Localization of the sulfur-cyanolysis site of serum albumin to subdomain 3-AB.
The results of kinetic experiments measuring the effects of a variety of ligands on the sulfur-cyanolysis reaction catalyzed by serum albumin point to the conclusion that the active site for cyanolysis is on subdomain 3-AB. Relationships among the inhibition by short-chain fatty acids, the activation by p-nitrophenyl acetate, and the influence of bilirubin and L-tryptophan on these effects indicate that the cyanolysis active site and the known primary binding site for indoles are both near, but on opposite sides of, tyrosine-409 of bovine albumin (tyrosine-411 of human albumin).
Jarabak
R
R
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.
Westley
J
J
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002417:Cattle; D003486:Cyanides / Q000378:metabolism* / Q000493:pharmacokinetics; D006801:Humans; D008658:Inactivation, Metabolic; D007211:Indoles / Q000378:metabolism; D007700:Kinetics; D012709:Serum Albumin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013455:Sulfur / Q000378:metabolism*; D014364:Tryptophan / Q000378:metabolism
D003486:Cyanides; D007211:Indoles; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D013455:Sulfur; C015292:indolepropionic acid; D014364:Tryptophan