tryptophan has been researched along with 3,3-dimethylallyl pyrophosphate in 12 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 4 (33.33) | 29.6817 |
2010's | 6 (50.00) | 24.3611 |
2020's | 2 (16.67) | 2.80 |
Authors | Studies |
---|---|
Gray, CR; Sanz-Cervera, JF; Silks, LA; Williams, RM | 1 |
Grundmann, A; Li, SM; Ruan, HL; Westrich, L; Yin, WB | 1 |
Kremer, A; Li, SM; Westrich, L | 1 |
Heide, L; Li, SM; Metzger, U; Schall, C; Stec, E; Stehle, T; Unsöld, I; Zocher, G | 1 |
Hamacher, A; Kassack, MU; Li, SM; Ludwig, L; Wollinsky, B; Yu, X | 1 |
Moore, BS; Qian, Q; Schultz, AW; Tanner, ME | 1 |
Poulter, CD; Rudolf, JD | 1 |
Li, SM; Winkelblech, J | 1 |
Cheng, JZ; Jakubczyk, D; O'Connor, SE | 1 |
Fan, A; Li, SM; Stec, E; Stehle, T; Zocher, G | 1 |
Hino, T; Mizutani, K; Nagano, S; Nishimura, D; Sato, Y; Shiozaki-Sato, Y; Suemune, H; Takagi, H; Takahashi, S | 1 |
Christianson, DW; Eaton, SA; Ronnebaum, TA; Roose, BW | 1 |
1 review(s) available for tryptophan and 3,3-dimethylallyl pyrophosphate
Article | Year |
---|---|
Biosynthesis of the ergot alkaloids.
Topics: Biosynthetic Pathways; Ergot Alkaloids; Fungi; Hemiterpenes; Humans; Molecular Structure; Organophosphorus Compounds; Tryptophan | 2014 |
11 other study(ies) available for tryptophan and 3,3-dimethylallyl pyrophosphate
Article | Year |
---|---|
Studies on the biosynthesis of asperparaline A: origin of the spirosuccinimde ring system.
Topics: Alkaloids; Aspergillus; Carbon Isotopes; Hemiterpenes; Isoleucine; Nuclear Magnetic Resonance, Biomolecular; Organophosphorus Compounds; Piperazines; Spectrometry, Mass, Electrospray Ionization; Spiro Compounds; Succinimides; Tryptophan | 2003 |
CdpNPT, an N-prenyltransferase from Aspergillus fumigatus: overproduction, purification and biochemical characterisation.
Topics: Aspergillus fumigatus; Carbon; Chromatography, High Pressure Liquid; Cloning, Molecular; Dimethylallyltranstransferase; Diphosphates; Diterpenes; Escherichia coli; Hemiterpenes; Kinetics; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Chemical; Molecular Sequence Data; Organophosphorus Compounds; Substrate Specificity; Tryptophan | 2007 |
A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization.
Topics: Alkyl and Aryl Transferases; Aspergillus fumigatus; Cloning, Molecular; Coenzymes; Diphosphates; Diterpenes; DNA, Fungal; Escherichia coli; Gene Expression; Hemiterpenes; Magnetic Resonance Spectroscopy; Mass Spectrometry; Metals; Molecular Sequence Data; Multigene Family; Organophosphorus Compounds; Prenylation; Recombinant Proteins; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Substrate Specificity; Tryptophan | 2007 |
The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.
Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Aspergillus fumigatus; Bacteria; Catalysis; Catalytic Domain; Crystallography, X-Ray; Dimethylallyltranstransferase; Fungal Proteins; Fungi; Hemiterpenes; Magnesium; Models, Chemical; Models, Molecular; Molecular Sequence Data; Molecular Structure; Organophosphorus Compounds; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Substrate Specificity; Terpenes; Tryptophan | 2009 |
Prenylation at the indole ring leads to a significant increase of cytotoxicity of tryptophan-containing cyclic dipeptides.
Topics: Alanine; Biocatalysis; Cell Line, Tumor; Cell Survival; Chromatography, High Pressure Liquid; Dimethylallyltranstransferase; Dipeptides; Fungal Proteins; Hemiterpenes; Humans; Indoles; Inhibitory Concentration 50; Magnetic Resonance Spectroscopy; Organophosphorus Compounds; Peptides, Cyclic; Prenylation; Proline; Recombinant Proteins; Stereoisomerism; Structure-Activity Relationship; Substrate Specificity; Tryptophan | 2012 |
Mechanistic studies on CymD: a tryptophan reverse N-prenyltransferase.
Topics: Actinobacteria; Dimethylallyltranstransferase; Halogenation; Hemiterpenes; Indoles; Kinetics; Organophosphorus Compounds; Prenylation; Protons; Tryptophan | 2012 |
Tyrosine O-prenyltransferase SirD catalyzes S-, C-, and N-prenylations on tyrosine and tryptophan derivatives.
Topics: Dimethylallyltranstransferase; Escherichia coli; Fungal Proteins; Gene Expression; Hemiterpenes; Kinetics; Organophosphorus Compounds; Phenylalanine; Piperazines; Prenylation; Recombinant Proteins; Saccharomycetales; Substrate Specificity; Sulfhydryl Compounds; Tryptophan; Tyrosine | 2013 |
Biochemical investigations of two 6-DMATS enzymes from Streptomyces reveal new features of L-tryptophan prenyltransferases.
Topics: Base Sequence; Chromatography, High Pressure Liquid; Cloning, Molecular; Dimethylallyltranstransferase; Hemiterpenes; Kinetics; Molecular Sequence Data; Naphthols; Organophosphorus Compounds; Polyisoprenyl Phosphates; Prenylation; Recombinant Fusion Proteins; Sesquiterpenes; Streptomyces; Tryptophan | 2014 |
Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme.
Topics: Alkyl and Aryl Transferases; Aspergillus fumigatus; Catalysis; Chromatography, High Pressure Liquid; Fungal Proteins; Hemiterpenes; Indoles; Magnetic Resonance Spectroscopy; Models, Molecular; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Organophosphorus Compounds; Plasmids; Prenylation; Protein Engineering; Tryptophan; Tryptophan Synthase; Tyrosine | 2015 |
Crystal structures of a 6-dimethylallyltryptophan synthase, IptA: Insights into substrate tolerance and enhancement of prenyltransferase activity.
Topics: Alkyl and Aryl Transferases; Hemiterpenes; Indoles; Organophosphorus Compounds; Prenylation; Streptomyces; Substrate Specificity; Tryptophan | 2022 |
Structural Basis of Substrate Promiscuity and Catalysis by the Reverse Prenyltransferase
Topics: Biological Products; Catalysis; Dimethylallyltranstransferase; Fusarium; Hemiterpenes; Indoles; Neoprene; Nitrogen; Organophosphorus Compounds; Prenylation; Substrate Specificity; Tryptophan; Tryptophan Synthase | 2022 |