Mechanism of alpha-oxoamine synthases: identification of the intermediate Claisen product in the 8-amino-7-oxononanoate synthase reaction.
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.
Kerbarh
Olivier
O
School of Chemistry, Joseph Black Building, University of Edinburgh, West Mains Road, Edinburgh, UKEH9 3JJ.
Campopiano
Dominic J
DJ
Baxter
Robert L
RL
D000217:Acyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D011732:Pyridoxal Phosphate / Q000378:metabolism
D011732:Pyridoxal Phosphate; D000217:Acyltransferases; C021929:8-amino-7-oxononanoate synthase