Enzyme

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EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.3 With oxygen as acceptor
ID:1.1.3.43
Description:Paromamine 6'-oxidase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.3.43
BRENDA Enzyme Link: BRENDA 1.1.3.43
KEGG Enzyme Link: KEGG1.1.3.43
BioCyc Enzyme Link: BioCyc 1.1.3.43
ExPASy Enzyme Link: ExPASy1.1.3.43
EC2PDB Enzyme Link: EC2PDB 1.1.3.43
ExplorEnz Enzyme Link: ExplorEnz 1.1.3.43
PRIAM enzyme-specific profiles Link: PRIAM 1.1.3.43
IntEnz Enzyme Link: IntEnz 1.1.3.43
MEDLINE Enzyme Link: MEDLINE 1.1.3.43
MSA:

1.1.3.43;

Phylogenetic Tree:

1.1.3.43;

Uniprot:
M-CSA:
RHEA:34035 O2 + paromamine = 6'-oxoparomamine + H2O2
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[O;H0;+0:4]=[O;H0;+0:5]>>[*:1]-[CH;+0:2]=[O;H0;+0:3].[OH;+0:4]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The oxidoreductases LivQ and NeoQ are responsible for the different 6'-modifications in the aminoglycosides lividomycin and neomycin.Clausnitzer D, Piepersberg W, Wehmeier UF2011 Sep21689223
Biosynthesis of 3'-deoxy-carbamoylkanamycin C in a Streptomyces tenebrarius mutant strain by tacB gene disruption.Yu Y, Hou X, Ni X, Xia H2008 Feb18408324
Elaboration of neosamine rings in the biosynthesis of neomycin and butirosin.Huang F, Spiteller D, Koorbanally NA, Li Y, Llewellyn NM, Spencer JB2007 Feb 1217206729