[Pyruvate decarboxylase: mechanistic model of paracatalytic interactions].
The recent data from literature concerning mechanisms of nonenzymic and enzymic thiamine diphosphate-dependent catalysis have been analyzed. The application of model nonenzymic quinone, molecular oxygen and ferricyanide oxidation of 2-(l-hydroxyethyl)- and 2-(l-hydroxybenzyl)thiazole ions to catalysis by thiamin diphosphate-dependent enzymes especially pyruvate decarboxylase are summarized in this review. Mechanisms of paracatalytic interactions of pyruvate decarboxylase and possibility of biocatalyst design to change reaction specificity of the enzyme have been discussed.
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D000079:Acetaldehyde / Q000737:chemistry; D002384:Catalysis; D005292:Ferricyanides / Q000737:chemistry; D008956:Models, Chemical; D010084:Oxidation-Reduction; D011767:Pyruvate Decarboxylase / Q000737:chemistry* / Q000378:metabolism; D011809:Quinones / Q000737:chemistry
D005292:Ferricyanides; D011809:Quinones; D011767:Pyruvate Decarboxylase; D000079:Acetaldehyde