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Journal of Lipid Research, Vol. 3, 243-245, April 1962
Copyright © 1962 by Lipid Research, Inc.

Stereospecific reduction of crotonyl coenzyme A

Joseph D. Robinson , Roscoe O. Brady , and Charles R. Maxwell

Laboratory of Neurochemistry, National Institute of Neurological Diseases and Blindness; and Radiation Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland

An enzyme preparation obtained from brain tissue catalyzes the stereospecific reduction of crotonyl CoA to butyrate. Tritium from TPNH³ was localized predominantly on the ßbeta;-carbon of recovered butyric acid. Both this enzyme and a preparation from adipose tissue, which also catalyzes the reduction of crotonyl CoA, catalyze the synthesis of long-chain fatty acids from malonyl CoA and acetyl CoA. The significance of these findings is considered in view of the demonstration that, in long-chain fatty acids synthesized in the presence of TPNH³, labeled hydrogen is localized on alternate carbon atoms beginning with the ßbeta;-carbon.

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