Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.13.210
Description:4-methyl-5-nitrocatechol 5-monooxygenase.
Alternative Name: MNC monooxygenase.
4-methyl-5-nitrocatechol oxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.13.210
BRENDA Enzyme Link: BRENDA 1.14.13.210
KEGG Enzyme Link: KEGG1.14.13.210
BioCyc Enzyme Link: BioCyc 1.14.13.210
ExPASy Enzyme Link: ExPASy1.14.13.210
EC2PDB Enzyme Link: EC2PDB 1.14.13.210
ExplorEnz Enzyme Link: ExplorEnz 1.14.13.210
PRIAM enzyme-specific profiles Link: PRIAM 1.14.13.210
IntEnz Enzyme Link: IntEnz 1.14.13.210
MEDLINE Enzyme Link: MEDLINE 1.14.13.210
MSA:

1.14.13.210;

Phylogenetic Tree:

1.14.13.210;

Uniprot:
M-CSA:
RHEA:48016 4-methyl-5-nitrocatechol + NADH + O2 = 2-hydroxy-5-methylquinone + H(+) + H2O + NAD(+) + nitrite
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]=[N+;H0:10](-[*:11])-[c;H0;+0:12]1:[cH;+0:13]:[c;H0;+0:14](-[*:15]):[c;H0;+0:16](-[OH;+0:17]):[cH;+0:18]:[c;H0;+0:19]:1-[*:20].[O;H0;+0:21]=[O;H0;+0:22]>>[*:15]-[C;H0;+0:14]1=[CH;+0:13]-[C;H0;+0:12](=[O;H0;+0:21])-[C;H0;+0:19](-[*:20])=[CH;+0:18]-[C;H0;+0:16]-1=[O;H0;+0:17].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]=[N;H0;+0:10]-[*:11].[OH2;+0:22]
Reaction
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References

TitleAuthorsDatePubMed ID
Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT.Haigler BE, Suen WC, Spain JC1996 Oct8830701
Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics.Leungsakul T, Johnson GR, Wood TK2006 Jun16751499

RHEA:48012 4-methyl-5-nitrocatechol + NADPH + O2 = 2-hydroxy-5-methylquinone + H(+) + H2O + NADP(+) + nitrite
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]=[N+;H0:10](-[*:11])-[c;H0;+0:12]1:[cH;+0:13]:[c;H0;+0:14](-[*:15]):[c;H0;+0:16](-[OH;+0:17]):[cH;+0:18]:[c;H0;+0:19]:1-[*:20].[O;H0;+0:21]=[O;H0;+0:22]>>[*:15]-[C;H0;+0:14]1=[CH;+0:13]-[C;H0;+0:12](=[O;H0;+0:21])-[C;H0;+0:19](-[*:20])=[CH;+0:18]-[C;H0;+0:16]-1=[O;H0;+0:17].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]=[N;H0;+0:10]-[*:11].[OH2;+0:22]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT.Haigler BE, Suen WC, Spain JC1996 Oct8830701
Protein engineering of the 4-methyl-5-nitrocatechol monooxygenase from Burkholderia sp. strain DNT for enhanced degradation of nitroaromatics.Leungsakul T, Johnson GR, Wood TK2006 Jun16751499