Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates

Aman Iqbal, Ian. J. Clifton, Rasheduzzaman Chowdhury, David Ivison, Carmen Domene, Christopher J. Schofield*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Structural and biochemical analyses reveal how ornithine acetyl-transferases catalyse the reversible transfer of an acetyl-group from a basic (ornithine) to an acidic (glutamate) amino acid by employing a common mechanism involving an acetyl-enzyme intermediate but using different side chain binding modes.

Original languageEnglish
Pages (from-to)6219-6225
Number of pages7
JournalOrganic & biomolecular chemistry
Volume9
Issue number18
Early online date28 Jul 2011
DOIs
Publication statusPublished - 21 Sept 2011

Keywords

  • SERINE-PROTEASE CATALYSIS
  • ACYL-ENZYME COMPLEX
  • CRYSTAL-STRUCTURE
  • GENE-CLUSTER
  • ACETYLTRANSFERASE
  • INTERMEDIATE
  • MECHANISM

Fingerprint

Dive into the research topics of 'Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates'. Together they form a unique fingerprint.

Cite this