | 2007 |
Inositol-1-phosphate synthetase mRNA as a new target for antisense inhibition of Mycobacterium tuberculosis.
Topics: Anti-Bacterial Agents; Colony Count, Microbial; Cysteine; Glycopeptides; Hydrogen Peroxide; Inositol; Microbial Sensitivity Tests; Mycobacterium tuberculosis; Myo-Inositol-1-Phosphate Synthase; Oligonucleotides, Antisense; Oxidants; RNA, Messenger; Thionucleotides | 2007 |
Thiols in nitric oxide synthase-containing Nocardia sp. strain NRRL 5646.
Topics: Aldehyde Oxidoreductases; Base Sequence; Chromatography, High Pressure Liquid; Cysteine; Glycopeptides; Inositol; Molecular Sequence Data; Molecular Structure; Nitric Oxide; Nocardia; RNA, Ribosomal, 16S; Sequence Analysis, DNA | 2007 |
Crystal structures and site-directed mutagenesis of a mycothiol-dependent enzyme reveal a novel folding and molecular basis for mycothiol-mediated maleylpyruvate isomerization.
Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Catalytic Domain; cis-trans-Isomerases; Coenzymes; Corynebacterium glutamicum; Crystallography, X-Ray; Cysteine; Glycopeptides; Inositol; Isomerases; Mutation, Missense; Mycobacterium tuberculosis; Pimelic Acids; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship | 2007 |
Synthesis of fused bicyclic thioglycosides of N-acylated glucosamine as analogues of mycothiol.
Topics: Acetylglucosamine; Bridged Bicyclo Compounds; Carbohydrate Conformation; Cysteine; Glucosamine; Glycopeptides; Inositol; Models, Molecular; Molecular Conformation; Thioglycosides | 2007 |
Innate protection of Mycobacterium smegmatis against the antimicrobial activity of nitric oxide is provided by mycothiol.
Topics: Anti-Bacterial Agents; Cysteine; Drug Resistance, Bacterial; Genes, Bacterial; Glycopeptides; Inositol; Mutation; Mycobacterium smegmatis; Nitric Oxide | 2007 |
Mycothiol import by Mycobacterium smegmatis and function as a resource for metabolic precursors and energy production.
Topics: Acetylcysteine; Carbon Radioisotopes; Cysteine; Glycopeptides; Inositol; Inositol Phosphates; Models, Biological; Molecular Structure; Mutation; Mycobacterium smegmatis; Pyruvic Acid | 2007 |
Comparative analysis of mutants in the mycothiol biosynthesis pathway in Mycobacterium smegmatis.
Topics: Acetyltransferases; Cysteine; Glycopeptides; Inositol; Mutation; Mycobacterium smegmatis; NADH, NADPH Oxidoreductases; Signal Transduction | 2007 |
Steady-state and pre-steady-state kinetic analysis of Mycobacterium smegmatis cysteine ligase (MshC).
Topics: Adenosine Triphosphate; Catalysis; Cysteine; Diphosphates; Glucosamine; Glycopeptides; Hydrogen-Ion Concentration; Inositol; Kinetics; Ligases; Models, Chemical; Molecular Structure; Mycobacterium smegmatis | 2007 |
Synthesis of natural product-inspired inhibitors of Mycobacterium tuberculosis mycothiol-associated enzymes: the first inhibitors of GlcNAc-Ins deacetylase.
Topics: Amidohydrolases; Bacterial Proteins; Binding Sites; Cysteine; Furans; Glycopeptides; Inositol; Isoxazoles; Models, Molecular; Mycobacterium tuberculosis; Oxazines; Oxazoles; Protein Binding; Pyrans; Stereoisomerism; Sulfonamides; Thioglycosides | 2007 |
Mycothiol disulfide reductase: solid phase synthesis and evaluation of alternative substrate analogues.
Topics: Binding Sites; Combinatorial Chemistry Techniques; Cysteine; Disulfides; Enzyme Activation; Enzyme Inhibitors; Glycopeptides; Glycosides; Inositol; Kinetics; Molecular Conformation; NADH, NADPH Oxidoreductases; Stereoisomerism; Structure-Activity Relationship; Substrate Specificity | 2008 |
Regulation of mycothiol metabolism by sigma(R) and the thiol redox sensor anti-sigma factor RsrA.
Topics: Actinobacteria; Bacterial Proteins; Cysteine; Gene Expression Regulation, Bacterial; Glycopeptides; Inositol; Sigma Factor; Streptomyces coelicolor; Sulfhydryl Compounds; Transcription Factors | 2008 |
Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor.
