Page last updated: 2024-08-17

aspartic acid and fosfomycin

aspartic acid has been researched along with fosfomycin in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (14.29)18.2507
2000's3 (42.86)29.6817
2010's2 (28.57)24.3611
2020's1 (14.29)2.80

Authors

AuthorsStudies
Duncan, K; Kempsell, KE; Kim, DH; Lane, WS; Lees, WJ; Walsh, CT1
Eschenburg, S; Schönbrunn, E1
Amrhein, N; Etezady-Esfarjani, T; Macheroux, P; Samland, AK1
Abdul-Latif, FA; Delachaume, C; Eschenburg, S; Fassy, F; Priestman, MA; Schönbrunn, E1
Endo, K; Noguchi, K; Ohsawa, K; Ohtaki, A; Sasaki, Y; Takenoya, M; Yajima, S; Yohda, M1
Attia, M; Berti, PJ; Gilpin, ME; Jiang, S; Ting, YL1
Guo, Y; Han, R; Hu, F; Hu, Z; Li, D; Wang, C; Xin, L; Xu, X1

Other Studies

7 other study(ies) available for aspartic acid and fosfomycin

ArticleYear
Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin.
    Biochemistry, 1996, Apr-16, Volume: 35, Issue:15

    Topics: Alkyl and Aryl Transferases; Anti-Bacterial Agents; Aspartic Acid; Catalysis; Cell Wall; Cysteine; Drug Resistance, Microbial; Escherichia coli; Fosfomycin; Kinetics; Mutagenesis, Site-Directed; Thermodynamics; Transferases

1996
Comparative X-ray analysis of the un-liganded fosfomycin-target murA.
    Proteins, 2000, Aug-01, Volume: 40, Issue:2

    Topics: Alkyl and Aryl Transferases; Aspartic Acid; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Enterobacter cloacae; Fosfomycin; Ligands; Models, Molecular; Phosphates; Protein Conformation; Solvents; Water

2000
Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae.
    Biochemistry, 2001, Feb-13, Volume: 40, Issue:6

    Topics: Alkyl and Aryl Transferases; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Cysteine; Enterobacter cloacae; Enzyme Inhibitors; Fosfomycin; Mutagenesis, Site-Directed; Phosphates; Phosphoenolpyruvate; Recombinant Proteins; Uridine Diphosphate N-Acetylglucosamine

2001
A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA).
    The Journal of biological chemistry, 2005, Apr-08, Volume: 280, Issue:14

    Topics: Alkyl and Aryl Transferases; Anti-Bacterial Agents; Aspartic Acid; Bacterial Proteins; Crystallography, X-Ray; Drug Resistance, Microbial; Enterobacter cloacae; Enzyme Inhibitors; Fosfomycin; Macromolecular Substances; Models, Molecular; Molecular Structure; Naphthalenesulfonates; Protein Structure, Tertiary

2005
Crystal structure of 1-deoxy-d-xylulose 5-phosphate reductoisomerase from the hyperthermophile Thermotoga maritima for insights into the coordination of conformational changes and an inhibitor binding.
    Journal of structural biology, 2010, Volume: 170, Issue:3

    Topics: Aldose-Ketose Isomerases; Aspartic Acid; Base Sequence; Catalytic Domain; Crystallography, X-Ray; DNA Primers; DNA, Bacterial; Enzyme Stability; Fosfomycin; Kinetics; Models, Molecular; Multienzyme Complexes; Oxidoreductases; Protein Conformation; Recombinant Proteins; Static Electricity; Thermotoga maritima

2010
Lyme disease enolpyruvyl-UDP-GlcNAc synthase: fosfomycin-resistant MurA from Borrelia burgdorferi, a fosfomycin-sensitive mutant, and the catalytic role of the active site Asp.
    Biochemistry, 2011, Mar-29, Volume: 50, Issue:12

    Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Amino Acid Substitution; Aspartic Acid; Biocatalysis; Borrelia burgdorferi; Catalytic Domain; Codon, Initiator; Drug Resistance, Bacterial; Fosfomycin; Hydrogen-Ion Concentration; Kinetics; Lyme Disease; Molecular Sequence Data; Mutation; Salts; Temperature

2011
Asp50Glu mutation in MurA results in fosfomycin resistance in Enterococcus faecium.
    Journal of global antimicrobial resistance, 2022, Volume: 30

    Topics: Alkyl and Aryl Transferases; Amino Acid Substitution; Anti-Bacterial Agents; Aspartic Acid; Bacterial Proteins; Drug Resistance, Bacterial; Enterococcus faecium; Fosfomycin; Glutamic Acid; Mutation

2022