EC Number   |
Reaction |
Reference |
|---|
    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 |
