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Substrate specificity in thiamin diphosphate-dependent decarboxylases

Authors
Journal
Bioorganic Chemistry
0045-2068
Publisher
Elsevier
Volume
43
Identifiers
DOI: 10.1016/j.bioorg.2011.12.001
Keywords
  • Thiamin-Diphosphate
  • Pyruvate
  • Benzoylformate
  • Mutagenesis
  • Carboligation
Disciplines
  • Biology

Abstract

Abstract Thiamin diphosphate (ThDP) is the biologically active form of vitamin B1, 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.

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