Enzymatic Racemization of Leucine and α-Aminobutyrate

Part III. Properties of Partially Purified Racemase

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.