A Catalytic Mechanism for the Enzyme Benzylamine Oxidase from Pig Plasma

Overview

Journal Biochem J

Specialty Biochemistry

Date 1972 Dec 1

PMID 4664929

Citations 6

Authors

C E Taylor

R S Taylor

C Rasmussen

P F Knowles

Affiliations

Soon will be listed here.

Abstract

Initial-velocity and product-inhibition studies on the enzyme benzylamine oxidase from pig plasma indicate that the order of substrate addition and product release is benzylamine on, ammonia off, oxygen on, hydrogen peroxide off, benzaldehyde off. Ammonia, but not benzaldehyde, is released under strictly anaerobic conditions which provides independent evidence for this order. Benzyl alcohol is a substrate for the enzyme. A chemical mechanism consistent with all the data is proposed.

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Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine....

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Properties of cupric ions in benzylamine oxidase from pig plasma as studied by magnetic-resonance and kinetic methods.

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