2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	-	-	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	active site structure a catayltic triad of Cys-His-Asn residues	665474	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	active site structure and catalytic reaction mechanism, T97, R46, W42, C122, R161, H258, and N289 are important for activity, structure-function relationship	-, 659493	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	active site structure contains a catalytic triad of His249-Asn279-Cys112 residues	486939	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	active site structure with a CoA/malonyl-ACP-binding channel leading from the enzyme surface to the buried active site Cys residue, a second channel leads from the active site to the surface with a threonine residue controlling the passage of longer acyl chains	665477	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	catalytic reaction mechanism for decarboxylation and condensation	-, 659724	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	catalytic reaction mechanism might include a water molecule or a hydroxyl anion in Cys112 deprotonation, large conformational changes in the active site e.g. through disordering of four essential loops and the movement of the two catalytic residues Cys112 and His244	666011	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	catalytic reaction mechanism via a tetrahedral transition state, active site structure contains an oxyanion hole and a tunnel, catalytic residues are Cys112, His244, and Asn274, which are all required for condensation activity of the enzyme, additionally His244 and Asp274 are required for decarboxylation, Cys112 is essential for transacylation, overview	666950	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	catalytic residues are Cys112, His244, and Asn274, catalytic reaction mechanism includes acetylation of Cys112 in the primer binding pocket, structure and reaction mechanism modeling	665472	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	catalytic residues are Cys123, His323, and Asn353	666668	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	data support a new model for catalysis, in which FabH exists in an open form that permits binding of the long chain acyl-coenzyme A substrate binding and release of the corresponding 3-ketoacyl ACP product. Catalysis and intermediate steps in the process are proposed to occur in a closed form of the mtFabH. These conformational changes may be critical for binding and dissociation steps in other enzymes of the FAS pathways, including transfers between the type I and type II FASII components of Mycobacterium tuberculosis	-, 686049	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	ping pong reaction mechanism, catalysis involves His261, Arg150, and Arg306, determination of substrate binding site	663922	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	ping pong reaction mechanism, catalytically important residues are Phe298 and His238	660466	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	proposed mechanism of condensation reaction in Streptococcus gordonii FabH between catalytic residues His249, Asn279 and Cys112	-, 736659	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	the active site is formed by Ala-Cys-Ala	665464	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	the enzyme catalyzes the Claisen condensation reaction by a ping-pong mechanism	-, 735963	
2.3.1.180	acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	two-stage mechanism, driven by a dipole moment, the active site cysteine, Cys112 in YpFabH attacks the acyl group of a fatty acyl donor, transferring the acyl group to the enzyme. The bound fatty acyl donor molecule is displaced, and the receiving molecule or fatty acyl thioester to be elongated binds, initiating the transfer of the acyl group from the condensing enzyme to the recipient. The remaining residues of the catalytic triad, His243 and Asn273, are thought to stabilise the fatty acyl intermediate during transition states	737251