Active-site titration of pig-plasma benzylamine oxidase.
1. Titration of benzylamine oxidase with benzylamine under anaerobic conditions shows that full reduction of the enzymic 470-nm chromophore is obtained on the addition of one mole of substrate per mole of enzyme. Concomitantly, one mole of benzaldehyde per mole of enzyme is produced. 2. 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 prosthetic groups were obtained under conditions where equilibration between enzyme and phenylhydrazine is insufficiently complete. 3. It is concluded that pig-plasma benzylamine oxidase contains a single catalytically active site. This means that the two copper atoms present in the enzyme may be structurally or functionally different.
D000693:Anaerobiosis; D000818:Animals; D001595:Benzylamine Oxidase / Q000097:blood; D001596:Benzylamines; D001665:Binding Sites; D003300:Copper / Q000032:analysis; D007700:Kinetics; D008995:Monoamine Oxidase / Q000097:blood; D010659:Phenylhydrazines; D013053:Spectrophotometry; D013552:Swine
D001596:Benzylamines; D010659:Phenylhydrazines; D003300:Copper; D001595:Benzylamine Oxidase; D008995:Monoamine Oxidase