title: Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system.
abstract: Mycobacterium smegmatis extracts contain two fatty acyl synthetase systems (Brindley, D.N., Matsumura, S. and Bloch, K. (1966) Nature 224, 666-669). One is the extensively studied multienzyme complex, (molecular weight 1.39 - 10(6)) which produces shorter C16 and C18) and longer (C24 and higher) fatty acids in a bimodal pattern. The second synthetase is acyl carrier-protein (ACP) dependent and elongates the CoA derivatives of C12 and longer chains. In contrast to the type I synthetase which also extends long fatty acyl chains, the ACP-dependent system produces homologous fatty acids up to 30 carbon atoms long in approximately equal proportions. Other properties which distinguish the ACP-dependent system from the multienzyme complex include the resistance to high concentrations of palmitoyl-CoA and to low ionic strength and the lack of stimulation by mycobacterial polysaccharides. The possibility that the two fatty acid synthetases are complimentary in their function is discussed.
mesh_terms: D000255:Adenosine Triphosphate; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism; D064429:Fatty Acid Synthases / Q000302:isolation & purification / Q000378:metabolism; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium; D009161:Mycobacterium / Q000201:enzymology*; D009243:NAD; D009994:Osmolar Concentration; D010084:Oxidation-Reduction; D013329:Structure-Activity Relationship
chemical_list: D002352:Carrier Proteins; D007527:Isoenzymes; D009243:NAD; D000255:Adenosine Triphosphate; D064429:Fatty Acid Synthases; D008274:Magnesium