EC number:1.3.99.16

Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.99 With unknown physiological acceptors
ID:1.3.99.16
Description:Isoquinoline 1-oxidoreductase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.99.16
BRENDA Enzyme Link: BRENDA 1.3.99.16
KEGG Enzyme Link: KEGG1.3.99.16
BioCyc Enzyme Link: BioCyc 1.3.99.16
ExPASy Enzyme Link: ExPASy1.3.99.16
EC2PDB Enzyme Link: EC2PDB 1.3.99.16
ExplorEnz Enzyme Link: ExplorEnz 1.3.99.16
PRIAM enzyme-specific profiles Link: PRIAM 1.3.99.16
IntEnz Enzyme Link: IntEnz 1.3.99.16
MEDLINE Enzyme Link: MEDLINE 1.3.99.16

EC number:1.3.99.16

MSA:

1.3.99.16;
Phylogenetic Tree:

1.3.99.16;
Uniprot:
M-CSA:
RHEA:11588 A + H2O + isoquinoline = AH2 + isoquinolin-1(2H)-one
RULE(radius=1) [*:1]:[n;H0;+0:2]:[cH;+0:3]:[*:4].[OH2;+0:5]>>[*:1]:[nH;+0:2]:[c;H0;+0:3](:[*:4])=[O;H0;+0:5]
Reaction
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References

TitleAuthorsDatePubMed ID
Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase.Lehmann M, Tshisuaka B, Fetzner S, Röger P, Lingens F1994 Apr 158157655
Molecular cloning of the isoquinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence comparisons with other molybdenum-containing hydroxylases.Lehmann M, Tshisuaka B, Fetzner S, Lingens F1995 Jun 167782304