1.3.1.96: Botryococcus squalene synthase
This is an abbreviated version!
For detailed information about Botryococcus squalene synthase, go to the full flat file.
Reaction
Synonyms
squalene synthase, squalene synthase-like 2, SSL-2
ECTree
Advanced search results
Substrates Products
Substrates Products on EC 1.3.1.96 - Botryococcus squalene synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REACTION DIAGRAM
squalene + diphosphate + NADP+
-
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
-
ir
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
r
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
-
ir
?
-
-
SSL-2 cannot efficiently use farnesyl diphosphate as a substrate
-
-
?
additional information
?
-
SSL-2 shows a low capacity for squalene biosynthesis when incubated with farnesyl diphosphate as substrate
-
-
?
additional information
?
-
-
SSL-2 shows a low capacity for squalene biosynthesis when incubated with farnesyl diphosphate as substrate
-
-
?
additional information
?
-
analysis of substrate specificity, overview
-
-
?
additional information
?
-
squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-tohead condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. 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, oerview
-
-
?
additional information
?
-
-
SSL-2 cannot efficiently use farnesyl diphosphate as a substrate
-
-
?