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:1.3.99.18
Description:Quinaldate 4-oxidoreductase.
Alternative Name: Quinaldic acid 4-oxidoreductase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.99.18
BRENDA Enzyme Link: BRENDA 1.3.99.18
KEGG Enzyme Link: KEGG1.3.99.18
BioCyc Enzyme Link: BioCyc 1.3.99.18
ExPASy Enzyme Link: ExPASy1.3.99.18
EC2PDB Enzyme Link: EC2PDB 1.3.99.18
ExplorEnz Enzyme Link: ExplorEnz 1.3.99.18
PRIAM enzyme-specific profiles Link: PRIAM 1.3.99.18
IntEnz Enzyme Link: IntEnz 1.3.99.18
MEDLINE Enzyme Link: MEDLINE 1.3.99.18
MSA:

1.3.99.18;

Phylogenetic Tree:

1.3.99.18;

Uniprot:
M-CSA:
RHEA:16697 A + H2O + quinaldate = AH2 + kynurenate
RULE(radius=1) [*:1]:[cH;+0:2]:[*:3].[OH2;+0:4]>>[*:1]:[c;H0;+0:2](:[*:3])-[OH;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Microbial metabolism of quinoline and related compounds. XVIII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1.Fetzner S, Lingens F1993 Jun8357532
Microbial metabolism of quinoline and related compounds. XX. Quinaldic acid 4-oxidoreductase from Pseudomonas sp. AK-2 compared to other procaryotic molybdenum-containing hydroxylases.Sauter M, Tshisuaka B, Fetzner S, Lingens F1993 Nov8292263