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