1.3.1.96: Botryococcus squalene synthase

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For detailed information about Botryococcus squalene synthase, go to the full flat file.

Reaction

Synonyms

squalene synthase, squalene synthase-like 2, SSL-2

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.1 With NAD⁺ or NADP⁺ as acceptor

                1.3.1.96 Botryococcus squalene synthase

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1	Activating Compound
1	AA Sequence
2	Cloned(Commentary)
3	Cofactor
3	General Information
1	Inhibitors
1	Ki Value [mM]
5	Localization
4	Metals/Ions
1	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
7	Organism
1	Pathway
2	pH Optimum
2	Protein Variants
1	Reaction
7	Reference
13	Substrates and Products (Substrate)
2	Subunits
12	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]

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Natural Substrates Products on EC 1.3.1.96 - Botryococcus squalene synthase

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

presqualene diphosphate + NADPH + H+

squalene + diphosphate + NADP+

Botryococcus braunii

G0Y287

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741903

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r

additional information

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Botryococcus braunii

G0Y287

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

741903

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