Beta-ketoacyl-acyl-carrier-protein synthase III
3-Ketoacyl-acyl carrier protein synthase III
Beta-ketoacyl-acyl carrier protein synthase III
Beta-ketoacyl (acyl carrier protein) synthase III
Beta-ketoacyl-[acyl-carrier-protein] synthase III
Acetyl-CoA:malonyl-[acyl-carrier-protein] C-acyltransferase
[Acyl-carrier protein]-decarboxylated malonyl group (Peptidyl-Ser-phosphopantetheine-S-enolate)
Peptidyl-Cys-tetrahedral-acetyl-keto-[acyl-carrier protein]
The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I.
Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis.
Reaction mechanism of recombinant 3-oxoacyl-(acyl-carrier-protein) synthase III from Cuphea wrightii embryo, a fatty acid synthase type II condensing enzyme.
Mechanism of chalcone synthase. pKa of the catalytic cysteine and the role of the conserved histidine in a plant polyketide synthase.
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
beta-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket.
Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III.
Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III.
Refined structures of beta-ketoacyl-acyl carrier protein synthase III.
Crystal structure of the priming beta-ketosynthase from the R1128 polyketide biosynthetic pathway.
First X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling.
A template search reveals mechanistic similarities and differences in beta-ketoacyl synthases (KAS) and related enzymes.
The structural biology of type II fatty acid biosynthesis.
Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity.
Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A.
Crystal structure and substrate specificity of the beta-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus.
The thiolase superfamily: condensing enzymes with diverse reaction specificities.
Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes.
Probing reactivity and substrate specificity of both subunits of the dimeric Mycobacterium tuberculosis FabH using alkyl-CoA disulfide inhibitors and acyl-CoA substrates.
Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH.
Divergent evolution of the thiolase superfamily and chalcone synthase family.
Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
This enzyme belongs to chalcone synthase family in thiolase superfamily (see [21]). This enzyme is homologous to the counterpart enzymes from different bacteria (D00826 and D00867 in EzCatDB), with a slightly different catalytic site. Moreover, these enzymes are categorized in type III of beta-ketoacyl-acyl-carrier protein synthases (KAS). According to the literature, the catalysis proceeds through the Ping-Pong reaction mechanism. According to the literature [2], [3], [5], [9], [10], [14], [15] and [21], this enzyme catalyzes the following reactions: (A) Transfer of acyl group from sulfur atom of acetyl-CoA to catalytic cysteine (see [9]): (A0) Asn274 (of 1d9b) modulate the pKa of His244, whereas His244 may lower the pKa of the sidechain of Cys112. (A1) Asp140 acts as a general base to deprotonate the nucleophile, Cys112, through the sidechain of Ser276. (Helix dipole moment may also activate the cysteine sidechain.) (A2) The activated thiol group of Cys112 makes a nucleophilic attack on the acetyl group of acetyl-CoA, leading to a transition-state (I00132). The oxyanion hole, composed of the mainchain amide groups of Cys112 and Gly306, stabilizes the negative charge of the oxyanion on the tetrahedral transition-state (I00132). (A3) His244 acts as a general acid to protonate the leaving sulfur atom of CoA, generating an acetyl group on Cys112 (I00133). (B) Decarboxylation of malonyl-ACP (Elimination of carboxylate group from malonyl group) forming carbanion/enolate transition-state (I00134): (B0) Asn274 and His244 interact with the carbonyl oxygen of the second substrate, malonyl-ACP, and stabilize it. (B1) His244 may act as a general base to deprotonate the carboxylic group of malonyl-ACP, to facilitate the decarboxylation. This reaction generates a carbanion/enolate transition-state (I00134). The enolate is stabilized by Asn274 and His244. (C) Transfer of acetyl group from catalytic cysteine to carbanion on the transition-state (I00134): (C0) Asn274 and His244 stabilize the enol group of the transition-state (I00134). (C1) The carbanion makes a nucleophilic attack on the acetyl group of the acetyl intermediate (I00133), forming a tetrahedral transition-state (I00135). The oxyanion of the tetrahedral transition-state (I00135) is stabilized by the oxyanion hole composed of the mainchain amide groups of Cys112 and Gly306. (C2) Asp140 may act as a general acid to protonate the leaving catalytic residue, Cys112, through the sidechain of Ser276.