Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis.
Two activities were found in E. coli extracts which could complement unsaturated fatty acid synthesis of a cerulenin treated E. coli fatty acid synthetase. One of these is beta-ketoacyl-ACP synthase I, but it is not known whether the other activity represents the previously characterized beta-ketoacyl-ACP synthase II. A mutant strain exhibiting a temperature sensitive unsaturated fatty acid synthetic activity apparently lacked an active beta-ketoacyl-ACP synthase I.
Siggaard-Andersen
M
M
Department of Physiology, Carlsberg Laboratory, Copenhagen Valby.
D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000378:metabolism / Q000502:physiology*; D000217:Acyltransferases / Q000502:physiology*; D002569:Cerulenin / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005231:Fatty Acids, Unsaturated / Q000096:biosynthesis*; D009154:Mutation
D005231:Fatty Acids, Unsaturated; D002569:Cerulenin; D000217:Acyltransferases; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase