Any feedback?
Literature summary extracted from
- Active site arginine controls the stereochemistry of hydride transfer in cyclohexanone monooxygenase (2018), Arch. Biochem. Biophys., 659, 47-56 .
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.13.22 | D57A | variant retains stereospecificity for the proR hydrogen, substitution results in slow decomposition of the C4a-peroxyflavin intermediate in the presence of cyclohexanone | Acinetobacter johnsonii |
| 1.14.13.22 | R327K | variant lacks stereospecificity for hydride transfer and abstracts either the proR or proS hydrogen from NADPH | Acinetobacter johnsonii |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.22 | Acinetobacter johnsonii | P12015 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.22 | CHMO | - |
Acinetobacter johnsonii |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.13.22 | metabolism | wild type elicits a kinetic isotope effect of 4.7 and 1.1 with 4(R)-[4-2H]NADPH and 4(S)-[4-2H]NADPH, respectively, consistent with transfer of the proR hydrogen to FAD | Acinetobacter johnsonii |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
