Active-Site Titration of Pig-Plasma Benzylamine Oxidase

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Abstract
Titration of benzylamine oxidase (EC 1.4.3.6) with benzylamine under anaerobic conditions shows that full reduction of the enzymic 470 nm chromophore is obtained on the addition of 1 mol of substrate/mol of enzyme. Concomitantly, 1 mol of benzaldehyde/mol of enzyme is produced. A single prosthetic group interacting with carbonyl reagents can be detected on titration of benzylamine oxidase with phenylhydrazine. Titration data reported to indicate a higher content of porsthetic groups were obtained under conditions where equilibration between enzyme and phenylhydrazine is insufficently complete. Pig plasma benzylamine oxidase apparently contains a single catalytically active site. The 2 Cu atoms present in the enzyme may be structurally or functionally different.