Date of this Version
The Journal of Biological Chemistry, Vol. 248, No. 10, Issue of May 25, pp. 3517-3519, 1973
A fatty acid synthetase from Corynebacterium diphtheriae has been purified to a specific activity of 450 nmoles of malonyl coenzyme A incorporated per min per mg. The enzyme is optimally active in 0.5 M phosphate buffer. C. diphtheriae appears to be the most primitive organism having a multienzyme complex for fatty acid synthesis.