veratryl alcohol has been researched along with tryptophan in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (60.00) | 18.2507 |
| 2000's | 2 (40.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Collins, PJ; Dobson, AD; Field, JA; Teunissen, P | 1 |
| Blodig, W; Choinowski, T; Piontek, K; Winterhalter, KH | 1 |
| Aust, SD; Nie, G; Reading, NS; Timofeevski, SL | 1 |
| Blodig, W; Doyle, WA; Piontek, K; Smith, AT | 1 |
| Dorlet, P; Doyle, WA; Ivancich, A; Smith, AT | 1 |
5 other study(ies) available for veratryl alcohol and tryptophan
| Article | Year |
|---|---|
Stabilization of lignin peroxidases in white rot fungi by tryptophan.
Topics: Azo Compounds; Basidiomycota; Benzyl Alcohols; Culture Media; Gene Expression Regulation, Enzymologic; Gene Expression Regulation, Fungal; Hydrogen Peroxide; Indoles; Oxidation-Reduction; Peroxidases; Polymerase Chain Reaction; Transcription, Genetic; Tryptophan | 1997 |
The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle.
Topics: Benzyl Alcohols; Binding Sites; Calcium; Crystallography, X-Ray; Free Radicals; Fungal Proteins; Hemeproteins; Hydrogen Bonding; Hydrogen Peroxide; Lignin; Models, Molecular; Molecular Structure; Oxidation-Reduction; Peroxidases; Phanerochaete; Protein Folding; Protein Structure, Secondary; Protoporphyrins; Spectrophotometry; Spin Labels; Tryptophan | 1999 |
Addition of veratryl alcohol oxidase activity to manganese peroxidase by site-directed mutagenesis.
Topics: Alcohol Oxidoreductases; Benzyl Alcohols; Binding Sites; Enzyme Stability; Escherichia coli; Heme; Hydrogen Peroxide; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Manganese; Mutagenesis, Site-Directed; Oxalates; Peroxidases; Phanerochaete; Recombinant Proteins; Solubility; Spectrophotometry; Substrate Specificity; Tryptophan | 1999 |
Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.
Topics: Amino Acid Substitution; Benzyl Alcohols; Catalysis; Crystallography, X-Ray; Escherichia coli; Heme; Hydrogen Bonding; Hydroxylation; Isoenzymes; Models, Molecular; Mutation; Oxidation-Reduction; Peroxidases; Phanerochaete; Protein Conformation; Recombinant Proteins; Tryptophan | 2001 |
Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.
Topics: Amino Acid Substitution; Benzyl Alcohols; Catalysis; Coprinus; Electron Spin Resonance Spectroscopy; Fungal Proteins; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Peroxidase; Peroxidases; Protein Engineering; Protein Structure, Tertiary; Substrate Specificity; Tryptophan | 2009 |