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Information on EC 1.3.1.96 - Botryococcus squalene synthase and Organism(s) Botryococcus braunii and UniProt Accession G0Y287

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IUBMB Comments
Isolated from the green alga Botryococcus braunii BOT22. Acts in the reverse direction. cf. EC 2.5.1.21, squalene synthase, where squalene is formed directly from farnesyl diphosphate.
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This record set is specific for:
Botryococcus braunii
UNIPROT: G0Y287
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The taxonomic range for the selected organisms is: Botryococcus braunii
The expected taxonomic range for this enzyme is: Botryococcus braunii
Synonyms
ssl-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
squalene synthase-like 2
-
squalene synthase
-
-
squalene synthase-like 2
-
-
SSL-2
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
squalene:NADP+ oxidoreductase
Isolated from the green alga Botryococcus braunii BOT22. Acts in the reverse direction. cf. EC 2.5.1.21, squalene synthase, where squalene is formed directly from farnesyl diphosphate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
show the reaction diagram
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
show the reaction diagram
-
-
-
r
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
required for activity
Mg2+
-
required for activity
Mn2+
-
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
squalestatin
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Tween 80
-
increasing concentrations of Tween 80 up to 2% enhance enzyme activity approximately 2.5fold
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001
squalestatin
-
at pH 7.3 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
in MOPS buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SSL-2 catalyzes the NADPH-dependent biosynthesis of approximately 90% bisfarnesyl ether and 10% squalene
physiological function
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BOSS_BOTBR
465
0
52149
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52500
-
x * 52500, calculated from amino acid sequence and estimated from SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52500, calculated from amino acid sequence and estimated from SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y168A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Y168F
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SSL-2, sequence comparisons, recombinant expression of C-terminally truncated wild-type and mutant enzymes enzymes, lacking 87 amino acids, in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okada, S.; Devarenne, T.P.; Chappell, J.
Molecular characterization of squalene synthase from the green microalga Botryococcus braunii, race B
Arch. Biochem. Biophys.
373
307-317
2000
Botryococcus braunii, Botryococcus braunii Berkeley
Manually annotated by BRENDA team
Okada, S.; Devarenne, T.P.; Murakami, M.; Abe, H.; Chappell, J.
Characterization of botryococcene synthase enzyme activity, a squalene synthase-like activity from the green microalga Botryococcus braunii, Race B
Arch. Biochem. Biophys.
422
110-118
2004
Botryococcus braunii, Botryococcus braunii Berkeley (Showa)
Manually annotated by BRENDA team
Niehaus, T.D.; Kinison, S.; Okada, S.; Yeo, Y.S.; Bell, S.A.; Cui, P.; Devarenne, T.P.; Chappell, J.
Functional identification of triterpene methyltransferases from Botryococcus braunii race B
J. Biol. Chem.
287
8163-8173
2012
Botryococcus braunii
Manually annotated by BRENDA team
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
Proc. Natl. Acad. Sci. USA
108
12260-12265
2011
Botryococcus braunii (G0Y287), Botryococcus braunii
Manually annotated by BRENDA team
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
Biochemistry
53
7570-7581
2014
Botryococcus braunii (G0Y287)
Manually annotated by BRENDA team