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3-oxoacyl-[acyl-carrier-protein] synthase III C-terminal domain-containing protein
This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.41, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria. [1]. 10600651. Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme. Abbadi A, Brummel M, Schutt BS, Slabaugh MB, Schuch R, Spener F;. Biochem J 2000;345:153-160. (from Pfam)
FAE1/Type III polyketide synthase-like protein
The members of this family are described as 3-ketoacyl-CoA synthases, type III polyketide synthases, fatty acid elongases and fatty acid condensing enzymes, and are found in both prokaryotic and eukaryotic (mainly plant) species. The region featured in this family contains the active site residues, as well as motifs involved in substrate binding [1]. [1]. 12139488. Alteration of reaction and substrate specificity of a bacterial type III polyketide synthase by site-directed mutagenesis. Funa N, Ohnishi Y, Ebizuka Y, Horinouchi S;. Biochem J 2002;367:781-789. (from Pfam)
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III
This domain is found on 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III EC:2.3.1.180, the enzyme responsible for initiating the chain of reactions of the fatty acid synthase in plants and bacteria. [1]. 10600651. Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme. Abbadi A, Brummel M, Schutt BS, Slabaugh MB, Schuch R, Spener F;. Biochem J 2000;345:153-160. (from Pfam)
Thiolase, N-terminal domain
Thiolase is reported to be structurally related to beta-ketoacyl synthase (Pfam:PF00109), and also chalcone synthase. [1]. 9402066. The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. Mathieu M, Modis Y, Zeelen JP, Engel CK, Abagyan RA, Ahlberg A, Rasmussen B, Lamzin VS, Kunau WH, Wierenga RK;. J Mol Biol 1997;273:714-728. (from Pfam)
beta-ketoacyl-ACP synthase 3
beta-ketoacyl-ACP synthase III
beta-ketoacyl-[acyl-carrier-protein] synthase 3 initiates the elongation in type II fatty acid synthase by specifically using acetyl-CoA over acyl-CoA
FabH in general initiate elongation in type II fatty acid synthase systems found in bacteria and plants. The two members of this subfamily from Bacillus subtilis differ from each other, and from FabH from E. coli, in acyl group specificity. Active site residues include Cys112, His244 and Asn274 of E. coli FabH. Cys-112 is the site of acyl group attachment.
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