Squalene synthase

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Squalene synthase

Existing structural data : 1EZF

Properties of human protein
Mass / length primary structure 417 amino acids
Secondary to quaternary structure Monomer; multipass membrane protein (ER)
Cofactor Mg 2+
Identifier
Gene name FDFT1
External IDs
Enzyme classification
EC, category 2.5.1.21 transferase
Response type Transfer of a farnesyl residue
Substrate 2 farnesyl diphosphate + 2 NADPH / H +
Products Squalene + 2 PP i + 2 NADP +
Occurrence
Parent taxon Eukaryotes

Squalene synthase (SQS) (also: farnesyl diphosphate farnesyl transferase, FDFT) is the enzyme that catalyzes the condensation reaction of two molecules of farnesyl diphosphate to squalene in eukaryotes . This is a sub-step in cholesterol biosynthesis and the first reaction that leads exclusively to cholesterol in animals. It is a transmembrane protein that is located on the endoplasmic reticulum . SQS is a promising pharmacological target for lowering cholesterol levels.

There are homologous enzymes in carotene- producing organisms that condense geranylgeranyl diphosphate (GGPP) to phytoene as part of this synthesis .

Catalyzed reaction

The reaction takes place in two sub-steps:

2 Farnesyl diphosphate
Presqualene diphosphate+ PP i

First, two farnesyl diphosphate molecules condense to form prequalene diphosphate.

Presqualene diphosphate+ 2  NADPH / H +
Squalene+ 2  NADP + + PP i

Then presqualene diphosphate is reduced to squalene and rearranged.

Individual evidence

  1. a b European Institute of Bioinformatics (EBI): InterPro IPR006449 Farnesyl-diphosphate farnesyltransferase. Retrieved August 15, 2011 .
  2. UniProt P37268
  3. Do R, Kiss RS, Gaudet D, Engert JC: Squalene synthase: a critical enzyme in the cholesterol biosynthesis pathway . In: Clin. Genet. . 75, No. 1, January 2009, pp. 19-29. doi : 10.1111 / j.1399-0004.2008.01099.x . PMID 19054015 .

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