Pyridoxal Phosphate in Enzymatic and Non-Enzymatic Catalysis

Authors

  • M. Markova Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague
  • B. Kralova Department of Biochemistry and Microbiology, Institute of Chemical Technology, Prague

Abstract

This review covers recent results on the ability of pyridoxal phosphate, either alone or as an enzyme cofactor of enzymes, to catalyze reactions with amino acids. Although pyridoxal phosphate catalyzes many different reactions in water solutions, its reaction specificity is quite poor. In biological systems, both reaction and substrate specificity is determined by apoenzymes. So far, more than twenty structures of pyridoxal 5´-phosphate-dependent enzymes have been solved. Most of them are evolutionarily related to aspartate aminotransferase. On the basis of structure motifs, they have been divided into four families with aspartate aminotransferase, tryptophan synthase, D-amino acid transferase and alanine racemase as representatives. A remarkable convergent evolution is observed in two fold types with a similar cofactor binding and reaction mechanism.

Published

2004-03-15

How to Cite

Markova, M., & Kralova, B. (2004). Pyridoxal Phosphate in Enzymatic and Non-Enzymatic Catalysis. Chemické Listy, 98(2). Retrieved from http://chemicke-listy.cz/ojs3/index.php/chemicke-listy/article/view/2163

Issue

Section

Articles