Phenylpyruvate decarboxylase

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{{STRUCTURE_2q5o| PDB=2q5o | SIZE=400| SCENE= |right|CAPTION=Phenylpyruvate decarboxylase dimer complex with phenylpyruvate, deaza-ThDP and Mg+2 (green) ion [[2q5o]] }}
{{STRUCTURE_2q5o| PDB=2q5o | SIZE=400| SCENE= |right|CAPTION=Phenylpyruvate decarboxylase dimer complex with phenylpyruvate, deaza-ThDP and Mg+2 (green) ion [[2q5o]] }}
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== Function ==
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'''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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'''Phenylpyruvate decarboxylase''' (PPDC) catalyzes the conversion of phenylpyruvate to phenylacetaldehyde. PPDC participates in phenylalanine and tryptophan metabolism<ref>PMID:12902239</ref>.
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== Structural highlights ==
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PPDC active site contains the ThDP cofactor and the phenypyruvate substrate<ref>PMID:17905741</ref>.
== 3D Structures of phenylpyruvate decarboxylase ==
== 3D Structures of phenylpyruvate decarboxylase ==

Revision as of 08:21, 23 June 2016

Template:STRUCTURE 2q5o

Contents

Function

Phenylpyruvate 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 highlights

PPDC active site contains the ThDP cofactor and the phenypyruvate substrate[2].

3D Structures of phenylpyruvate decarboxylase

2q5j, 2q5l – AbPPDC + deaza-ThDP derivative – Azospirillum brasilense

2q5o - AbPPDC + deaza-ThDP + phenylpyruvate

2q5q - AbPPDC + deaza-ThDP + phenylvalerate

References

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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