Indole pyruvate decarboxylase

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<StructureSection load='1ovm' size='340' side='right' caption='Indole pyruvate decarboxylase tetramer complex with thiamine diphosphate and Mg+2 ions (green), [[1ovm]]' scene=''>
<StructureSection load='1ovm' size='340' side='right' caption='Indole pyruvate decarboxylase tetramer complex with thiamine diphosphate and Mg+2 ions (green), [[1ovm]]' scene=''>
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'''Indolepyruvate decarboxylase''' (IPDC) catalyzes the conversion of 3-(indol-3-yl)pyruvate to 2-(indol-3-yl)acetaldehyde. IPDC participates in tryptophan metabolism<ref>PMID:12752451</ref>.
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'''Indole pyruvate decarboxylase''' (IPDC) catalyzes the conversion of 3-(indol-3-yl)pyruvate to 2-(indol-3-yl)acetaldehyde. IPDC participates in tryptophan metabolism<ref>PMID:12752451</ref>.
</StructureSection>
</StructureSection>
== 3D Structures of indole pyruvate decarboxylase==
== 3D Structures of indole pyruvate decarboxylase==

Current revision

Indole pyruvate decarboxylase tetramer complex with thiamine diphosphate and Mg+2 ions (green), 1ovm

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3D Structures of indole pyruvate decarboxylase

1ovm – IPDC – Enterobacter cloacae

References

  1. Schutz A, Sandalova T, Ricagno S, Hubner G, Konig S, Schneider G. Crystal structure of thiamindiphosphate-dependent indolepyruvate decarboxylase from Enterobacter cloacae, an enzyme involved in the biosynthesis of the plant hormone indole-3-acetic acid. Eur J Biochem. 2003 May;270(10):2312-21. PMID:12752451

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