Interaction of the Lathyrogen Beta-Aminopropionitrile (BAPN) with a Copper-Containing Amine Oxidase.

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Abstract
Pig plasma amine oxidase, an enzyme thought to closely resemble the oxidase functional in collagen and elastin crosslinking, was assayed in the presence of a lathyrogen. BAPN [beta-aminopropionitrile] was shown to inhibit enzyme activity competitively and reversibly and to form a complex with the active site of the enzyme. The product of the enzymatic oxidative deamination of BAPN was isolated and partially characterized. Its properties indicate the existence of a highly reactive aldehyde intermediate in BAPN metabolism. The data presented suggest 2 likely alternatives for the mechanism of action of BAPN. BAPN may compete with native substrate molecules for the active site of the amine oxidase functional in crosslinking, or BAPN or a highly reactive aldehyde derived from BAPN by the action of amine oxidase may react with the functional groups of strategic lysyl side chains of collagen and elastin and block enzyme activity and crosslink formation.

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