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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.97 expressed in Saccharomyces cerevisiae strain TN7 Botryococcus braunii
2.5.1.103 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.103 2 (2E,6E)-farnesyl diphosphate Botryococcus braunii
-
 presqualene diphosphate + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.96 Botryococcus braunii G0Y287
-
-
1.3.1.97 Botryococcus braunii G0Y288 race B
-
2.5.1.103 Botryococcus braunii G0Y286 race B
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.96 additional information SSL-2 shows a low capacity for squalene biosynthesis when incubated with farnesyl diphosphate as substrate Botryococcus braunii ?
-
 ?
1.3.1.96 presqualene diphosphate + NADPH + H+
-
 Botryococcus braunii squalene + diphosphate + NADP+
-
 ?
1.3.1.97 additional information SSL-3 does not appear able to directly utilize farnesyl diphosphate as a substrate Botryococcus braunii ?
-
 ?
1.3.1.97 presqualene diphosphate + NADPH + H+
-
 Botryococcus braunii C30 botryococcene + NADP+ + diphosphate
-
 ?
2.5.1.103 2 (2E,6E)-farnesyl diphosphate
-
 Botryococcus braunii presqualene diphosphate + diphosphate
-
 ?
2.5.1.103 2 (2E,6E)-farnesyl diphosphate condensation of two molecules of farnesyl diphosphate Botryococcus braunii presqualene diphosphate + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.96 squalene synthase-like 2
-
 Botryococcus braunii
1.3.1.96 SSL-2
-
 Botryococcus braunii
1.3.1.97 squalene synthase-like 3
-
 Botryococcus braunii
1.3.1.97 SSL-3
-
 Botryococcus braunii
2.5.1.103 squalene synthase-like
-
 Botryococcus braunii
2.5.1.103 SSL
-
 Botryococcus braunii

General Information

EC Number General Information Comment Organism
1.3.1.96 metabolism SSL-2 catalyzes the NADPH-dependent biosynthesis of approximately 90% bisfarnesyl ether and 10% squalene Botryococcus braunii
2.5.1.103 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
2.5.1.103 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
2.5.1.103 additional information bisfarnesyl ether biosynthesis from (2E,6E)-farnesyl diphosphate by SSL-2, overview Botryococcus braunii