Structure, evolution and action of vitamin B6-dependent enzymes

Curr Opin Struct Biol. 1998 Dec;8(6):759-69. doi: 10.1016/s0959-440x(98)80096-1.

Abstract

The number of known three-dimensional structures of vitamin B6-dependent enzymes has doubled in the past two years. A fourth type of fold for B6-dependent enzymes, involving a TIM-barrel domain, has been discovered. Alanine racemase is the first known representative of this new fold. Significant progress has been made in understanding the allosteric effects in the tryptophan synthase reaction.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alanine Racemase / chemistry*
  • Alanine Racemase / metabolism
  • Alanine Transaminase / chemistry*
  • Alanine Transaminase / metabolism
  • Aspartate Aminotransferases / chemistry*
  • Aspartate Aminotransferases / metabolism
  • D-Alanine Transaminase
  • Models, Molecular
  • Protein Conformation
  • Pyridoxine / metabolism*
  • Tryptophan Synthase / chemistry*
  • Tryptophan Synthase / metabolism

Substances

  • Aspartate Aminotransferases
  • Alanine Transaminase
  • D-Alanine Transaminase
  • Tryptophan Synthase
  • Alanine Racemase
  • Pyridoxine