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

Timothy L. Born, John S. Blanchard

Research output: Contribution to journalReview article

68 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)607-613
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume3
Issue number5
DOIs
StatePublished - Oct 1 1999

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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