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Literature summary for 2.5.1.21 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
Search for more literature for 2.5.1.21

Cloned(Commentary)

Cloned (Comment) Organism
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
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
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
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

Inhibitors Comment Organism Structure
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

Localization Comment Organism GeneOntology No. Textmining
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
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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
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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
-
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
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Organism

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

Subunits

Subunits Comment Organism
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
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
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
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

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

General Information

General Information Comment Organism
metabolism squalene synthase catalyzes the first committed step in sterol biosynthesis Arabidopsis thaliana
metabolism squalene synthase catalyzes the first committed step in sterol biosynthesis Botryococcus braunii
metabolism squalene synthase catalyzes the first committed step in sterol biosynthesis Homo sapiens
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
additional information the hinge domain plays an essential functional role, such as assembly of ergosterol multi-enzymecomplexes in fungi Saccharomyces cerevisiae
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