Topics: Alkylating Agents; Amidohydrolases; Anti-Bacterial Agents; Bacterial Proteins; Cysteine; Drug Resistance, Bacterial; Gene Expression Regulation, Bacterial; Glycopeptides; Inositol; Mutation; Regulon; Sigma Factor; Streptomyces coelicolor; Transcription Factors | 2008 |
An N-acyl homolog of mycothiol is produced in marine actinomycetes.
Topics: Actinobacteria; Amidohydrolases; Biosynthetic Pathways; Cysteine; Glycopeptides; Inositol; Magnetic Resonance Spectroscopy; Molecular Structure; Oxidation-Reduction; Water Microbiology | 2008 |
Mycothiol biosynthesis is essential for ethionamide susceptibility in Mycobacterium tuberculosis.
Topics: Amino Acid Sequence; Animals; Antitubercular Agents; Bacterial Proteins; Catalase; Corynebacterium glutamicum; Cysteine; Drug Resistance, Bacterial; Ethionamide; Glycopeptides; Glycosyltransferases; Humans; Inositol; Isoniazid; Mice; Mice, Inbred C57BL; Mice, SCID; Microbial Sensitivity Tests; Mixed Function Oxygenases; Molecular Sequence Data; Mycobacterium Infections; Mycobacterium tuberculosis; Sequence Alignment; Sequence Deletion; Tuberculosis, Multidrug-Resistant | 2008 |
Unusual production of glutathione in Actinobacteria.
Topics: Actinobacteria; Amino Acid Sequence; Bacterial Proteins; Cysteine; Glutathione; Glycopeptides; Inositol; Molecular Sequence Data; Sequence Alignment | 2009 |
The 1.6 A crystal structure of Mycobacterium smegmatis MshC: the penultimate enzyme in the mycothiol biosynthetic pathway.
Topics: Bacterial Proteins; Binding Sites; Carbon-Nitrogen Ligases; Conserved Sequence; Crystallization; Crystallography, X-Ray; Cysteine; Glycopeptides; Hydrolysis; Inositol; Mycobacterium smegmatis; Protein Binding; Protein Structure, Secondary; Substrate Specificity; Trypsin | 2008 |
Mycothiol disulfide reductase: a continuous assay for slow time-dependent inhibitors.
Topics: Cysteine; Enzyme Assays; Enzyme Inhibitors; Glycopeptides; Inositol; Kinetics; NADH, NADPH Oxidoreductases; NADP; Recombinant Proteins; Substrate Specificity; Sulfhydryl Compounds; Time Factors | 2009 |
Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange.
Topics: Arsenate Reductases; Arsenates; Arsenites; Biocatalysis; Corynebacterium glutamicum; Cysteine; Disulfides; Electron Transport; Electrons; Genes, Bacterial; Glycopeptides; Inositol; Kinetics; Oxidation-Reduction; Substrate Specificity; Sulfhydryl Compounds | 2009 |
Toward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: an enzyme involved in the biosynthetic pathway of mycothiol.
Topics: Adenosine; Adenosine Triphosphate; Biosynthetic Pathways; Carbon-Nitrogen Ligases; Catalytic Domain; Cysteine; Glycopeptides; Hydrogen-Ion Concentration; Imidazoles; Inositol; Ligases; Molecular Sequence Data; Molecular Structure; Mutagenesis, Site-Directed; Mycobacterium smegmatis; Protein Structure, Tertiary | 2009 |
Dequalinium, a new inhibitor of Mycobacterium tuberculosis mycothiol ligase identified by high-throughput screening.
Topics: Anti-Infective Agents; Bacterial Proteins; Carrier Proteins; Cysteine; Dequalinium; Dose-Response Relationship, Drug; Drug Evaluation, Preclinical; Enzyme Inhibitors; Glycopeptides; Inositol; Kinetics; Ligases; Luminescent Measurements; Maltose-Binding Proteins; Mycobacterium tuberculosis | 2009 |
Conjugates of plumbagin and phenyl-2-amino-1-thioglucoside inhibit MshB, a deacetylase involved in the biosynthesis of mycothiol.
Topics: Acetylcysteine; Amidohydrolases; Bacterial Proteins; Cell Survival; Cysteine; Enzyme Inhibitors; Glycopeptides; Indicators and Reagents; Inositol; Mycobacterium tuberculosis; NADH, NADPH Oxidoreductases; Naphthoquinones; Oxidation-Reduction; Structure-Activity Relationship; Substrate Specificity; Thioglucosides | 2010 |
Intramolecular alpha-glucosaminidation: synthesis of mycothiol.
