Protein Variants | Comment | Organism |
---|---|---|
S146A | mutation in oxygenase component C2, mutant is more effective than the wild-type in catalyzing the hydroxylation of 4-aminophenylacetate. Both variants first hydroxylate to give 3-hydroxy-4-aminophenylacetate, which is further hydroxylated to give 3,5-dihydroxy-4-aminophenylacetate | Acinetobacter baumannii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter baumannii | Q6Q272 | oxygenase component C2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-aminophenylacetate + FMNH2 + O2 | - |
Acinetobacter baumannii | 4-amino-3,5-dihydroxyphenylacetate + FMN + H2O | - |
? | |
additional information | wild-type shows a hydroxylation rate constant (kOH) for 4-aminophenylacetate of 0.028 per s compared to 17 per s for 4-hydroxyphenylacetate. Mutant S146A shows hydroxylation rate constants of 2.6 per s for 4-aminophenylacetate compared to 2.5 per s for 4-hydroxyphenylacetate | Acinetobacter baumannii | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
C2-hpah | - |
Acinetobacter baumannii |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | - |
substrate 4-aminophenylacetate can only bind to the wild-type enzyme at pH 6.0, substrate can bind to mutant S146A at both pH 6.0 and 9.0 | Acinetobacter baumannii |
9 | - |
substrate can bind to mutant S146A at both pH 6.0 and 9.0 | Acinetobacter baumannii |