EC Number   |
General Information |
Reference |
|---|
   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 |
720917 |
| 2.5.1.103 | metabolism |
different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, the same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, overview |
741903 |
| 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 |
720917 |
| 2.5.1.103 | more |
bisfarnesyl ether biosynthesis from (2E,6E)-farnesyl diphosphate by SSL-2, overview |
720917 |
| 2.5.1.103 | more |
proposed catalytic cascades for the enzyme-mediated biosynthesis of squalene and botryococcene, and molecular modeling of Botryococcus braunii botryococcene and squalene synthase enzymes, overview. Substrate docking and molecular modeling |
741903 |