Topics: Catalysis; Cysteine; Glucosamine; Glycopeptides; Glycosylation; Inositol; Molecular Structure; Mycobacterium tuberculosis; Nuclear Magnetic Resonance, Biomolecular; Stereoisomerism; Thioglycosides | 2010 |
Characterization of the N-acetyl-α-D-glucosaminyl l-malate synthase and deacetylase functions for bacillithiol biosynthesis in Bacillus anthracis .
Topics: Bacillus anthracis; Binding Sites; Borohydrides; Cysteine; Glucosamine; Glycopeptides; Glycosyltransferases; Inositol; Intramolecular Lyases; Molecular Weight; Oxidation-Reduction; Sulfhydryl Compounds; Uridine Diphosphate | 2010 |
Identification and quantification of mycothiol in Actinobacteria by a novel enzymatic method.
Topics: Actinobacteria; Chemistry Techniques, Analytical; cis-trans-Isomerases; Corynebacterium glutamicum; Cysteine; Glycopeptides; Inositol | 2010 |
Organic hydroperoxide resistance protein and ergothioneine compensate for loss of mycothiol in Mycobacterium smegmatis mutants.
Topics: Antitubercular Agents; Bacterial Proteins; Biosynthetic Pathways; Cysteine; DNA Transposable Elements; Drug Resistance, Bacterial; Ergothioneine; Glycopeptides; Hydrogen Peroxide; Inositol; Isoniazid; Microbial Viability; Mutagenesis, Insertional; Mycobacterium smegmatis | 2011 |
Precise null deletion mutations of the mycothiol synthesis genes reveal their role in isoniazid and ethionamide resistance in Mycobacterium smegmatis.
Topics: Antitubercular Agents; Bacterial Proteins; Cysteine; Drug Resistance, Multiple, Bacterial; Ethionamide; Glycopeptides; Inositol; Isoniazid; Mycobacterium smegmatis; Sequence Deletion | 2011 |
The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) change depending on environmental conditions.
Topics: Amidohydrolases; Bacterial Proteins; Coenzymes; Cysteine; Glycopeptides; Inositol; Metals, Heavy; Mycobacterium smegmatis; Mycobacterium tuberculosis | 2011 |
Evaluation of NTF1836 as an inhibitor of the mycothiol biosynthetic enzyme MshC in growing and non-replicating Mycobacterium tuberculosis.
Topics: Animals; Bacterial Proteins; Chlorocebus aethiops; Cysteine; Dibenzothiazepines; Drug Evaluation, Preclinical; Enzyme Inhibitors; Glycopeptides; Inositol; Mycobacterium tuberculosis; Structure-Activity Relationship; Vero Cells | 2011 |
Coresistance to isoniazid and ethionamide maps to mycothiol biosynthetic genes in Mycobacterium bovis.
Topics: Antitubercular Agents; Bacterial Proteins; Carbon-Sulfur Lyases; Cysteine; Drug Resistance, Bacterial; Ethionamide; Glycopeptides; Glycosyltransferases; Inositol; Isoniazid; Mycobacterium bovis | 2011 |
Desymmetrization of 2,4,5,6-tetra-O-benzyl-D-myo-inositol for the synthesis of mycothiol.
Topics: Animals; Benzyl Compounds; Cysteine; Glycopeptides; Inositol; Inositol Phosphates; Molecular Structure; Stereoisomerism | 2011 |
The DinB superfamily includes novel mycothiol, bacillithiol, and glutathione S-transferases.
Topics: Amidohydrolases; Bacterial Proteins; Cloning, Molecular; Cysteine; Enterococcus faecalis; Glucosamine; Glutathione Transferase; Glycopeptides; Inositol; Multigene Family; Mycobacterium smegmatis; Mycobacterium tuberculosis; Phylogeny; Pyrazoles; Sequence Homology, Amino Acid | 2011 |
Thiols screened by the neocarzinostatin protein for preserving or detoxifying its bound enediyne antibiotic.
Topics: Anti-Bacterial Agents; Cysteine; Enediynes; Glutathione; Glycopeptides; Inositol; Molecular Structure; Streptomyces; Sulfhydryl Compounds; Zinostatin | 2012 |
Characterization of BshA, bacillithiol glycosyltransferase from Staphylococcus aureus and Bacillus subtilis.
