Enzyme

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EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.37
Description:Kanamycin B dioxygenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.37
BRENDA Enzyme Link: BRENDA 1.14.11.37
KEGG Enzyme Link: KEGG1.14.11.37
BioCyc Enzyme Link: BioCyc 1.14.11.37
ExPASy Enzyme Link: ExPASy1.14.11.37
EC2PDB Enzyme Link: EC2PDB 1.14.11.37
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.37
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.37
IntEnz Enzyme Link: IntEnz 1.14.11.37
MEDLINE Enzyme Link: MEDLINE 1.14.11.37
MSA:

1.14.11.37;

Phylogenetic Tree:

1.14.11.37;

Uniprot:
M-CSA:
RHEA:35831 2-oxoglutarate + kanamycin B + O2 = 2'-dehydrokanamycin A + CO2 + NH4(+) + succinate
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]=[C;H0;+0:6](-[OH;+0:7])-[C;H0;+0:8](=[*:9])-[*:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:11].[*:9]=[C;H0;+0:8](-[*:10])-[OH;+0:12].[*:5]=[C;H0;+0:6]=[O;H0;+0:7].[NH3;+0:4]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
The last step of kanamycin biosynthesis: unique deamination reaction catalyzed by the α-ketoglutarate-dependent nonheme iron dioxygenase KanJ and the NADPH-dependent reductase KanK.Sucipto H, Kudo F, Eguchi T2012 Apr 222374809