BRENDA home
History
Enzyme Nomenclature
Information on EC 1.3.1.96 - Botryococcus squalene synthase
for references in articles please use BRENDA:EC1.3.1.96Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.3.1.96 Botryococcus squalene synthaseIUBMB 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.
Specify your search results
The expected taxonomic range for this enzyme is: Botryococcus braunii
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
squalene synthase
squalene synthase-like 2
SSL-2
SSL-2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
squalene + diphosphate + NADP+ = presqualene diphosphate + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
presqualene diphosphate + NADPH + H+
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
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
-
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tween 80
-
increasing concentrations of Tween 80 up to 2% enhance enzyme activity approximately 2.5fold
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BOSS_BOTBR
465
0
52149
Swiss-Prot
other Location (Reliability: 3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52500
-
x * 52500, calculated from amino acid sequence and estimated from SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 52500, calculated from amino acid sequence and estimated from SDS-PAGE
?
-
x * 52500, calculated from amino acid sequence and estimated from SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.3.1.96)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda5 Ver: 69ad221-main (2022-06-24 14:26:09 +0200)