title: Mechanism of alpha-oxoamine synthases: identification of the intermediate Claisen product in the 8-amino-7-oxononanoate synthase reaction.
abstract: The reactive beta-ketoacid pyridoxal-5'-phosphate aldimine formed in the condensation step of the 8-amino-7-oxononanoate synthase reaction was 'trapped' in the enzyme-bound form by carrying out the reaction with l-alanine methyl ester and pimeloyl-CoA affording the more stable methyl ester of the putative intermediate, the characterisation of which provides the first definitive evidence for a beta-ketoacid intermediate in an alpha-oxamine synthase mechanism.
authors.affiliation: School of Chemistry, Joseph Black Building, University of Edinburgh, West Mains Road, Edinburgh, UKEH9 3JJ.
authors.forename: Olivier
authors.initials: O
authors.lastname: Kerbarh
authors.forename: Dominic J
authors.initials: DJ
authors.lastname: Campopiano
authors.forename: Robert L
authors.initials: RL
authors.lastname: Baxter
mesh_terms: D000217:Acyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D011732:Pyridoxal Phosphate / Q000378:metabolism
chemical_list: D011732:Pyridoxal Phosphate; D000217:Acyltransferases; C021929:8-amino-7-oxononanoate synthase