Experientia

, Volume 47, Issue 11–12, pp 1104–1118 | Cite as

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

  • D. M. Smith
  • N. R. Thomas
  • D. Gani
Multi-Author Review Molecular Recognition

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.

Key words

Transaminase decarboxylase serine hydroxymethyltransferase pyridoxal 5′-phosphate enzyme mechanism stereochemistry kinetics 
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Copyright information

© Birkhäuser Verlag Basel 1991

Authors and Affiliations

  • D. M. Smith
    • 1
  • N. R. Thomas
    • 1
  • D. Gani
    • 1
  1. 1.Department of ChemistryThe Purdie Building, The UniversitySt. Andrews(Scotland)

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