Other Biochemistry, Biophysics, and Structural Biology Commons^™

Characterization Of A Fatty Acid Synthetase From Corynebacterium Diphtheriae, Herman W. Knoche, Kirston E. Koths

Department of Biochemistry: Faculty Publications

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.

Palmityl Coenzyme A Inhibition Of Fatty Acid Synthesis, Herman Knoche, Theodore W. Esders, Kirston Koths, Konrad Bloch

Department of Biochemistry: Faculty Publications

The effects of acyl-CoA derivatives (C₈ to C₂₀) on the activity

of the fatty acid synthetases from yeast and Corynebacterium

diphtheriae have been examined. Both enzyme

systems are inhibited by the longer chain acyl thioesters

(C₁₆ to C₂₀) and protected against this inhibition by bovine

serum albumin (BSA). Identical relief from acyl-CoA inhibition

is provided by the 6-0-methylglucose-containing

lipopolysaccharide (MGLP), from Mycobacterium phlei. It

is shown that MGLP forms a stable complex with palmitylCoA.

This interaction accounts for the BSA-like effects of

the polysaccharide. BSA and MGLP have two further effects

on the fatty …