2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] - - 2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] mechanism, formation of a malonyl-enzyme intermediate 486863, 486864, 486881, 486882 2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] isolation and characterization of an enzyme-intermediate 486882, 486883 2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] mechanism, kinetic studies 486886, 486891 2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] putative active site structure and involved catalytic residues 661061 2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] catalytic mechanism, [acyl-carrier protein] binding site, residues Phe200 and Met126 are involved 663400 2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] the catalytic malonyl transferase activity is intrinsic to an individual acyl carrier protein. An arginine/lysine in loop II and an arginine/glutamine in helix III are the catalytic residues for transferase function. The hydrogen bonding properties of these residues are indespensible for the transferase reaction 705648 2.3.1.39 malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] residues Arg113, Ser88 and His188 constitute the enzyme's catalytic triad, catalytic mechanism, detailed overview. Malonyl-CoA binds to MCAT, involving Ser88, Arg113, Met117 and Phe187. The second step forming an ACP-MCAT-malonyl intermediate is rate-limiting instead of the malonyl-CoA-MCAT intermediate formed in the first step. His87, Arg113 and Ser88 render different contributions for the two intermediates 735606