title: Aldolase activity of serum albumins.
abstract: Bovine and human serum albumins catalyze the aldol reaction of aromatic aldehyedes and acetone, with saturation kinetics and moderate and opposite enantioselectivity. The reaction occurs at the binding site in domain IIa, and is inhibited by warfarin. Kinetic data are consistent with an enamine mechanism. The activity is conserved in a 103 aminoacid peptide derived from the albumin sequence.
authors.affiliation: Department of Chemical and Pharmaceutical Sciences, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.
authors.forename: Fabio
authors.initials: F
authors.lastname: Benedetti
authors.forename: Federico
authors.initials: F
authors.lastname: Berti
authors.forename: Silvia
authors.initials: S
authors.lastname: Bidoggia
mesh_terms: D000096:Acetone / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002384:Catalysis / Q000187:drug effects; D002417:Cattle; D002625:Chemistry, Organic; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D012996:Solutions; D013237:Stereoisomerism; D014859:Warfarin / Q000494:pharmacology
chemical_list: D000447:Aldehydes; D012709:Serum Albumin; D012996:Solutions; D000096:Acetone; D014859:Warfarin; D005634:Fructose-Bisphosphate Aldolase