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Interplay of organic and biological chemistry in understanding coenzyme mechanisms: example of thiamin diphosphate‐dependent decarboxylations of 2‐oxo acids
Author(s) -
Jordan Frank
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01061-3
Subject(s) - chemistry , decarboxylation , oxidative decarboxylation , cofactor , coenzyme a , enzyme , mechanism (biology) , enzyme catalysis , oxidative phosphorylation , catalysis , biochemistry , reductase , philosophy , epistemology
With the publication of the three‐dimensional structures of several thiamin diphosphate‐dependent enzymes, the chemical mechanism of their non‐oxidative and oxidative decarboxylation reactions is better understood. Chemical models for these reactions serve a useful purpose to help evaluate the additional catalytic rate acceleration provided by the protein component. The ability to generate, and spectroscopically observe, the two key zwitterionic intermediates invoked in such reactions allowed progress to be made in elucidating the rates and mechanisms of the elementary steps leading to and from these intermediates. The need remains to develop chemical models, which accurately reflect the enzyme‐bound conformation of this coenzyme.