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3‑Oxoacyl-[acyl-carrier-protein] synthase I (KAS I or FabB) is a key enzyme in type II fatty acid synthesis (FAS II), catalyzing the condensation reaction that elongates fatty acid chains by adding two carbons from malonyl-ACP to an acyl-ACP substrate. This process is essential for the biosynthesis of long-chain fatty acids, critical for cell membranes and energy storage. It is a homodimeric protein using a conserved catalytic triad—His-His-Cys.
Cerulenin covalently binds to the active site cysteine residue, blocking enzymatic activity
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