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Literature summary for 2.5.1.103 extracted from

  • Bell, S.A.; Niehaus, T.D.; Nybo, S.E.; Chappell, J.
    Structure-function mapping of key determinants for hydrocarbon biosynthesis by squalene and squalene synthase-like enzymes from the green alga Botryococcus braunii race B (2014), Biochemistry, 53, 7570-7581 .
    View publication on PubMed
Search for more literature for 2.5.1.103

Cloned(Commentary)

Cloned (Comment) Organism
gene SSL-1, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Botryococcus braunii

Protein Variants

Protein Variants Comment Organism
Y175A site-sirected mutagenesis, mutant substrate specificity and activity compared to the wild-type Botryococcus braunii
Y175F site-sirected mutagenesis, mutant substrate specificity and activity compared to the wild-type Botryococcus braunii

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Botryococcus braunii

Natural Substrates/ Products (Substrates)

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

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 + NADPH + H+
-
 Botryococcus braunii diphosphate + presqualene diphosphate + NADP+
-
 ?
additional information no synthesis of squalene from presqualene diphosphate, analysis of substrate specificity, overview Botryococcus braunii ?
-
 ?

Synonyms

Synonyms Comment Organism
SSL-1
-
 Botryococcus braunii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Botryococcus braunii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
 assay at Botryococcus braunii

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Botryococcus braunii

General Information

General Information Comment Organism
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 Botryococcus braunii
additional information 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 Botryococcus braunii