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Literature summary for 2.3.1.38 extracted from

  • Rangan, V.S.; Smith, S.
    Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue (1997), J. Biol. Chem., 272, 11975-11978.
    View publication on PubMed
Search for more literature for 2.3.1.38

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutants in Escherichia coli BL21 (DE3) Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
R606A oligonucleotide-directed in vitro mutagenesis, 6.6fold increase in activity about 16000fold increase in selectivity for acetyl-CoA against malonyl-CoA, increased production of medium-chain length fatty acids Rattus norvegicus
R606K oligonucleotide-directed in vitro mutagenesis, 1.7fold increase in activity about 16fold increase in selectivity for acetyl-CoA against malonyl-CoA Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0018
-
 acetyl-CoA recombinant purified mutant R606A Rattus norvegicus
0.0029
-
 acetyl-CoA recombinant purified mutant R606K Rattus norvegicus
0.0039
-
 acetyl-CoA recombinant purified wild-type enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant mutants from E. coli Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + an [acyl-carrier protein] = CoA + an acetyl-[acyl-carrier protein] mechanism Rattus norvegicus
a
acetyl-CoA + an [acyl-carrier protein] = CoA + an acetyl-[acyl-carrier protein] Arg-606 is responsible for malonyl-CoA specificity of the bifunctional enzyme Rattus norvegicus
a

Renatured (Commentary)

Renatured (Comment) Organism
recombinant enzyme purified from E. coli, refolding after treatment of inclusion bodies with urea Rattus norvegicus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Rattus norvegicus
2.68
-
 recombinant purified wild-type enzyme Rattus norvegicus
4.53
-
 recombinant purified mutant R606K Rattus norvegicus
17.8
-
 recombinant purified mutant R606A Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + pantetheine dual specificity of a malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase Rattus norvegicus CoA + acetyl-S-pantetheine
-
 r
acetyl-CoA + pantetheine octanoyl-S-pantetheine, decanoyl-S-pantetheine, and dodecanoyl-S-pantetheine can also serve as substrates for the backward reaction Rattus norvegicus CoA + acetyl-S-pantetheine
-
 r
acetyl-CoA + [acyl-carrier protein] dual specificity of a malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase Rattus norvegicus CoA + acetyl-[acyl-carrier protein]
-
 ?

Synonyms

Synonyms Comment Organism
malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase
-
 Rattus norvegicus
More cf. EC 2.3.1.85 and EC 2.3.1.86 Rattus norvegicus
More dual specificity of a malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.9
-
 acetyl-CoA recombinant purified wild-type enzyme Rattus norvegicus
3.4
-
 acetyl-CoA recombinant purified mutant R606K Rattus norvegicus
4.2
-
 acetyl-CoA recombinant purified mutant R606A Rattus norvegicus