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Literature summary extracted from

  • Linscott, K.B.; Niehaus, T.D.; Zhuang, X.; Bell, S.A.; Chappell, J.
    Mapping a kingdom-specific functional domain of squalene synthase (2016), Biochim. Biophys. Acta, 1861, 1049-1057.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.21 gene BSS, recombinant enzyme expression in an enzyme-deficient SQS-knockout Saccharomyces cerevisiae DELTAerg9 strain, the enzyme can partially complement the knockout mutation when the gene is weakly expressed, but when highly expressed, the non-fungal squalene synthase cannot complement the yeast mutation and instead leads to the accumulation of a toxic intermediate(s) as defined by mutations of genes downstream in the ergosterol pathway Botryococcus braunii
2.5.1.21 gene erg9, recombinant expression in enzyme-deficient SQS-knockout Saccharomyces cerevisiae DELTAerg9 strain, the endogenous enzyme partially complements the knockout mutation, restoration of the complete complementation phenotype is mapped to a 26-amino acid hinge region linking the catalytic and membrane-spanning domains specific to fungal squalene synthases Saccharomyces cerevisiae
2.5.1.21 gene SQS, recombinant enzyme expression in an enzyme-deficient SQS-knockout Saccharomyces cerevisiae DELTAerg9 strain, the enzyme can partially complement the knockout mutation when the gene is weakly expressed, but when highly expressed, the non-fungal squalene synthase cannot complement the yeast mutation and instead leads to the accumulation of a toxic intermediate(s) as defined by mutations of genes downstream in the ergosterol pathway Arabidopsis thaliana
2.5.1.21 gene SQS, recombinant enzyme expression in an enzyme-deficient SQS-knockout Saccharomyces cerevisiae DELTAerg9 strain, the enzyme can partially complement the knockout mutation when the gene is weakly expressed, but when highly expressed, the non-fungal squalene synthase cannot complement the yeast mutation and instead leads to the accumulation of a toxic intermediate(s) as defined by mutations of genes downstream in the ergosterol pathway Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.21 additional information overexpression of the enzyme's C-terminal domain containing a hinge domain from fungi, not from animals or plants, leads to growth inhibition of wild-type yeast Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.5.1.21 endoplasmic reticulum membrane squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane Arabidopsis thaliana 5789
-
2.5.1.21 endoplasmic reticulum membrane squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane Botryococcus braunii 5789
-
2.5.1.21 endoplasmic reticulum membrane squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane Homo sapiens 5789
-
2.5.1.21 endoplasmic reticulum membrane squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain which consists of a hinge region and a membrane spanning helix responsible for tethering the enzyme to the cytosolic face of the endoplasmic reticulum Saccharomyces cerevisiae 5789
-

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.21 Arabidopsis thaliana
-
 gene SQS
-
2.5.1.21 Botryococcus braunii Q9SDW9 gene BSS
-
2.5.1.21 Homo sapiens P37268 gene SQS or FDFT1
-
2.5.1.21 Saccharomyces cerevisiae P53866 gene erg9 or SQS1
-

Subunits

EC Number Subunits Comment Organism
2.5.1.21 More squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane Arabidopsis thaliana
2.5.1.21 More squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane Botryococcus braunii
2.5.1.21 More squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane Homo sapiens
2.5.1.21 More squalene synthase consists of both an N-terminal catalytic domain and a C-terminal domain tethering the enzyme to the endoplasmic reticulum membrane Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.5.1.21 SQS
-
 Arabidopsis thaliana
2.5.1.21 SQS
-
 Botryococcus braunii
2.5.1.21 SQS
-
 Homo sapiens
2.5.1.21 SQS
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.5.1.21 metabolism squalene synthase catalyzes the first committed step in sterol biosynthesis Arabidopsis thaliana
2.5.1.21 metabolism squalene synthase catalyzes the first committed step in sterol biosynthesis Botryococcus braunii
2.5.1.21 metabolism squalene synthase catalyzes the first committed step in sterol biosynthesis Homo sapiens
2.5.1.21 metabolism squalene synthase catalyzes the first committed step in sterol biosynthesis, role of squalene synthase in the ergosterol biosynthetic pathway of budding yeast, overview Saccharomyces cerevisiae
2.5.1.21 additional information the hinge domain plays an essential functional role, such as assembly of ergosterol multi-enzymecomplexes in fungi Saccharomyces cerevisiae
2.5.1.21 physiological function the catalytic domain performs the head-to-head dimerization of two molecules of farnesyl diphosphate to form squalene, a 30 carbon isoprenoid oxidized by squalene monooxygenase (Erg1) and cyclized by lanosterol synthase Saccharomyces cerevisiae