4-hydroxyphenylacetic acid has been researched along with flavin mononucleotide in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ballou, DP; Chaiyen, P; Entsch, B; Sucharitakul, J | 1 |
| Ballou, DP; Chaiyen, P; Entsch, B; Phongsak, T; Sucharitakul, J; Svasti, J | 1 |
| Chaiyen, P; Chosrowjan, H; Mataga, N; Phongsak, T; Sucharitakul, J; Tanaka, F; Taniguchi, S | 1 |
| Chaiyen, P; Ruangchan, N; Sucharitakul, J; Tongsook, C | 1 |
4 other study(ies) available for 4-hydroxyphenylacetic acid and flavin mononucleotide
| Article | Year |
|---|---|
The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis.
Topics: Acinetobacter baumannii; Apoenzymes; Catalysis; Flavin Mononucleotide; Hydroxylation; Kinetics; Mixed Function Oxygenases; Models, Chemical; NAD; Oxidation-Reduction; Oxidoreductases; Oxygen; Phenylacetates; Protein Binding; Thermodynamics | 2005 |
Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase.
Topics: Acinetobacter baumannii; Binding Sites; Flavin Mononucleotide; FMN Reductase; Kinetics; Mixed Function Oxygenases; Models, Biological; Oxidation-Reduction; Phenylacetates; Substrate Specificity; Time Factors | 2007 |
Ultrafast solvation dynamics of flavin mononucleotide in the reductase component of p-hydroxyphenylacetate hydroxylase.
Topics: Animals; Binding Sites; Crotalid Venoms; Crotalus; Flavin Mononucleotide; Kinetics; Mixed Function Oxygenases; Oxidation-Reduction; Oxidoreductases; Phenylacetates; Solvents; Spectrometry, Fluorescence | 2009 |
pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.
Topics: Acinetobacter baumannii; Catalytic Domain; Enzyme Inhibitors; Flavin Mononucleotide; Hydrogen-Ion Concentration; Hydroxylation; Kinetics; Mixed Function Oxygenases; Models, Molecular; Oxygen; Phenylacetates; Pseudomonas aeruginosa | 2011 |