Application | Comment | Organism |
---|---|---|
industry | squalene has industrial value as a lubricant, health promoting agent, and/or drop-in biofuel, establishment of an efficient Escherichia coli-based system for squalene production | Thermosynechococcus vestitus |
industry | squalene has industrial value as a lubricant, health promoting agent, and/or drop-in biofuel, establishment of an efficient Escherichia coli-based system for squalene production | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
gene hsqs, recombinant functional expression of mutant enzyme with truncated membrane-binding domains, i.e. 30 residues of the N-terminus and 47 residues of the C-terminus, in Escherichia coli strain XL1-Blue, performance of the squalene hyperproducing strain is best at 37°C | Homo sapiens |
gene tsqs, recombinant functional expression of wild-type full-length enzyme in Escherichia coli strain XL1-Blue, performance of the squalene hyperproducing strain is best at 37°C | Thermosynechococcus vestitus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | significant truncation of squalene synthase at the C-terminus retains partial cellular activity. Construction of a squalene-producing strain as a convenient platform for gene discovery and the construction of the pathway toward natural and non-natural hopanoids/steroids. Using farnesyl diphosphate as the starting material, squalene is produced by the exogenously expressed squalene synthase, SQS, in Escherichia coli. The production of squalene can be enhanced by overexpressing the rate-limiting steps, enzyme isopentenyl-diphosphate DELTA-isomerase, Idi EC 5.3.3.2, or/and adding an alternative supply route, i.e. the MEV pathway, overview | Thermosynechococcus vestitus |
additional information | significant truncation of squalene synthase at the C-terminus retains partial cellular activity. Construction of a squalene-producing strain as a convenient platform for gene discovery and the construction of the pathway toward natural and non-natural hopanoids/steroids. Using farnesyl diphosphate as the starting material, squalene is produced by the exogenously expressed squalene synthase, SQS, in Escherichia coli. The production of squalene can be enhanced by overexpressing the rate-limiting steps, enzyme isopentenyl-diphosphate DELTA-isomerase, Idi EC 5.3.3.2, or/and adding an alternative supply route, i.e. the MEV pathway, overview | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | bound | Thermosynechococcus vestitus | 16020 | - |
membrane | bound, the membrane-binding domains of the human enzyme are 30 residues of the N-terminus and 47 residues of the C-terminus | Homo sapiens | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 (2E,6E)-farnesyl diphosphate + NADPH + H+ | Thermosynechococcus vestitus | - |
squalene + 2 diphosphate + NADP+ | - |
? | |
2 (2E,6E)-farnesyl diphosphate + NADPH + H+ | Homo sapiens | - |
squalene + 2 diphosphate + NADP+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P37268 | gene hsqs | - |
Thermosynechococcus vestitus | - |
gene tsqs | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 (2E,6E)-farnesyl diphosphate + NADPH + H+ | - |
Thermosynechococcus vestitus | squalene + 2 diphosphate + NADP+ | - |
? | |
2 (2E,6E)-farnesyl diphosphate + NADPH + H+ | - |
Homo sapiens | squalene + 2 diphosphate + NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SQS | - |
Thermosynechococcus vestitus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Thermosynechococcus vestitus | |
NADPH | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
physiological function | squalene is biosynthesized via the head-to-head condensation of two molecules of farnesyl diphosphate, which is catalyzed by the single enzyme squalene synthase. Squalene is a precursor of thousands of bioactive triterpenoids | Thermosynechococcus vestitus |
physiological function | squalene is biosynthesized via the head-to-head condensation of two molecules of farnesyl diphosphate, which is catalyzed by the single enzyme squalene synthase. Squalene is a precursor of thousands of bioactive triterpenoids | Homo sapiens |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
510 | - |
(2E,6E)-farnesyl diphosphate | pH and temperature not specified in the publication, recombinant enzyme | Homo sapiens | |
1800 | - |
(2E,6E)-farnesyl diphosphate | pH and temperature not specified in the publication, recombinant enzyme | Thermosynechococcus vestitus |