Phenylpyruvate decarboxylase: Difference between revisions
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<StructureSection load='2q5o' size='450' side='right' scene='' caption='Phenylpyruvate decarboxylase dimer complex with phenylpyruvate, deaza-ThDP and Mg+2 (green) ion [[2q5o]]'> | |||
== Function == | == Function == | ||
'''Phenylpyruvate decarboxylase''' (PPDC) catalyzes the conversion of phenylpyruvate to phenylacetaldehyde. PPDC participates in phenylalanine and tryptophan metabolism<ref>PMID:12902239</ref>. PPDC is a thiamine diphosphate (ThDP) (i.e., vitamin B1)-dependent enzyme. | '''Phenylpyruvate decarboxylase''' (PPDC) catalyzes the conversion of phenylpyruvate to phenylacetaldehyde. PPDC participates in phenylalanine and tryptophan metabolism<ref>PMID:12902239</ref>. PPDC is a thiamine diphosphate (ThDP) (i.e., vitamin B1)-dependent enzyme. | ||
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== Structural highlights == | == Structural highlights == | ||
PPDC active site contains the ThDP cofactor and the phenypyruvate substrate<ref>PMID:17905741</ref>. | PPDC active site contains the ThDP cofactor and the phenypyruvate substrate<ref>PMID:17905741</ref>. | ||
</StructureSection> | |||
== 3D Structures of phenylpyruvate decarboxylase == | == 3D Structures of phenylpyruvate decarboxylase == | ||
Revision as of 12:13, 8 September 2016
FunctionPhenylpyruvate decarboxylase (PPDC) catalyzes the conversion of phenylpyruvate to phenylacetaldehyde. PPDC participates in phenylalanine and tryptophan metabolism[1]. PPDC is a thiamine diphosphate (ThDP) (i.e., vitamin B1)-dependent enzyme. Structural highlightsPPDC active site contains the ThDP cofactor and the phenypyruvate substrate[2]. |
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3D Structures of phenylpyruvate decarboxylase3D Structures of phenylpyruvate decarboxylase
2q5j, 2q5l – AbPPDC + deaza-ThDP derivative – Azospirillum brasilense
2q5o - AbPPDC + deaza-ThDP + phenylpyruvate
2q5q - AbPPDC + deaza-ThDP + phenylvalerate
ReferencesReferences
- ↑ Vuralhan Z, Morais MA, Tai SL, Piper MD, Pronk JT. Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae. Appl Environ Microbiol. 2003 Aug;69(8):4534-41. PMID:12902239
- ↑ Versees W, Spaepen S, Wood MD, Leeper FJ, Vanderleyden J, Steyaert J. Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase. J Biol Chem. 2007 Nov 30;282(48):35269-78. Epub 2007 Sep 28. PMID:17905741 doi:http://dx.doi.org/10.1074/jbc.M706048200