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Literature summary for 2.5.1.21 extracted from

  • Ericsson, J.; Appelkvist, E.L.; Thelin, A.; Chojnacki, T.; Dallner, G.
    Isoprenoid biosynthesis in rat liver peroxisomes. Characterization of cis-prenyltransferase and squalene synthetase (1992), J. Biol. Chem., 267, 18708-18714.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
NADPH stimulates Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
additional information peroxisomal squalene synthase is inhibited by sonication, microsomal enzyme not Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Rattus norvegicus 5777
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.16
-
-
Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
farnesyl diphosphate + farnesyl diphosphate
-
Rattus norvegicus diphosphate + presqualene diphosphate
-
?
farnesyl diphosphate + NAD(P)H
-
Rattus norvegicus squalene + diphosphate + NAD(P)+
-
?
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 Rattus norvegicus squalene + NAD(P)+ + diphosphate
-
?