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

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Abstract

Pyridoxal 5′-phosphate is a coenzyme for a number of enzymes which catalyse reactions at Cα 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-α-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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  1. Department of Chemistry, The Purdie Building, The University, KY16 9ST, St. Andrews, Fife, Scotland

    D. M. Smith, N. R. Thomas & D. Gani

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  1. D. M. Smith
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Much of the work described here was undertaken in the Chemistry Department at Southhampton University prior to our move to St. Andrews.

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Smith, D.M., Thomas, N.R. & Gani, D. A comparison of pyridoxal 5′-phosphate dependent decarboxylase and transaminase enzymes at a molecular level. Experientia 47, 1104–1118 (1991). https://doi.org/10.1007/BF01918374

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