Reaction of aortic lysyl oxidase with beta-aminopropionitrile.

摘要: beta-Aminopropionitrile (BAPN) is a potent irreversible inhibitor of lysyl oxidase, the enzyme which initiates cross-linkage formation in elastin and collagen. The initial interaction BAPN with aortic oxidase competitive or alkyl amine substrates. Irreversible inhibition develops time- temperature-dependent fashion upon incubation absence substrate limiting inactivation rate constant 0.16 min-1 KI 6 microM at 37 degrees C. labeled carbons [1,2-14C]BAPN [3-14C]BAPN covalently bind to equivalent extents parallel development inactivation, negating possibility that nitrile moiety eliminated from by enzymatic action. copper content not significantly altered BAPN. extent labeling [14C]BAPN reduced prior treatment carbonyl-modifying reagents, suggesting enzyme-inhibitor Schiff base formation. However, processed free aldehyde product oxidase. A mechanism postulated involves covalent bond between an nucleophile ketenimine formed enzyme-assisted beta-proton abstraction.