Enzyme

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     1. Oxidoreductases
        1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
            1.13.11 With incorporation of two atoms of oxygen
ID:1.13.11.74
Description:2-aminophenol 1,6-dioxygenase.
Cath: 3.40.830.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.13.11.74
BRENDA Enzyme Link: BRENDA 1.13.11.74
KEGG Enzyme Link: KEGG1.13.11.74
BioCyc Enzyme Link: BioCyc 1.13.11.74
ExPASy Enzyme Link: ExPASy1.13.11.74
EC2PDB Enzyme Link: EC2PDB 1.13.11.74
ExplorEnz Enzyme Link: ExplorEnz 1.13.11.74
PRIAM enzyme-specific profiles Link: PRIAM 1.13.11.74
IntEnz Enzyme Link: IntEnz 1.13.11.74
MEDLINE Enzyme Link: MEDLINE 1.13.11.74
MSA:

1.13.11.74;

Phylogenetic Tree:

1.13.11.74;

Uniprot:
M-CSA:
RHEA:26305 2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde
RULE(radius=1) [*:1]-[c;H0;+0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[cH;+0:6]:[c;H0;+0:7]:1-[OH;+0:8].[O;H0;+0:9]=[O;H0;+0:10]>>[*:1]-[C;H0;+0:2](=[CH;+0:3]-[CH;+0:4]=[CH;+0:5]-[CH;+0:6]=[O;H0;+0:10])-[C;H0;+0:7](=[O;H0;+0:8])-[OH;+0:9]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme.Takenaka S, Murakami S, Shinke R, Hatakeyama K, Yukawa H, Aoki K1997 Jun 69169437
Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor.Li de F, Zhang JY, Hou YJ, Liu L, Hu Y, Liu SJ, Wang da C, Liu W2013 Jan23275161
Crystallization and preliminary crystallographic analysis of 2-aminophenol 1,6-dioxygenase complexed with substrate and with an inhibitor.Li DF, Zhang JY, Hou Y, Liu L, Liu SJ, Liu W2012 Nov 123143244
A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli.Wu JF, Sun CW, Jiang CY, Liu ZP, Liu SJ2005 Jan15580337