| EC |
1.14.13.210 |
| Accepted name: |
4-methyl-5-nitrocatechol 5-monooxygenase |
| Reaction: |
4-methyl-5-nitrocatechol + NAD(P)H + H+ + O2 = 2-hydroxy-5-methylquinone + nitrite + NAD(P)+ + H2O |
| Other name(s): |
dntB (gene name); 4-methyl-5-nitrocatechol oxygenase; MNC monooxygenase |
| Systematic name: |
4-methyl-5-nitrocatechol,NAD(P)H:oxygen 5-oxidoreductase (5-hydroxylating, nitrite-forming) |
| Comments: |
Contains FAD. The enzyme, isolated from the bacterium Burkholderia sp. DNT, can use both NADH and NADPH, but prefers NADPH. It has a narrow substrate range, but can also act on 4-nitrocatechol. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Haigler, B.E., Suen, W.C. and Spain, J.C. Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT. J. Bacteriol. 178 (1996) 6019–6024. [DOI] [PMID: 8830701] |
| 2. |
Leungsakul, T., Johnson, G.R. and Wood, T.K. Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics. Appl. Environ. Microbiol. 72 (2006) 3933–3939. [DOI] [PMID: 16751499] |
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| [EC 1.14.13.210 created 2016] |
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