| EC |
1.5.3.27 |
| Accepted name: |
2-(methylaminoethyl)phosphonate oxidase |
| Reaction: |
2-(methylaminoethyl)phosphonate + O2 + H2O = phosphonoacetaldehyde + methylamine + H2O2 |
| Other name(s): |
pbfD (gene name); N-methyl-(2-aminoethyl)phosphonate oxidase |
| Systematic name: |
2-(methylaminoethyl)phosphonate oxidase:oxygen oxidoreductase (phosphonoacetaldehyde-forming) |
| Comments: |
Contaions FAD. The enzyme also acts, with lower efficiency, on 2-aminoethylphosphonate, generating phosphonoacetaldehyde and ammonia. The enzyme from Acinetobacter baumannii also transformed 2-(dimethylaminoethyl)phosphonate with appreciable efficiency, generating dimethylamine in place of methylamine. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Zangelmi, E., Ruffolo, F., Dinhof, T., Gerdol, M., Malatesta, M., Chin, J.P., Rivetti, C., Secchi, A., Pallitsch, K. and Peracchi, A. Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism. iScience 26:108108 (2023). [DOI] [PMID: 37876809] |
|
| [EC 1.5.3.27 created 2024] |
| |
|
| |
|
Printable version