Topics: Antioxidants; Bacillaceae Infections; Bacillus subtilis; Bacterial Proteins; Cysteine; Enzyme Inhibitors; Glucosamine; Glycopeptides; Inositol; Kinetics; Malates; Models, Molecular; Molecular Targeted Therapy; Molecular Weight; N-Acetylglucosaminyltransferases; Protein Conformation; Recombinant Proteins; Staphylococcal Infections; Staphylococcus aureus; Substrate Specificity; Uridine Diphosphate N-Acetylglucosamine | 2012 |
An enzyme-initiated Smiles rearrangement enables the development of an assay of MshB, the GlcNAc-Ins deacetylase of mycothiol biosynthesis.
Topics: Amidohydrolases; Bacterial Proteins; Biocatalysis; Catalytic Domain; Cysteine; Glycopeptides; Inositol; Models, Molecular; Mycobacterium tuberculosis; Substrate Specificity | 2012 |
Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria.
Topics: Cysteine; Disulfides; Gene Deletion; Glycopeptides; Inositol; Magnetic Resonance Spectroscopy; Models, Molecular; Mycobacterium smegmatis; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Protein Conformation | 2012 |
Nickel-catalyzed α-glycosylation of C(1)-hydroxyl D-myo-inositol: a formal synthesis of mycothiol.
Topics: Catalysis; Cysteine; Glycopeptides; Glycosylation; Inositol; Nickel; Streptomyces | 2013 |
Bacterial mechanisms of reversible protein S-thiolation: structural and mechanistic insights into mycoredoxins.
Topics: Cysteine; Glycopeptides; Inositol; Mycobacterium smegmatis; Oxidative Stress; Oxidoreductases | 2012 |
NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase.
Topics: Amino Acid Sequence; Antitubercular Agents; Catalytic Domain; Cloning, Molecular; Corynebacterium glutamicum; Crystallography, X-Ray; Cysteine; Dimerization; Electrons; Escherichia coli Proteins; Glycopeptides; Hydrogen-Ion Concentration; Inositol; Kinetics; Molecular Conformation; Molecular Sequence Data; Mycobacterium tuberculosis; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Ribonucleotides; Scattering, Radiation; Sequence Homology, Amino Acid; Surface Properties; Thioredoxin-Disulfide Reductase; Thioredoxins; X-Rays | 2013 |
Conformational preferences of plumbagin with phenyl-1-thioglucoside conjugates in solution and bound to MshB determined by aromatic association.
Topics: Amidohydrolases; Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Cysteine; Enzyme Inhibitors; Glycopeptides; Inositol; Kinetics; Ligands; Molecular Conformation; Molecular Docking Simulation; Mycobacterium tuberculosis; Naphthoquinones; Protein Structure, Secondary; Superoxides; Thermodynamics; Thioglucosides | 2013 |
Physiological roles of mycothiol in detoxification and tolerance to multiple poisonous chemicals in Corynebacterium glutamicum.
Topics: Corynebacterium glutamicum; Cysteine; Ethanol; Glycopeptides; Inactivation, Metabolic; Industrial Microbiology; Inositol; Metals, Heavy; Naphthalenes; Oxidation-Reduction; Resorcinols | 2013 |
Ergothioneine is a secreted antioxidant in Mycobacterium smegmatis.
Topics: Antioxidants; Bacterial Proteins; Culture Media; Cysteine; Drug Resistance, Bacterial; Ergothioneine; Glycopeptides; Inositol; Microbial Sensitivity Tests; Mutation; Mycobacterium smegmatis; Oxidative Stress | 2013 |
Mycobacterium tuberculosis is extraordinarily sensitive to killing by a vitamin C-induced Fenton reaction.
Topics: Antitubercular Agents; Ascorbic Acid; Cysteine; DNA Damage; Drug Resistance, Bacterial; Glycopeptides; Hydrogen Peroxide; Inositol; Iron; Lipids; Microbial Sensitivity Tests; Microbial Viability; Models, Biological; Mycobacterium tuberculosis; Oxidants; Reactive Oxygen Species; Sterilization; Transcription, Genetic | 2013 |
Protein S-mycothiolation functions as redox-switch and thiol protection mechanism in Corynebacterium glutamicum under hypochlorite stress.
Topics: Bacterial Proteins; Corynebacterium glutamicum; Cysteine; Disulfides; Glucose; Glycogen; Glycopeptides; Inositol; Oxidants; Oxidation-Reduction; Peroxidases; Protein Processing, Post-Translational; Proteome; Sodium Hypochlorite; Stress, Physiological; Transcriptome | 2014 |
Automated docking studies provide insights into molecular determinants of ligand recognition by N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB).
