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Literature summary for 2.3.1.86 extracted from

  • Engeser, H.; Hubner, K.; Straub, J.; Lynen, F.
    Identity of malonyl and palmitoyl transferase of fatty acid synthetase from yeast. Functional interrelationships between the acyl transferases (1979), Eur. J. Biochem., 101, 407-412.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithio-bis(2-nitrobenzoic acid) covalent binding to palmitoyl residues, malonyl-CoA protects Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of transacylase activity Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H+ = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+ structure Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 7 malonyl-CoA + 7 NADH + 7 NADPH + 14 H+ intermediates are never released into the medium Saccharomyces cerevisiae palmitoyl-CoA + 7 CoA + 7 CO2 + 7 NAD+ + 7 NADP+ + 7 H2O
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Saccharomyces cerevisiae