Structure/function studies on enzymes in the diaminopimelate pathway of bacterial cell wall biosynthesis

Curr Opin Chem Biol. 1999 Oct;3(5):607-13. doi: 10.1016/s1367-5931(99)00016-2.

Abstract

Within the past 18 months work has continued on the structure and mechanisms of enzymes involved in the diaminopimelic acid/lysine biosynthetic pathway. A novel structure has been determined for a PLP-independent epimerase, and structures with bound substrates have been solved for two other enzymes. Additionally, new studies have appeared describing the chemical mechanisms of three enzymes in the pathway.

Publication types

  • Review

MeSH terms

  • Acyltransferases / metabolism*
  • Amidohydrolases / metabolism*
  • Amino Acid Isomerases / metabolism*
  • Amino Acid Oxidoreductases / metabolism*
  • Cell Wall / metabolism*
  • Diaminopimelic Acid / metabolism*
  • Models, Chemical
  • Models, Molecular
  • Structure-Activity Relationship
  • Succinyldiaminopimelate Transaminase
  • Transaminases / metabolism*

Substances

  • Diaminopimelic Acid
  • Amino Acid Oxidoreductases
  • diaminopimelate dehydrogenase
  • Acyltransferases
  • succinyl-CoA-tetrahydrodipicolinate N-succinyltransferase
  • Transaminases
  • Succinyldiaminopimelate Transaminase
  • Amidohydrolases
  • succinyldiaminopimelate desuccinylase
  • Amino Acid Isomerases
  • diaminopimelate epimerase