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Literature summary extracted from

  • Agnew, W.S.
    Squalene synthetase (1985), Methods Enzymol., 110, 359-373.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.21 farnesyl diphosphate no inhibition of presqualene diphosphate synthase reaction; substrate inhibitor of squalene synthase reaction Saccharomyces cerevisiae

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.5.1.21 additional information
-
assay methods Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.21 farnesyl diphosphate + farnesyl diphosphate
-
Saccharomyces cerevisiae diphosphate + presqualene diphosphate
-
?
2.5.1.21 presqualene diphosphate + NAD(P)H in presence of reducing pyridine nucleotide, preferably NADPH, squalene is formed, in absence of reducing cofactor the rate of the condensation reaction is lower and all of the product accumulates as presqualene diphosphate Saccharomyces cerevisiae squalene + NAD(P)+ + diphosphate
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.21 NADH NADH or NADPH required for squalene synthase reaction Saccharomyces cerevisiae
2.5.1.21 NADPH NADPH or NADH required for squalene synthase reaction Saccharomyces cerevisiae