Topics: Amidohydrolases; Bacterial Proteins; Crystallography, X-Ray; Cysteine; Glycopeptides; Hydrogen Bonding; Inositol; Ligands; Molecular Docking Simulation; Mycobacterium tuberculosis; Protein Structure, Secondary; Substrate Specificity; Thermodynamics | 2014 |
Mycothiol/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis.
Topics: Bacterial Proteins; Biocatalysis; Cysteine; Disulfides; Glycopeptides; Hydrogen Peroxide; Hydrogen-Ion Concentration; Inositol; Kinetics; Models, Biological; Mycobacterium tuberculosis; NADP; Oxidation-Reduction; Peroxiredoxins | 2014 |
Reengineering redox sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection.
Topics: Cell Line, Tumor; Cysteine; Glycopeptides; Green Fluorescent Proteins; Humans; Inositol; Macrophages; Mycobacterium tuberculosis; Oxidation-Reduction; Protein Engineering; Tuberculosis | 2014 |
Enhancing Corynebacterium glutamicum robustness by over-expressing a gene, mshA, for mycothiol glycosyltransferase.
Topics: Corynebacterium glutamicum; Cysteine; Gene Expression; Glycopeptides; Glycosyltransferases; Inositol; Microbial Viability; Stress, Physiological | 2014 |
Metabolic coupling of two small-molecule thiols programs the biosynthesis of lincomycin A.
Topics: Anti-Bacterial Agents; Biological Products; Biosynthetic Pathways; Biotransformation; Cysteine; Ergothioneine; Glycopeptides; Glycosylation; Inositol; Lincomycin; Lincosamides; Molecular Sequence Data; Streptomyces | 2015 |
Biochemistry: Elusive source of sulfur unravelled.
Topics: Anti-Bacterial Agents; Cysteine; Ergothioneine; Glycopeptides; Inositol; Lincomycin; Streptomyces | 2015 |
Ergothioneine protects Streptomyces coelicolor A3(2) from oxidative stresses.
Topics: Cysteine; Ergothioneine; Glutamate-Cysteine Ligase; Glycopeptides; Hydrogen Peroxide; Inositol; Oxidative Stress; Streptomyces coelicolor | 2015 |
Lincosamide synthetase--a unique condensation system combining elements of nonribosomal peptide synthetase and mycothiol metabolism.
Topics: Cysteine; Glycopeptides; Inositol; Lincomycin; Lincosamides; Peptide Synthases | 2015 |
Corynebacterium diphtheriae methionine sulfoxide reductase a exploits a unique mycothiol redox relay mechanism.
Topics: Amino Acid Sequence; Catalytic Domain; Corynebacterium diphtheriae; Cysteine; Disulfides; Glycopeptides; Inositol; Methionine; Methionine Sulfoxide Reductases; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases; Thioredoxin-Disulfide Reductase; Thioredoxins | 2015 |
The Corynebacterium glutamicum mycothiol peroxidase is a reactive oxygen species-scavenging enzyme that shows promiscuity in thiol redox control.
Topics: Bacterial Proteins; Corynebacterium glutamicum; Cysteine; Disulfides; Glycopeptides; Hydrogen Peroxide; Inositol; Kinetics; Molecular Sequence Data; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Peroxidases; Reactive Oxygen Species; Sequence Analysis, Protein; Sulfhydryl Compounds; Thioredoxins | 2015 |
Synthesis of mycothiol conjugate analogues and evaluation of their antimycobacterial activity.
Topics: Antitubercular Agents; Cysteine; Glycopeptides; Inositol; Microbial Sensitivity Tests; Mycobacterium tuberculosis | 2015 |
Biosynthesis of mercapturic acid derivative of the labdane-type diterpene, cyslabdan that potentiates imipenem activity against methicillin-resistant Staphylococcus aureus: cyslabdan is generated by mycothiol-mediated xenobiotic detoxification.
Topics: Acetylcysteine; Amidohydrolases; Biosynthetic Pathways; Cysteine; Diterpenes; Glycopeptides; Imipenem; Inactivation, Metabolic; Inositol; Methicillin-Resistant Staphylococcus aureus; Multigene Family; Mycelium; Organophosphates; Streptomyces; Xenobiotics | 2016 |
The versatile low-molecular-weight thiols: Beyond cell protection.
