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