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・ Beta-globin co-transcriptional cleavage ribozyme
・ Beta-glucan
・ Beta-glucan-transporting ATPase
・ Beta-glucogallin O-galloyltransferase
・ Beta-glucogallin—tetrakisgalloylglucose O-galloyltransferase
・ Beta-glucosidase
・ Beta-glucoside kinase
・ Beta-glucuronidase
・ Beta-Hexachlorocyclohexane
・ Beta-Hydride elimination
・ Beta-Hydroxy beta-methylbutyric acid
・ Beta-Hydroxybutyric acid
・ Beta-Hydroxybutyryl-CoA
・ Beta-keratin
・ Beta-ketoacyl-(acyl-carrier-protein) synthase III
Beta-ketoacyl-ACP synthase
・ Beta-ketoacyl-acyl-carrier-protein synthase I
・ Beta-ketoacyl-acyl-carrier-protein synthase II
・ Beta-ketodecanoyl-(acyl-carrier-protein) synthase
・ Beta-ketothiolase deficiency
・ Beta-L-arabinosidase
・ Beta-L-rhamnosidase
・ Beta-lactam Ring Records
・ Beta-lactamase
・ Beta-lactamase inhibitor protein
・ Beta-lactoglobulin
・ Beta-Lysine
・ Beta-lysine 5,6-aminomutase
・ Beta-Lytic metalloendopeptidase
・ Beta-M


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Beta-ketoacyl-ACP synthase : ウィキペディア英語版
Beta-ketoacyl-ACP synthase

In molecular biology, Beta-ketoacyl-ACP synthase , is an enzyme involved in fatty acid synthesis. It results in the formation of acetoacetyl ACP.
It is the enzyme that catalyses the condensation of malonyl-ACP with the growing fatty acid chain. It is found as a component of a number of enzymatic systems, including fatty acid synthetase (FAS), which catalyses the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH; the multi-functional 6-methysalicylic acid synthase (MSAS) from ''Penicillium patulum'', which is involved in the biosynthesis of a polyketide antibiotic; polyketide antibiotic synthase enzyme systems; ''Emericella nidulans'' multifunctional protein Wa, which is involved in the biosynthesis of conidial green pigment; ''Rhizobium'' nodulation protein nodE, which probably acts as a beta-ketoacyl synthase in the synthesis of the nodulation Nod factor fatty acyl chain; and yeast mitochondrial protein CEM1. The condensation reaction is a two-step process: first the acyl component of an activated acyl primer is transferred to a cysteine residue of the enzyme and is then condensed with an activated malonyl donor with the concomitant release of carbon dioxide.
Beta-ketoacyl synthase contains two protein domains. The active site is located between the N- and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine. Residues from both domains contribute to substrate binding and catalysis〔 〕
==See also==

* 3-oxoacyl-(acyl-carrier-protein) reductase

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