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Literature summary for 2.3.1.41 extracted from

  • Witkowski, A.; Joshi, A.K.; Smith, S.
    Mechanism of the beta-ketoacyl synthase reaction catalyzed by the animal fatty acid synthase (2002), Biochemistry, 41, 10877-10887.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C161Q site-directed mutagenesis, active site Cys mutant, no condensation activity, but 377fold increased decarboxylation activity Rattus norvegicus
additional information triple and quadruple mutants of fatty acid synthase complex including mutation sites in the beta-ketoacyl-[acyl-carrier-protein] synthase. e.g. H293A, H331A, K326A,S581A, kinetics, overview Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide kinetics Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information mutants Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] mechanism Rattus norvegicus
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] active site cysteine Rattus norvegicus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
mutants Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
Rattus norvegicus 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
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