EC Number |
General Information |
Reference |
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2.3.1.179 | evolution |
the enzyme protein contains conserved domains of KAS-I and II, elongating condensing enzymes, condensing enzymes superfamily, and 3-oxoacyl-[ACP] synthase II. Comparisons of Elaeis oleifera and Elaeis guineensis enzymes, overview |
736673 |
2.3.1.179 | malfunction |
endogenous H2O2 (mainly produced by pyruvate oxidase) inhibits FabF activity by specifically oxidizing its active site cysteine-thiol residue |
711299 |
2.3.1.179 | malfunction |
KASII inhibition does not significantly influence the wax ester and triacylglycerol levels in the plant, but the the C16/C18 ratio is significantly increased in total lipid extracts of leaf tissue when KASIIRNAi-3 is expressed with or without wax ester biosynthesis gene |
737248 |
2.3.1.179 | metabolism |
enzyme overexpression increases pinocembrin production in recombinant Escherichia coli |
757353 |
2.3.1.179 | metabolism |
KAS-II enzyme catalyzes the elongation of C16:0-ACP to C18:0-ACP in plastidial fatty acid biosynthesis pathway |
736673 |
2.3.1.179 | metabolism |
rate-limiting KAS-II enzyme catalyzes the elongation of C16:0-ACP to C18:0-ACP in plastidial fatty acid biosynthesis pathway |
736673 |
2.3.1.179 | metabolism |
the beta-ketoacyl-acyl carrier protein (ACP) synthases, FabB, FabF, and FabH, catalyse the Claisen condensation of fatty acyl-thioesters and malonyl-ACP to form a 3-oxoacyl-ACP intermediate elongated by two carbon atoms. The initial cycle of elongation is catalysed by FabH, involving condensation of malonyl-ACP and acetyl-CoA, while subsequent cycles of elongation are performed by FabB or FabF |
737251 |
2.3.1.179 | metabolism |
the enzyme is involved in fatty-acid biosynthesis |
735397 |
2.3.1.179 | more |
active site structure of wild-type and mutant enzymes, ligand binding structures, overview |
735397 |
2.3.1.179 | more |
enzyme structure and active site architecture, comparison with FabH, EC 2.3.1.180. Substrate binding is controlled by residue Phe401 |
737251 |