phenylglyoxylic acid has been researched along with thiamine pyrophosphate in 6 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (50.00) | 29.6817 |
| 2010's | 3 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Hasson, MS; Jordan, F; Kenyon, GL; McLeish, MJ; Polovnikova, L; Sergienko, EA; Wang, J | 1 |
| Golbik, R; Hübner, G; König, S; Schütz, A; Tittmann, K | 1 |
| Chakraborty, S; Jordan, F; Kenyon, GL; McLeish, MJ; Nemeria, N; Yep, A | 1 |
| Andrews, FH; McLeish, MJ | 1 |
| Andrews, FH; Horton, JD; Kneen, MM; Logsdon, MG; Malik, AM; McLeish, MJ; Rogers, MP; Shin, D; Suh, SW; Yoon, HJ | 1 |
| Bielecki, M; Howe, GW; Kluger, R | 1 |
1 review(s) available for phenylglyoxylic acid and thiamine pyrophosphate
| Article | Year |
|---|---|
Substrate specificity in thiamin diphosphate-dependent decarboxylases.
Topics: Acyl Coenzyme A; Bacteria; Carboxy-Lyases; Catalytic Domain; Glyoxylates; Mandelic Acids; Mutagenesis, Site-Directed; Pyruvic Acid; Saccharomyces cerevisiae; Substrate Specificity; Thiamine Pyrophosphate | 2012 |
5 other study(ies) available for phenylglyoxylic acid and thiamine pyrophosphate
| Article | Year |
|---|---|
Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase.
Topics: Alanine; Amino Acid Substitution; Binding Sites; Carboxy-Lyases; Glyoxylates; Histidine; Indicators and Reagents; Kinetics; Mandelic Acids; Nitrobenzoates; Spectrophotometry; Substrate Specificity; Thiamine Pyrophosphate | 2000 |
Intermediates and transition states in thiamin diphosphate-dependent decarboxylases. A kinetic and NMR study on wild-type indolepyruvate decarboxylase and variants using indolepyruvate, benzoylformate, and pyruvate as substrates.
Topics: Amino Acid Substitution; Base Sequence; Carboxy-Lyases; Catalytic Domain; DNA, Bacterial; Genetic Variation; Glyoxylates; Kinetics; Mandelic Acids; Models, Molecular; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Pseudomonas putida; Pyruvates; Substrate Specificity; Thiamine Pyrophosphate; Zymomonas | 2005 |
Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects.
Topics: Acrolein; Aldehyde-Lyases; Benzaldehydes; Benzoin; Butyrates; Circular Dichroism; Deuterium Exchange Measurement; Glyoxylates; Kinetics; Mandelic Acids; Models, Chemical; Phenylpyruvic Acids; Pseudomonas fluorescens; Pyridines; Thiamine Pyrophosphate | 2008 |
The kinetic characterization and X-ray structure of a putative benzoylformate decarboxylase from M. smegmatis highlights the difficulties in the functional annotation of ThDP-dependent enzymes.
Topics: Bacterial Proteins; Carboxy-Lyases; Catalytic Domain; Crystallography, X-Ray; Glyoxylates; Kinetics; Mandelic Acids; Mycobacterium smegmatis; Thiamine Pyrophosphate | 2015 |
Competing Protonation and Halide Elimination as a Probe of the Character of Thiamin-Derived Reactive Intermediates.
Topics: Biocatalysis; Carboxy-Lyases; Decarboxylation; Glyoxylates; Mandelic Acids; Thiamine Pyrophosphate | 2019 |