EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.13.2 | expression in Escherichia coli | Pseudomonas aeruginosa |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.13.2 | E49Q | mutation enhances the positive charge in the active site of PHBH, rate of hydroxylation is above that of wild-type, the rate of release of product is slower than the rate of return of the flavin to the oxidized state | Pseudomonas aeruginosa |
1.14.13.2 | E49Q | investigation of oxygen half-reaction | Pseudomonas aeruginosa |
1.14.13.2 | H72N | rate of turnover is only about 8% of wild-type enzyme at all pH values | Pseudomonas aeruginosa |
1.14.13.2 | H72N | investigation of oxygen half-reaction | Pseudomonas aeruginosa |
1.14.13.2 | K297M | mutation decreases the positive charge in the active site of PHBH but does not interfere with with the H-bond network, 25fold decrease in the rate of hydroxylation compared to wild-type enzyme | Pseudomonas aeruginosa |
1.14.13.2 | K297M | investigation of oxygen half-reaction | Pseudomonas aeruginosa |
1.14.13.2 | Y201F | investigation of oxygen half-reaction | Pseudomonas aeruginosa |
1.14.13.2 | Y385F | in the oxygen half-reaction, the rate of hydroxylation is 25fold slower than that for the wild-type enzyme at pH 6.5, in contrast to wild-type enzyme there is some formation of H2O2 in the reaction | Pseudomonas aeruginosa |
1.14.13.2 | Y385F | investigation of oxygen half-reaction | Pseudomonas aeruginosa |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.2 | 4-hydroxybenzoate + NADPH + O2 | Pseudomonas aeruginosa | - |
protocatechuate + NADP+ + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.2 | Pseudomonas aeruginosa | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.13.2 | 4-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O | rate of formation of the flavin hydroperoxide is not influenced by pH-change. Rate of hydroxylation reaction increases with pH. The H-bond network abstracts the phenolic proton from p-hydroxybenzoate in the transition state of oxygen transfer. Product deprotonation enhances the rate of a specific conformational change required for both product relase and the elimination of water | Pseudomonas aeruginosa |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.2 | 4-hydroxybenzoate + NADPH + O2 | - |
Pseudomonas aeruginosa | protocatechuate + NADP+ + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.2 | PHBH | - |
Pseudomonas aeruginosa |