Protein Variants | Comment | Organism |
---|---|---|
E20A | mutant retains activity | Plasmodium falciparum |
K61A | complete loss of the malonyl transferase activities | Escherichia coli |
K62A | complete loss of the malonyl transferase activities | Plasmodium falciparum |
Q66A | complete loss of the malonyl transferase activities | Escherichia coli |
Q66G | complete loss of the malonyl transferase activities | Escherichia coli |
Q66R | increase in the malonyl transferase activities | Escherichia coli |
Q67A | complete loss of the malonyl transferase activities | Plasmodium falciparum |
Q67G | complete loss of the malonyl transferase activities | Plasmodium falciparum |
Q67R | increase in the malonyl transferase activities | Plasmodium falciparum |
T65A | mutant retains activity | Plasmodium falciparum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.02 | - |
malonyl-CoA | acyl carrier protein mutant E20A, pH 7.5, 25°C | Plasmodium falciparum | |
0.033 | - |
malonyl-CoA | acyl carrier protein mutant Q67R, pH 7.5, 25°C | Plasmodium falciparum | |
0.034 | - |
malonyl-CoA | acyl carrier protein mutant T65A, pH 7.5, 25°C | Plasmodium falciparum | |
0.049 | - |
malonyl-CoA | acyl carrier protein mutant Q66R, pH 7.5, 25°C | Escherichia coli | |
0.049 | - |
malonyl-CoA | wild-type acyl carrier protein, pH 7.5, 25°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Plasmodium falciparum | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] | the catalytic malonyl transferase activity is intrinsic to an individual acyl carrier protein. An arginine/lysine in loop II and an arginine/glutamine in helix III are the catalytic residues for transferase function. The hydrogen bonding properties of these residues are indespensible for the transferase reaction | Escherichia coli | |
malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein] | the catalytic malonyl transferase activity is intrinsic to an individual acyl carrier protein. An arginine/lysine in loop II and an arginine/glutamine in helix III are the catalytic residues for transferase function. The hydrogen bonding properties of these residues are indespensible for the transferase reaction | Plasmodium falciparum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
malonyl-CoA + acyl-carrier protein | - |
Escherichia coli | CoA + malonyl-[acyl-carrier protein] | - |
? | |
malonyl-CoA + acyl-carrier protein | - |
Plasmodium falciparum | CoA + malonyl-[acyl-carrier protein] | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00027 | - |
malonyl-CoA | acyl carrier protein mutant E20A, pH 7.5, 25°C | Plasmodium falciparum | |
0.00032 | - |
malonyl-CoA | acyl carrier protein mutant T65A, pH 7.5, 25°C | Plasmodium falciparum | |
0.00047 | - |
malonyl-CoA | wild-type acyl carrier protein, pH 7.5, 25°C | Escherichia coli | |
0.0011 | - |
malonyl-CoA | acyl carrier protein mutant Q67R, pH 7.5, 25°C | Plasmodium falciparum | |
0.0015 | - |
malonyl-CoA | acyl carrier protein mutant Q66R, pH 7.5, 25°C | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0092 | - |
malonyl-CoA | acyl carrier protein mutant T65A, pH 7.5, 25°C | Plasmodium falciparum | |
0.0095 | - |
malonyl-CoA | wild-type acyl carrier protein, pH 7.5, 25°C | Escherichia coli | |
0.013 | - |
malonyl-CoA | acyl carrier protein mutant E20A, pH 7.5, 25°C | Plasmodium falciparum | |
0.03 | - |
malonyl-CoA | acyl carrier protein mutant Q66R, pH 7.5, 25°C | Escherichia coli | |
0.033 | - |
malonyl-CoA | acyl carrier protein mutant Q67R, pH 7.5, 25°C | Plasmodium falciparum |