title: Structural and biochemical analyses reveal how ornithine acetyl transferase binds acidic and basic amino acid substrates.
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.
authors.affiliation: Chemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
authors.forename: Aman
authors.initials: A
authors.lastname: Iqbal
authors.forename: Ian J
authors.initials: IJ
authors.lastname: Clifton
authors.forename: Rasheduzzaman
authors.initials: R
authors.lastname: Chowdhury
authors.forename: David
authors.initials: D
authors.lastname: Ivison
authors.forename: Carmen
authors.initials: C
authors.lastname: Domene
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Schofield
mesh_terms: D000123:Acetyltransferases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D018698:Glutamic Acid / Q000378:metabolism; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009952:Ornithine / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D018698:Glutamic Acid; D009952:Ornithine; D000123:Acetyltransferases; C020646:glutamate acetyltransferase