Enzyme

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     1. Oxidoreductases
        1.7 Acting on other nitrogenous compounds as donors
            1.7.1 With NAD+ or NADP+ as acceptor
ID:1.7.1.17
Description:FMN-dependent NADH-azoreductase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.7.1.17
BRENDA Enzyme Link: BRENDA 1.7.1.17
KEGG Enzyme Link: KEGG1.7.1.17
BioCyc Enzyme Link: BioCyc 1.7.1.17
ExPASy Enzyme Link: ExPASy1.7.1.17
EC2PDB Enzyme Link: EC2PDB 1.7.1.17
ExplorEnz Enzyme Link: ExplorEnz 1.7.1.17
PRIAM enzyme-specific profiles Link: PRIAM 1.7.1.17
IntEnz Enzyme Link: IntEnz 1.7.1.17
MEDLINE Enzyme Link: MEDLINE 1.7.1.17
MSA:

1.7.1.17;

Phylogenetic Tree:

1.7.1.17;

Uniprot:
M-CSA:
RHEA:55872 anthranilate + N,N-dimethyl-1,4-phenylenediamine + 2 NADP(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 H(+) + 2 NADPH
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]-[NH2;+0:4].[*:5]-[c;H0;+0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[n+;H0:10](-[*:11]):[cH;+0:12]:1.[*:13]-[n+;H0:14]1:[cH;+0:15]:[cH;+0:16]:[cH;+0:17]:[c;H0;+0:18](-[*:19]):[cH;+0:20]:1>>[*:5]-[C;H0;+0:6]1=[CH;+0:12]-[N;H0;+0:10](-[*:11])-[CH;+0:9]=[CH;+0:8]-[CH2;+0:7]-1.[*:13]-[N;H0;+0:14]1-[CH;+0:15]=[CH;+0:16]-[CH2;+0:17]-[C;H0;+0:18](-[*:19])=[CH;+0:20]-1.[*:1]-[N;H0;+0:2]=[N;H0;+0:4]-[*:3]
Reaction
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References

TitleAuthorsDatePubMed ID
Characteristics of major Escherichia coli reductases involved in aerobic nitro and azo reduction.Mercier C, Chalansonnet V, Orenga S, Gilbert C2013 Oct23795903
Expansion of substrate specificity and catalytic mechanism of azoreductase by X-ray crystallography and site-directed mutagenesis.Ito K, Nakanishi M, Lee WC, Zhi Y, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M2008 May 1618337254
Crystallization and preliminary X-ray analysis of AzoR (azoreductase) from Escherichia coli.Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M2005 Apr 116511052
Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase.Nakanishi M, Yatome C, Ishida N, Kitade Y2001 Dec 711583992