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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
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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
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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
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
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
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic reaction mechanism for decarboxylation and condensation
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
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
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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
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic residues are Cys123, His323, and Asn353
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
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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
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
the active site is formed by Ala-Cys-Ala
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
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
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
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
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
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
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
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
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
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
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
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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
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acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2
catalytic reaction mechanism for decarboxylation and condensation
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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
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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
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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
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