| EC |
1.14.15.38 |
| Accepted name: |
N,N-dimethyl phenylurea N-demethylase |
| Reaction: |
an N,N-dimethyl-N′-phenylurea compound + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = an N-methyl-N′-phenylurea compound + formaldehyde + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O |
| Other name(s): |
pdmAB (gene names) |
| Systematic name: |
N,N-dimethyl-N′-phenylurea compound,NAD(P)H:oxygen oxidoreductase (formaldehyde-forming) |
| Comments: |
The enzyme, found in members of the Sphingobium genus, initiates the degradation of N,N-dimethyl-phenylurea herbicides by mono-N-demethylation. The catalytic unit contains a Rieske [2Fe-2S] iron-sulfur cluster, and catalyses the monooxygenation of a methyl group. The resulting N-methoxyl group is unstable and decomposes spontaneously to form formaldehyde. The enzyme associates with additional proteins (a reductase and a [3Fe-4S] type ferredoxin) that are involved in the transfer of electrons from NAD(P)H to the active site. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Gu, T., Zhou, C., Sorensen, S.R., Zhang, J., He, J., Yu, P., Yan, X. and Li, S. The novel bacterial N-demethylase PdmAB is responsible for the initial step of N,N-dimethyl-substituted phenylurea herbicide degradation. Appl. Environ. Microbiol. 79 (2013) 7846–7856. [PMID: 24123738] |
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| [EC 1.14.15.38 created 2020] |
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