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Review
. 1991 Dec 1;47(11-12):1104-18.
doi: 10.1007/BF01918374.

A comparison of pyridoxal 5'-phosphate dependent decarboxylase and transaminase enzymes at a molecular level

D M Smith  1 , N R Thomas, D Gani
Affiliations
Review

A comparison of pyridoxal 5'-phosphate dependent decarboxylase and transaminase enzymes at a molecular level

D M Smith et al. Experientia. .

Abstract

Pyridoxal 5'-phosphate is a coenzyme for a number of enzymes which catalyse reactions at C alpha of amino acid substrates including transaminases, decarboxylases and serine hydroxymethyltransferase. Using the X-ray coordinates for a transaminase, aspartate aminotransferase, and the results of stereochemical and mechanistic studies for decarboxylases and serine hydroxymethyltransferase, an active-site structure for the decarboxylase group is constructed. The structure of the active-site is further refined through active-site pyridoxyllysine peptide sequence comparison and a 3-D catalytic mechanism for the L-alpha-amino acid decarboxylases is proposed. The chemistry of serine hydroxymethyltransferase is re-examined in the light of the proposed decarboxylase mechanism.

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