Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Enzymatic Racemization of Leucine and α-Aminobutyrate
Part III. Properties of Partially Purified Racemase
Takaharu OSUMITatsuo YAMAMOTOKenji SODA
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1969 Volume 33 Issue 3 Pages 430-435

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Abstract

A new amino acid racemase catalyzing the conversion of either D or L enantiomorph of leucine and α-aminobutyrate to the racemates, was partially purified from the cell-free extract of Pseudomonas striata. Both the racemase reactions are suggested to be catalyzed by a single enzyme because of the constant ratio between the activities during the purification, and of their very resemble behavior to pH, temperature and heating the enzyme. Pyridoxal phosphate functions as the coenzyme for this racemase.

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