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Literature summary extracted from
- Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase (2005), Biochemistry, 44, 13304-13314.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.13.2 | H72N | disruption of proton-transfer network, kinetic analysis | Pseudomonas aeruginosa |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.2 | Pseudomonas aeruginosa | P20586 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.13.2 | 4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O | kinetic scheme of reductive half-reaction, flavin movement can occur in the presence or absence of NADPH, but NADPH stimulates movement to the reactive conformation required for hydride transfer | Pseudomonas aeruginosa |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.2 | FAD | - |
Pseudomonas aeruginosa |  |
| 1.14.13.2 | NADPH | - |
Pseudomonas aeruginosa | |
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Release 2023.1 (January 2023)
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