EC number:1.5.3.6

Enzyme

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EC Tree
     1. Oxidoreductases
        1.5 Acting on the CH-NH group of donors
            1.5.3 With oxygen as acceptor
ID:1.5.3.6
Description:(R)-6-hydroxynicotine oxidase.
Alternative Name: D-6-hydroxynicotine oxidase.
6-hydroxy-D-nicotine oxidase.
Prosite: PDOC00674;
PDB:
PDBScop
Cath: 3.30.43.10; 3.30.465.10; 3.50.50.60; 3.90.660.10; 3.40.462.20;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.5.3.6
BRENDA Enzyme Link: BRENDA 1.5.3.6
KEGG Enzyme Link: KEGG1.5.3.6
BioCyc Enzyme Link: BioCyc 1.5.3.6
ExPASy Enzyme Link: ExPASy1.5.3.6
EC2PDB Enzyme Link: EC2PDB 1.5.3.6
ExplorEnz Enzyme Link: ExplorEnz 1.5.3.6
PRIAM enzyme-specific profiles Link: PRIAM 1.5.3.6
IntEnz Enzyme Link: IntEnz 1.5.3.6
MEDLINE Enzyme Link: MEDLINE 1.5.3.6

EC number:1.5.3.6

MSA:

1.5.3.6;
Phylogenetic Tree:

1.5.3.6;
Uniprot:
M-CSA:
RHEA:10012 (R)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2
RULE(radius=1) [*:1]-[N;H0;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[*:6].[O;H0;+0:7]=[O;H0;+0:8].[OH2;+0:9]>>([*:5]-[C;H0;+0:4](-[*:6])=[O;H0;+0:9].[*:1]-[NH;+0:2]-[*:3]).[OH;+0:7]-[OH;+0:8]
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Site-directed mutagenesis of the FAD-binding histidine of 6-hydroxy-D-nicotine oxidase. Consequences on flavinylation and enzyme activity.Mauch L, Bichler V, Brandsch R1989 Oct 232680607
Crystal structure of 6-hydroxy-D-nicotine oxidase from Arthrobacter nicotinovorans.Koetter JW, Schulz GE2005 Sep 1616095622