Abstract
Transaminase reaction between l-Iysine and α-ketoglutaric acid was found in the cell-free extracts of Flavobacterium fuscum, Fl. flavescens and Achrolnobacter liquidum. The transaminase in the extract of Fl. fuscum was partially purified and some properties were investigated. The formation of glutamic acid proceeded stoichiometrically with disappearance of the substrates by transamination. d-Lysine and pyruvic acid, phenylpyruvic acid or oxaloacetic acid could not participate in this reaction as an amino donor and an amino acceptor, respectively. The activity of the transaminase was inhibited by addition of penicillamine. As the keto analogue of l-lysine did not react with 2,4-dinitrophenylhydrazine to form a hydrazone, but reacted with o-aminobenzaldehyde and p-dimethylaminobenzaldehyde to produce respectively unique color, it was suggested that the keto analogue was present in a fom of a cyclic compound containing a piperidine ring.
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