Topics: Biological Products; Carbohydrates; Cysteine; Ergothioneine; Glycopeptides; Glycosylation; Inositol; Molecular Weight; Oxidation-Reduction; Sulfhydryl Compounds | 2015 |
Mycobacterium tuberculosis WhiB3 Responds to Vacuolar pH-induced Changes in Mycothiol Redox Potential to Modulate Phagosomal Maturation and Virulence.
Topics: Animals; Bacterial Proteins; Cell Line, Tumor; Cysteine; Glycopeptides; Humans; Hydrogen-Ion Concentration; Immunity, Innate; Inositol; Mice; Mycobacterium tuberculosis; Oxidation-Reduction; Phagosomes; Vacuoles | 2016 |
Ergothioneine Maintains Redox and Bioenergetic Homeostasis Essential for Drug Susceptibility and Virulence of Mycobacterium tuberculosis.
Topics: Animals; Antioxidants; Antitubercular Agents; Bacterial Proteins; Carbon; Cell Line; Chromatography, High Pressure Liquid; Cysteine; Disease Susceptibility; Energy Metabolism; Ergothioneine; Glycopeptides; Inositol; Lung; Macrophages; Mice; Mycobacterium tuberculosis; Oxidation-Reduction; Principal Component Analysis; Tandem Mass Spectrometry; Transcription Factors; Virulence | 2016 |
Persistent Mycobacterium bovis-BCG is resistant to glutathione induced reductive stress killing.
Topics: Adenosine Triphosphate; Anti-Bacterial Agents; Cysteine; Cytosol; Glutathione; Glycopeptides; Inositol; Microbial Viability; Mycobacterium bovis; NAD; Oxidation-Reduction | 2016 |
Mycothiol peroxidase MPx protects Corynebacterium glutamicum against acid stress by scavenging ROS.
Topics: Acids; Corynebacterium glutamicum; Cysteine; Glycopeptides; Inositol; Peroxidases; Protein Carbonylation; Reactive Oxygen Species; Sigma Factor | 2016 |
Mycothiol protects Corynebacterium glutamicum against acid stress via maintaining intracellular pH homeostasis, scavenging ROS, and S-mycothiolating MetE.
Topics: 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase; Bacterial Proteins; Corynebacterium glutamicum; Cysteine; Glycopeptides; Homeostasis; Hydrogen-Ion Concentration; Inositol; Methionine; Oxidoreductases; Reactive Oxygen Species; Recombinant Proteins; Stress, Physiological | 2016 |
S-nitrosomycothiol reductase and mycothiol are required for survival under aldehyde stress and biofilm formation in Mycobacterium smegmatis.
Topics: Aldehyde Oxidoreductases; Aldehydes; Biofilms; Cysteine; Cysteine Synthase; Glycopeptides; Inositol; Mycobacterium Infections, Nontuberculous; Mycobacterium smegmatis; S-Nitrosothiols | 2016 |
Thiol Redox and pKa Properties of Mycothiol, the Predominant Low-Molecular-Weight Thiol Cofactor in the Actinomycetes.
Topics: Actinobacteria; Coenzymes; Cysteine; Glycopeptides; Hydrogen-Ion Concentration; Inositol; Molecular Conformation; Molecular Weight; Oxidation-Reduction; Sulfhydryl Compounds | 2016 |
Overexpression of Mycothiol Disulfide Reductase Enhances Corynebacterium glutamicum Robustness by Modulating Cellular Redox Homeostasis and Antioxidant Proteins under Oxidative Stress.
Topics: Bacterial Proteins; Corynebacterium glutamicum; Cysteine; Glycopeptides; Homeostasis; Inositol; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxidative Stress | 2016 |
Redox chemistry of Mycobacterium tuberculosis alkylhydroperoxide reductase E (AhpE): Structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of AhpE via mycothiol.
Topics: Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Cysteine; Glycopeptides; Hydrogen Bonding; Inositol; Metabolic Networks and Pathways; Molecular Docking Simulation; Mycobacterium tuberculosis; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Peroxiredoxins; Protein Binding; Protein Conformation, alpha-Helical; Protein Structure, Quaternary; Scattering, Small Angle; Solutions; Thioredoxins | 2016 |
Theoretical Insights into the Reaction and Inhibition Mechanism of Metal-Independent Retaining Glycosyltransferase Responsible for Mycothiol Biosynthesis.
