Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.1 Carboxy-lyases
ID:4.1.1.74
Description:Indolepyruvate decarboxylase.
Alternative Name: Indole-3-pyruvate decarboxylase.
Indol-3-yl-pyruvate carboxy-lyase.
3-(indol-3-yl)pyruvate carboxy-lyase.
Prosite: PDOC00166;
PDB:
PDBScop
Cath: 3.40.50.970; 3.40.50.1220;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.1.74
BRENDA Enzyme Link: BRENDA 4.1.1.74
KEGG Enzyme Link: KEGG4.1.1.74
BioCyc Enzyme Link: BioCyc 4.1.1.74
ExPASy Enzyme Link: ExPASy4.1.1.74
EC2PDB Enzyme Link: EC2PDB 4.1.1.74
ExplorEnz Enzyme Link: ExplorEnz 4.1.1.74
PRIAM enzyme-specific profiles Link: PRIAM 4.1.1.74
IntEnz Enzyme Link: IntEnz 4.1.1.74
MEDLINE Enzyme Link: MEDLINE 4.1.1.74
MSA:

4.1.1.74;

Phylogenetic Tree:

4.1.1.74;

Uniprot:
M-CSA:
RHEA:18017 H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[*:5])-[*:6].[H+;H0:7]>>[*:1]=[C;H0;+0:2]=[O;H0;+0:3].[*:5]=[CH;+0:4]-[*:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-acetic acid biosynthesis.Koga J1995 May 187766676
The influence of steric and electronic parameters on the substrate behavior of -oxo acids to yeast pyruvate decarboxylase.Lehmann H, Fischer G, Hübner G, Kohnert KD, Schellenberger A1973 Jan 34687392
Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae.Kneen MM, Stan R, Yep A, Tyler RP, Saehuan C, McLeish MJ2011 Jun21501384
The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae.Dickinson JR, Salgado LE, Hewlins MJ2003 Mar 712499363