oxalyl-coenzyme-a and phenylglyoxylic-acid

Thiamin diphosphate (ThDP) is the biologically active form of vitamin B(1), and ThDP-dependent enzymes are found in all forms of life. The catalytic mechanism of this family requires the formation of a common intermediate, the 2α-carbanion-enamine, regardless of whether the enzyme is involved in C-C bond formation or breakdown, or even formation of C-N, C-O and C-S bonds. This demands that the enzymes must screen substrates prior to, and/or after, formation of the common intermediate. This review is focused on the group for which the second step is the protonation of the 2α-carbanion, i.e., the ThDP-dependent decarboxylases. Based on kinetic data, sequence/structure alignments and mutagenesis studies the factors involved in substrate specificity have been identified.

Topics: Acyl Coenzyme A; Bacteria; Carboxy-Lyases; Catalytic Domain; Glyoxylates; Mandelic Acids; Mutagenesis, Site-Directed; Pyruvic Acid; Saccharomyces cerevisiae; Substrate Specificity; Thiamine Pyrophosphate