Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.86 5,5'-dithio-bis(2-nitrobenzoic acid) covalent binding to palmitoyl residues, malonyl-CoA protects Saccharomyces cerevisiae

KM Value [mM]

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.86 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.86
-
 Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.86 acetyl-CoA + 7 malonyl-CoA + 14 NADPH + 14 H+ = hexadecanoyl-CoA + 7 CoA + 7 CO2 + 14 NADP+ + 7 H2O structure Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.86 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]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.86 25
-
 assay at Saccharomyces cerevisiae