ID: | 4.1.1.74 | ||
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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: |
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Cath: | 3.40.50.970; 3.40.50.1220; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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 |
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 |
Title | Authors | Date | PubMed ID |
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Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-acetic acid biosynthesis. | Koga J | 1995 May 18 | 7766676 |
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 A | 1973 Jan 3 | 4687392 |
Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae. | Kneen MM, Stan R, Yep A, Tyler RP, Saehuan C, McLeish MJ | 2011 Jun | 21501384 |
The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. | Dickinson JR, Salgado LE, Hewlins MJ | 2003 Mar 7 | 12499363 |