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Literature summary for 2.5.1.21 extracted from

  • Katabami, A.; Li, L.; Iwasaki, M.; Furubayashi, M.; Saito, K.; Umeno, D.
    Production of squalene by squalene synthases and their truncated mutants in Escherichia coli (2015), J. Biosci. Bioeng., 119, 165-171.
    View publication on PubMed
Search for more literature for 2.5.1.21

Application

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(Commentary)

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

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens P37268 gene hsqs
-
Thermosynechococcus vestitus
-
 gene tsqs
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
SQS
-
 Thermosynechococcus vestitus

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Thermosynechococcus vestitus
NADPH
-
 Homo sapiens

General Information

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 [mM/s]

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