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Author Osumi, Takaharu ♦ Yamamoto, Tatsuo ♦ Soda, Kenji
Source J-STAGE
Content type Text
Publisher Japan Society for Bioscience, Biotechnology, and Agrochemistry
Language English
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.
ISSN 00021369
Learning Resource Type Article
Publisher Date 1969-01-01
e-ISSN 18811280
Journal Agricultural and Biological Chemistry(bbb1961)
Volume Number 33
Issue Number 3
Page Count 6
Starting Page 430
Ending Page 435


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