Phenylpyruvate decarboxylase
From Proteopedia
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- | <StructureSection load='2q5o' size=' | + | <StructureSection load='2q5o' size='350' side='right' scene='46/468226/Cv/1' caption='Phenylpyruvate decarboxylase dimer complex with phenylpyruvate, deaza-ThDP and Mg+2 (green) ion [[2q5o]]'> |
== Function == | == Function == | ||
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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>. |
+ | *<scene name='46/468226/Cv/6'>ThDP cofactor/phenypyruvate substrate binding site</scene>. Water molecules are shown as red spheres. | ||
+ | *<scene name='46/468226/Cv/7'>Mg coordination site</scene>. | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of phenylpyruvate decarboxylase == | == 3D Structures of phenylpyruvate decarboxylase == |
Current revision
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3D Structures of phenylpyruvate decarboxylase
2q5j, 2q5l – AbPPDC + deaza-ThDP derivative – Azospirillum brasilense
2q5o - AbPPDC + deaza-ThDP + phenylpyruvate
2q5q - AbPPDC + deaza-ThDP + phenylvalerate
References
- ↑ 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