Purification and characterization of the fatty acid synthase from Bugula neritina.
The fatty acid synthase from Bugula neritina has been purified 100-fold using ammonium sulfate precipitation, ion-exchange and size exclusion chromatography. The purified enzyme has a molecular weight of approximately 382,000 Da, as judged by gel filtration. Polyacrylamide gel electrophoresis under denaturing conditions in the presence of SDS revealed one major protein band of approximately 190,000 Da suggesting that the enzyme is a homodimer. The size of the enzyme, together with the observation that the FAS activity is independent of the concentration of acyl carrier protein, indicate that the FAS from Bugula neritina is a type I. A detailed analysis of the products of the purified FAS indicated that palmitic acid is the primary product and longer chain fatty acids are not produced.
Department of Chemistry and Biochemistry, Center for Molecular Biology and Biotechnology, Florida Atlantic University, 777 Glades Road, Boca Raton, FL 33431-0991, USA.
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Kerr
D000105:Acetyl Coenzyme A / Q000378:metabolism; D000818:Animals; D002013:Bryozoa / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D064429:Fatty Acid Synthases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008316:Malonyl Coenzyme A / Q000378:metabolism; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D013379:Substrate Specificity
D009243:NAD; D008316:Malonyl Coenzyme A; D009249:NADP; D000105:Acetyl Coenzyme A; D064429:Fatty Acid Synthases