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Literature summary for 1.14.14.9 extracted from
- Hydroxylation of 4-hydroxyphenylethylamine derivatives by R263 variants of the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase (2017), Arch. Biochem. Biophys., 620, 1-11 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Acinetobacter baumannii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R263A | mutation of oxygenase component, 72% hydroxylation efficiency of phydroxyphenylacetate, 7% hydroxylation of tyramine | Acinetobacter baumannii |
| R263D | mutation of oxygenase component, variant can catalyze hydroxylation of tyramine to form dopamine with the highest yield (57%) while maintaining 86% hydroxylation efficiency of phydroxyphenylacetate | Acinetobacter baumannii |
| R263E | mutation of oxygenase component, 73% hydroxylation efficiency of phydroxyphenylacetate, no hydroxylation of tyramine | Acinetobacter baumannii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acinetobacter baumannii | Q6Q272 | oxygenase component C2 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-hydroxyphenylacetate + FMNH + O2 | - |
Acinetobacter baumannii | 3,4-dihydroxyphenylacetate + FMN + H2O | - |
? |  |
| octopamine + FMNH + O2 | no substrate of wild-type or mutant R263E, R263D, R263A, but substrate of mutant R263D/Y398D | Acinetobacter baumannii | norepinephrine + FMN + H2O | - |
? | |
| tyramine + FMNH + O2 | no substrate of wild-type or mutant R263E, but substrate of mutants R263D and R263A | Acinetobacter baumannii | dopamine + FMN + H2O | - |
? | |
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