Decarboxylase phenylpyruvate

Guo, Z., Goswami, A., Mirfakhrae, K. D., Patel, R. N. Asymmetric acyloin condensation catalyzed by phenylpyruvate decarboxylase. Tetrahedron Asymmetry 999, 10, 4667-4675. 

Pyruvate decarboxylase, R2 = Me Benzoylfoimate decarboxylase, Rj = Ph Phenylpyruvate decarboxylase, R2 = PhCH2... 

Stereoselective carbon-carbon bond-forming reactions are among the most useful S5mthetic methods in asymmetric synthesis as they allow the simultaneous creation of up to two adjacent stereocenters. Acyloin formation mediated by thiamine diphosphate-dependent decarboxylase, yeast pyruvate decarboxylase, bacterial benzoylformate decarboxylase, and phenylpyruvate decarboxylase has been reported [142-147]. 

Guo Z, Goswami A, Nanduri VB, Patel RN. Asymmetric acyloin condensation catalysed by phenylpyruvate decarboxylase. Part 2 Substrate specificity and purification of the enzyme. Tetrahedron Asymm. 2001 12 571 577. 

Kneen MM, Stan R, Yep A, lyier RP, Saehuan C, McLeish MJ. Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae. FEBSJ. 2011 278 1842-1853. 

Pyruvate decarboxylase is by far the best characterized enzyme among thiamine pyrophosphate-linked a-keto acid decarboxylases. Properties of this enzyme, its structure, and its catalytic mechanism have been described in a recent review [8]. Two other enzjmies belonging to the class of a-keto acid decarboxylases, benzoylformate decarboxylase and phenylpyruvate decarboxylase, are much less studied. 

The least studied among thiamine pyrophosphate-dependent nonoxidative a-keto acid decarboxylases is phenylpyruvate decarboxylase (EC 4.1.1.43), an enzyme found in Achromobacter auridice [95], Acinetobacter calcoaceticus [81] and the denitrifying bacterium Thauera aromatica [96]. This enzyme participates in catabolic pathways of aro-... 

Like benzoylformate decarboxylase, phenylpyruvate decarboxylase does not demonstrate any immunological similarity to pyruvate decarboxylase [82]. 

Anodier a-keto acid decarboxylase, phenylpyruvate decarboxylase, has been characterized but there are no reports on condensation reactions by this enzyme. 

Table 12.7-1. Time course for the transamination of phenylpyruvate to L-phenylalanine in the presence and absence of oxaloacetate decarboxylase.

Reaction time (min) Transaminase alone Phenylpyruvate (mM) Transaminase Oxaloacetate decarboxylase Phenylpyruvate (mM)... 

Phenyllactic and phenylpyruvic acids have an inhibitory effect on dopa decarboxylase and glutamic decarboxylase activity, but phenylalanine does not. Phenyl-acetic acid in equimolar concentrations had only half the inhibitory power of the two other metabolites. These findings might explain why low-phenylalanine diets restore pigmentation to normal in phenylke-tonuric individuals. 

Phenylpyruvic and phenyllactic acids inhibit glutamic acid decarboxylase in vitro. If the inhibition exists also in vivo, no y-isobutyric acid is produced. This compound seems to play an important role in the brain-blood barrier regulation. 

Aldol condensation Aldehyde 2-Keto aoid Synthesis of 2-hydroxy ketones Pyruvate decarboxylase, benzoyl formate deoarboxylase, phenylpyruvate deoarboxylase... 

PPDC catalyzes in vivo the condensation of phenylpyruvic acid 77 and acetaldehyde 28 for the synthesis of 3-(R)-hydroxy-l-phenyl-2-butanone 78 (Scheme 28.33). This enzyme is the least studied of the decarboxylases however, its uncommon substrate scope makes this enzyme a... 

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