Topics: Amidohydrolases; Bacterial Proteins; Biocatalysis; Cysteine; Glycopeptides; Glycosyltransferases; Inositol; Metals; Mycobacterium tuberculosis; Quantum Theory | 2017 |
Proteome analysis reveals differential expression of proteins involved in triacylglycerol accumulation by Rhodococcus jostii RHA1 after addition of methyl viologen.
Topics: Acyl Coenzyme A; Adaptation, Physiological; Catalase; Cysteine; Fatty Acids; Glycopeptides; Inositol; NADP; Nitrogen; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Paraquat; Peroxiredoxins; Proteome; Rhodococcus; Superoxide Dismutase; Triglycerides | 2017 |
Biochemical studies of inositol N-acetylglucosaminyltransferase involved in mycothiol biosynthesis in Corynebacterium diphtheria.
Topics: Catalytic Domain; Corynebacterium diphtheriae; Cysteine; Glycopeptides; Inositol; Kinetics; Models, Molecular; Mutagenesis; N-Acetylglucosaminyltransferases; Structure-Activity Relationship; Substrate Specificity | 2017 |
Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress.
Topics: Bacterial Proteins; Cysteine; Gene Expression Profiling; Glycopeptides; Hypochlorous Acid; Inositol; Metabolic Networks and Pathways; Metabolome; Mycobacterium smegmatis; Oxidants; Oxidation-Reduction; Protein Processing, Post-Translational; Proteome; Stress, Physiological | 2017 |
The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress.
Topics: Bacterial Proteins; Catalytic Domain; Corynebacterium diphtheriae; Cysteine; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycopeptides; Hydrogen Peroxide; Inositol; Oxidation-Reduction; Oxidative Stress; Protein Processing, Post-Translational; Proteomics; Sodium Hypochlorite | 2017 |
Mycothiol acetyltransferase (Rv0819) of Mycobacterium tuberculosis is a potential biomarker for direct diagnosis of tuberculosis using patient serum specimens.
Topics: Acetyltransferases; Adult; Aged; Antigens, Bacterial; Biomarkers; Cloning, Molecular; Cysteine; Early Diagnosis; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Female; Glycopeptides; Humans; Inositol; Male; Middle Aged; Mycobacterium tuberculosis; Sensitivity and Specificity; Tuberculosis, Pulmonary; Young Adult | 2017 |
Gamma-glutamylcysteine protects ergothioneine-deficient Mycobacterium tuberculosis mutants against oxidative and nitrosative stress.
Topics: Biosynthetic Pathways; Cysteine; Dipeptides; Ergothioneine; Gene Deletion; Glycopeptides; Humans; Inositol; Mycobacterium tuberculosis; Nitrosative Stress; Oxidative Stress; Tuberculosis | 2018 |
Synthesis of substrate analogues as potential inhibitors for Mycobacterium tuberculosis enzyme MshC.
Topics: Bacterial Proteins; Cysteine; Enzyme Inhibitors; Glycopeptides; Glycosylation; Inositol; Mycobacterium tuberculosis; Stereoisomerism | 2017 |
Alternative Thiol-Based Redox Systems.
Topics: Bacteria; Cysteine; Ergothioneine; Glucosamine; Glutathione; Glycopeptides; Homeostasis; Inositol; Oxidation-Reduction; Oxidative Stress; Sulfhydryl Compounds; Thioredoxins | 2018 |
Substrate-induced structural alterations of Mycobacterial mycothione reductase and critical residues involved.
Topics: Cysteine; Glycopeptides; Inositol; Models, Molecular; Mutation; Mycobacterium tuberculosis; NADP; Oxidation-Reduction; Oxidoreductases; Protein Binding; Protein Multimerization; Protein Structure, Quaternary | 2018 |
Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis.
Topics: Animals; Bacterial Proteins; Binding Sites; Cysteine; Disease Models, Animal; Enzyme Activation; Female; Glycopeptides; Inositol; Mice; Models, Molecular; Mutation; Mycobacterium tuberculosis; Nitroreductases; Oxidation-Reduction; Oxidative Stress; Phylogeny; Protein Binding; Protein Conformation; Structure-Activity Relationship; Tuberculosis | 2018 |
The functional interplay of low molecular weight thiols in Mycobacterium tuberculosis.
Topics: Animals; Cysteine; Dipeptides; Ergothioneine; Glycopeptides; Humans; Inositol; Mice; Molecular Weight; Mycobacterium tuberculosis; Oxidative Stress; Reactive Nitrogen Species; Reactive Oxygen Species; Sulfhydryl Compounds; Tuberculosis | 2018 |
Generation and characterization of thiol-deficient Mycobacterium tuberculosis mutants.
