EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.14.9 | - |
Acinetobacter baumannii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.14.9 | H396A | mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 7.1 compared to 9.8 for wild-type | Acinetobacter baumannii |
1.14.14.9 | H396N | mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 9.3 compared to 9.8 for wild-type | Acinetobacter baumannii |
1.14.14.9 | H396V | mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 7.3 compared to 9.8 for wild-type | Acinetobacter baumannii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.9 | Acinetobacter baumannii | Q6Q272 | oxygenase component C2 | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.9 | 4-hydroxyphenylacetate + NADH + O2 | - |
Acinetobacter baumannii | 3,4-dihydroxyphenylacetate + NAD+ + H2O | - |
? | |
1.14.14.9 | additional information | proton transfer is not the rate-limiting step in the formation of the C4a-(hydro)peroxyflavin intermediate. Residue His396 may act as an instantaneous proton provider for the proton-coupled electron transfer that occurs before the transition state of C4a-(hydro)peroxyflavin formation | Acinetobacter baumannii | ? | - |
? |