A snapshot of carnitine acetyltransferase

Rona Ruth Ramsay, James Henderson Naismith

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

Carnitine acetyltransferase (CrAT) is part of the carnitine system that protects the acylation state of the pools of acetyl-coenzyme A, a key metabolic intermediate, by transferring excess acetate and other short-chain acyl groups to and from carnitine. The homology of CrAT with other carnitine acyltransferases, such as carnitine palmitoyltransferase I (CPT-1) that regulates fatty acid metabolism, make the solving of its structure a landmark in understanding mechanism and ligand binding in this family.

Original languageEnglish
Pages (from-to)343-346
Number of pages4
JournalTrends in Biochemical Sciences
Volume28
Issue number7
DOIs
Publication statusPublished - Jul 2003

Keywords

  • TRANSITION-STATE STABILIZATION
  • CATALYTIC MECHANISM
  • CRYSTAL-STRUCTURE
  • ACYLTRANSFERASES
  • PALMITOYLTRANSFERASE
  • ENZYMOLOGY
  • TRANSPORT
  • BINDING
  • ACID

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