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Literature summary for 2.3.1.39 extracted from

  • Misra, A.; Surolia, N.; Surolia, A
    Catalysis and mechanism of malonyl transferase activity in type II fatty acid biosynthesis acyl carrier proteins (2009), Mol. Biosyst., 5, 651-659.
    View publication on PubMed

Protein Variants

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 [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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Plasmodium falciparum
-
-
-

Reaction

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 and Products (Substrate)

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 [1/s]

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 [mM/s]

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