Controlling reaction specificity in pyridoxal phosphate enzymes

Michael D. Toney

Research output: Contribution to journalArticle

80 Citations (Scopus)

Abstract

Pyridoxal 5′-phosphate enzymes are ubiquitous in the nitrogen metabolism of all organisms. They catalyze a wide variety of reactions including racemization, transamination, decarboxylation, elimination, retro-aldol cleavage, Claisen condensation, and others on substrates containing an amino group, most commonly α-amino acids. The wide variety of reactions catalyzed by PLP enzymes is enabled by the ability of the covalent aldimine intermediate formed between substrate and PLP to stabilize carbanionic intermediates at Cα of the substrate. This review attempts to summarize the mechanisms by which reaction specificity can be achieved in PLP enzymes by focusing on three aspects of these reactions: stereoelectronic effects, protonation state of the external aldimine intermediate, and interaction of the carbanionic intermediate with the protein side chains present in the active site. This article is part of a Special Issue entitled: Pyridoxal Phosphate Enzymology.

Original languageEnglish (US)
Pages (from-to)1407-1418
Number of pages12
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1814
Issue number11
DOIs
StatePublished - Nov 2011

Fingerprint

Pyridoxal Phosphate
Substrates
Enzymes
Decarboxylation
Protonation
Metabolism
Condensation
Catalytic Domain
Nitrogen
Amino Acids
Proteins

Keywords

  • Pyridoxal phosphate
  • Reaction specificity
  • Stereoelectronic effect
  • Vitamin B6

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Analytical Chemistry
  • Molecular Biology

Cite this

Controlling reaction specificity in pyridoxal phosphate enzymes. / Toney, Michael D.

In: Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1814, No. 11, 11.2011, p. 1407-1418.

Research output: Contribution to journalArticle

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