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This paper presents a kinetic study of the transamidinase reaction. The following results have been obtained. 1. The kinetic data are in agreement with a reaction mechanism involving two half-reactions with exclusively binary complexes between substrate and enzyme. 2. The true amidine acceptor is the form of the substrate bearing the unprotonated amino group. This has been demonstrated for hydroxylamine and glycine. 3. k1 and k5 vary as a function of the pH. This variation is related to the dissociation of a group or groups of the enzyme with a pK of approximately pH 8.5.
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Ronca et al. (1966) studied this question.
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