Topics: Bacterial Proteins; Cysteine; Dipeptides; Ergothioneine; Glycopeptides; Inositol; Mutation; Mycobacterium tuberculosis; Oxidative Stress; Sulfhydryl Compounds | 2018 |
Myo-inositol-1-phosphate synthase (Ino-1) functions as a protection mechanism in Corynebacterium glutamicum under oxidative stress.
Topics: Aerobiosis; Corynebacterium glutamicum; Cysteine; Gene Deletion; Glycopeptides; Inositol; Microbial Viability; Myo-Inositol-1-Phosphate Synthase; Oxidative Stress; Protein Carbonylation; Reactive Oxygen Species | 2019 |
Characterization and engineering control of the effects of reactive oxygen species on the conversion of sterols to steroid synthons in Mycobacterium neoaurum.
Topics: Cysteine; Ergothioneine; Glycopeptides; Inositol; Metabolic Engineering; Mycobacteriaceae; Reactive Oxygen Species; Sterols | 2019 |
Characterization of Xi-class mycothiol S-transferase from Corynebacterium glutamicum and its protective effects in oxidative stress.
Topics: Bacterial Proteins; Corynebacterium glutamicum; Cysteine; Glutathione Transferase; Glycopeptides; Inositol; Oxidation-Reduction; Oxidative Stress | 2019 |
Methionine sulfoxide reductase B from
Topics: Biocatalysis; Catalytic Domain; Conserved Sequence; Corynebacterium diphtheriae; Cysteine; Disulfides; Glycopeptides; Inositol; Magnetic Resonance Spectroscopy; Methionine Sulfoxide Reductases; Models, Molecular; Oxidation-Reduction; Safrole; Substrate Specificity; Sulfenic Acids; Thioredoxin-Disulfide Reductase; Thioredoxins; Zinc | 2020 |
Glutathione: A powerful but rare cofactor among Actinobacteria.
Topics: Actinobacteria; Bacterial Proteins; Butadienes; Cysteine; Epoxy Compounds; Glutathione; Glutathione Reductase; Glutathione Transferase; Glycopeptides; Hemiterpenes; Inositol; Metabolic Networks and Pathways; Oxidation-Reduction | 2020 |
Molecular mechanisms of Mycoredoxin-1 in resistance to oxidative stress in Corynebacterium glutamicum.
Topics: Amino Acid Sequence; Bacterial Proteins; Corynebacterium glutamicum; Cysteine; Disulfides; Fungal Proteins; Genes, Fungal; Glycopeptides; Inositol; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Sigma Factor; Thioredoxins | 2021 |
Topics: Anti-Bacterial Agents; Cells, Cultured; Cysteine; Glycopeptides; Humans; Hypochlorous Acid; Immune Evasion; Immunity, Innate; Inositol; Mycobacterium Infections, Nontuberculous; Mycobacterium smegmatis; Neutrophils; Phagocytosis; Phagosomes | 2021 |
Biodesulfurization Induces Reprogramming of Sulfur Metabolism in Rhodococcus qingshengii IGTS8: Proteomics and Untargeted Metabolomics.
Topics: Biochemical Phenomena; Cysteine; Glycopeptides; Inositol; Metabolomics; Multigene Family; Proteomics; Rhodococcus; Sulfur; Thiophenes | 2021 |
Involvement of a mycothiol-dependent reductase NCgl0018 in oxidative stress response of Corynebacterium glutamicum.
Topics: Bacterial Proteins; Corynebacterium glutamicum; Cysteine; Disulfides; Glycopeptides; Humans; Inositol; Oxidation-Reduction; Oxidative Stress; Oxidoreductases | 2021 |
Mycothiol Peroxidase Activity as a Part of the Self-Resistance Mechanisms against the Antitumor Antibiotic Cosmomycin D.
Topics: Anthracyclines; Anti-Bacterial Agents; Antioxidants; ATP-Binding Cassette Transporters; Cysteine; Glycopeptides; Inositol; Oxidoreductases; Peroxidase; Peroxidases; Streptomyces | 2022 |
Mycothiol maintains the homeostasis and signalling of nitric oxide in Streptomyces coelicolor A3(2) M145.
Topics: Anthraquinones; Anti-Bacterial Agents; Bacterial Proteins; Cysteine; Gene Expression Regulation, Bacterial; Homeostasis; Nitric Oxide; Streptomyces coelicolor | 2023 |