Cloned (Comment) | Organism |
---|---|
gene mobA, phylogenetic analysis | Comamonas testosteroni |
Protein Variants | Comment | Organism |
---|---|---|
V257A | a directed evolution study reveals that 3HB4H from Comamonas testosteroni strain GZ39 is considerably active with 4-hydroxybenzoate and that this activity increases in the V257A variant. The same variant slowly converts phenol to catechol, an activity not observed with the wild-type enzyme | Comamonas testosteroni |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-hydroxybenzoate + NADPH + H+ + O2 | Comamonas testosteroni | - |
3,4-dihydroxybenzoate + NADP+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Comamonas testosteroni | Q6SSJ6 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-hydroxybenzoate + NADPH + H+ + O2 | - |
Comamonas testosteroni | 3,4-dihydroxybenzoate + NADP+ + H2O | - |
? | |
additional information | enzyme 3HB4H catalyzes an ortho-hydroxylation reaction | Comamonas testosteroni | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
3-hydroxybenzoate 4-hydroxylase | - |
Comamonas testosteroni |
3HB4H | - |
Comamonas testosteroni |
FAD-dependent 4-hydroxybenzoate hydroxylase | - |
Comamonas testosteroni |
MobA | - |
Comamonas testosteroni |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Comamonas testosteroni | |
NADPH | - |
Comamonas testosteroni |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic analysis of FAD-dependent 4-hydroxybenzoate hydroxylases and 3-hydroxybenzoate 4-hydroxylase, phylogenetic analysis and tree, overview. Enzyme structure analysis and comparisons (PDB ID pdb: 2dkh). Enzyme 3HB4H is missing a flexible loop, which is involved in flavin movement and closing-off the active site. In 3HB4H, the conserved tyrosine 222 makes a hydrogen bond with the hydroxyl group of the phenolic substrate, substrate binding pocket and structure-function analysis, homology modeling, overview. Residues Asp75 and Tyr271 might enhance the electron donating capacity of the hydroxyl group of 3-hydroxybenzoate (3-HB). The carboxyl group of 3-HB preferentially interacts with the side chains of His135 and Lys247. This ionic interaction is proposed to determine the orientation of bound substrate | Comamonas testosteroni |
additional information | FAD-dependent hydroxybenzoate hydroxylase enzymes structure comparisons, overview | Comamonas testosteroni |