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Appl Environ Microbiol. 1972 April; 23(4): 699-703
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Mechanism of Proline Production by Kurthia catenaforma

Department of Applied Biochemistry, Chemical Research Laboratory, Tanabe Seiyaku Co., Ltd., Kashimacho, Higashiyodogawa-ku, Osaka, Japan

ABSTRACT

The fate of aspartic acid used for proline fermentation by Kurthia catenaforma was traced by using aspartic acid-U-¹⁴C. The radioactivities of proline and glutamic acid increased with the disappearance of aspartic acid. After 40 hr, aspartic acid disappeared from the medium and radioactive -ketoglutaric acid was detected. The radioactivity of proline reached 44% of aspartic acid radioactivity at 40 hr. The specific radioactivities of these amino acids and of -ketoglutaric acid supported the notion that proline is produced mainly from aspartic acid via -ketoglutaric acid and glutamic acid. Since the levels of glutamic acid dehydrogenases (EC 1.4.1.2 and EC 1.4.1.4) were low in this organism, it appears that the nitrogen atom of aspartic acid enters proline by the action of aspartate aminotransferase (EC 2.6.1.1). The mechanism of proline production is discussed on the basis of the role of aspartic acid in this fermentation.