Cloned (Comment) | Organism |
---|---|
- |
Acinetobacter baumannii |
Protein Variants | Comment | Organism |
---|---|---|
H120D | mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate | Acinetobacter baumannii |
H120E | mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate | Acinetobacter baumannii |
H120K | catalyzes hydroxylation with efficiency comparable to that of the wild-type enzyme, the hydroxylation rate constant for H120K is 5.7 per s and the product conversion ratio is 75%, compared to values of 16 s-1 and 90% for the wild-type enzyme | Acinetobacter baumannii |
H120N | mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate | Acinetobacter baumannii |
H120Q | mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate | Acinetobacter baumannii |
H120R | mutant is able to catalyze hydroxylation | Acinetobacter baumannii |
H120Y | mutant can form C4a-hydroperoxy-FMN, a reactive intermediate necessary for hydroxylation, but cannot hydroxylate 4-hydroxyphenylacetate | Acinetobacter baumannii |
S146A | product formation is pH-independent and constant at about 70% over a pH range of 6-10 | Acinetobacter baumannii |
S146C | product formation decreases from about 65% at pH 6.0 to 27% at pH 10.0 | Acinetobacter baumannii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter baumannii | Q6Q272 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-hydroxyphenylacetate + FMNH2 + O2 | - |
Acinetobacter baumannii | 3,4-hydroxyphenylacetate + FMN + H2O | hydroxylation rate constant is 16 per s and the product conversion ratio is 90% | ? |
Synonyms | Comment | Organism |
---|---|---|
HPA 3-hydroxylase | - |
Acinetobacter baumannii |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
hydroxylation reaction of wildtype oxygenase component is pH-independent between pH 6 and 10 | Acinetobacter baumannii |