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Literature summary for 2.5.1.103 extracted from

  • Niehaus, T.D.; Okada, S.; Devarenne, T.P.; Watt, D.S.; Sviripa, V.; Chappell, J.
    Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii (2011), Proc. Natl. Acad. Sci. USA, 108, 12260-12265.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.103

Cloned(Commentary)

Cloned (Comment) Organism
screening for squalene synthase-like genes, identification of gene SSL-1, DNA and amino acid sequence determmination and analysis, co-expression with SSL-2 leads to30fold increased squalene production Botryococcus braunii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 (2E,6E)-farnesyl diphosphate Botryococcus braunii
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 presqualene diphosphate + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Botryococcus braunii G0Y286 race B
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 (2E,6E)-farnesyl diphosphate
-
 Botryococcus braunii presqualene diphosphate + diphosphate
-
 ?
2 (2E,6E)-farnesyl diphosphate condensation of two molecules of farnesyl diphosphate Botryococcus braunii presqualene diphosphate + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
squalene synthase-like
-
 Botryococcus braunii
SSL
-
 Botryococcus braunii

General Information

General Information Comment Organism
evolution SSL_1 belongs to the family of squalene synthase-like enzymes. Triterpene metabolism in Botryococcus braunii operates differently from that in other organisms. While squalene synthase, an ancient and likely progenitor to the other Botryococcus triterpene synthases, catalyzes a two-step reaction within a single enzyme unit without intermediate release, yet in Botryococcus braunii, these activities appear to have separated and evolved interdependently for specialized greater triterpene oil production into SSL-1 an SSL-2 Botryococcus braunii
metabolism SSL-1 catalyzes the biosynthesis of presqualene diphosphate. The product presqualene diphosphate is further converted to botryococcene by SSL-3 or to squalene by SSL-2.. While squalene synthase, an ancient and likely progenitor to the other Botryococcus triterpene synthases, catalyzes a two-step reaction within a single enzyme unit without intermediate release, yet in Botryococcus braunii, these activities appear to have separated and evolved interdependently for specialized greater triterpene oil production Botryococcus braunii
additional information bisfarnesyl ether biosynthesis from (2E,6E)-farnesyl diphosphate by SSL-2, overview Botryococcus braunii