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Information on EC 1.3.1.97 - botryococcene synthase and Organism(s) Botryococcus braunii and UniProt Accession G0Y288

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     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.97 botryococcene synthase
IUBMB Comments
Isolated from the green alga Botryococcus braunii BOT22. Acts in the reverse direction. Involved in the production of botryococcenes, which are triterpenoid hydrocarbons of isoprenoid origin produced in large amount by this alga.
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Botryococcus braunii
UNIPROT: G0Y288
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The taxonomic range for the selected organisms is: Botryococcus braunii
The enzyme appears in selected viruses and cellular organisms
Synonyms
botryococcene synthase, ssl-3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
squalene synthase-like 3
-
botryococcene synthase
-
-
squalene synthase-like 3
-
-
squalene synthase-like protein 3
-
-
SSL-3
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
C30 botryococcene:NADP+ oxidoreductase
Isolated from the green alga Botryococcus braunii BOT22. Acts in the reverse direction. Involved in the production of botryococcenes, which are triterpenoid hydrocarbons of isoprenoid origin produced in large amount by this alga.
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+
C30 botryococcene + diphosphate + NADP+
show the reaction diagram
-
-
-
?
presqualene diphosphate + NADPH + H+
C30 botryococcene + NADP+ + diphosphate
show the reaction diagram
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
show the reaction diagram
mutant SSL-3
-
-
?
presqualene diphosphate + NADPH + H+
C30 botryococcene + NADP+ + diphosphate
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+
C30 botryococcene + diphosphate + NADP+
show the reaction diagram
-
-
-
?
presqualene diphosphate + NADPH + H+
C30 botryococcene + NADP+ + diphosphate
show the reaction diagram
-
-
-
?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
show the reaction diagram
mutant SSL-3
-
-
?
presqualene diphosphate + NADPH + H+
C30 botryococcene + NADP+ + diphosphate
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for activity
additional information
-
no enzyme activity is evident with Co2+ or Mn2+ as a cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
squalestatin
-
-
Triton X-100
-
-
Tween 80
-
enzyme activity is completely abolished by 0.5% (v/v) Tween 80
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
-
the enzyme catalyses the final step of B-race hydrocarbon biosynthesis
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?
BOCS_BOTBR
383
0
44156
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52500
-
x * 52500, estimated from amino acid sequence and SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N171A/G207Q
site-directed mutagenesis, combined N171A and G207Q mutations in the SSL-3 backbone result in complete conversion of SSL-3 from an enzyme that used presqualene diphosphate for botryococcene biosynthesis to one that used presqualene diphosphate for squalene biosynthesis
Y166A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Y166F
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
additional information
generation of an expression system for production of high levels of botryococcene in Nicotiana tabacum strain KY 1068 plants by diverting carbon flux from the cytosolic mevalonate pathway or the plastidic methylerythritol phosphate pathway by the targeted overexpression of an avian farnesyl diphosphate synthase along with botryococcene synthase SSL-3 and presqualene diphosphate synthase SSL-1, overview. The structure of purified botryococcene from tobacco is determined by 1H-NMR and 13C-NMR spectral analyses. Modifications of botryococcene in tobacco by coexpressed triterpene methyltransferases (TMTs) from Botryococcus braunii
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain TN7
gene SSL-3, recombinant expression of the enzyme in Nicotiana tabacum, ene constructs consisted of a peptide fusion of SSL-1 and SSL-3 connected by a triplet repeat peptide linker of Gly-Gly-Ser-Gly, with or without appending the C-terminal end (71 amino acids) of the Botryococcus braunii squalene synthase onto the C-terminus of SSL-3 and the FPS gene. The chimeric SSL1-3 genes and FPS gene are inserted downstream of the strong constitutive promoters Pcv and Pca, respectively. For trichome-specific expression of triterpene biosynthesis, the trichome-specific promoters Pcbt and Pcyp16 are fused to 5' end of botryococcene synthase gene, presqualene diphosphate synthase gene, and the FPS gene, respectively
gene SSL-3, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
expressed in Chlamydomonas reinhardtii chloroplasts
-
expressed in Escherichia coli BL21(DE3) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression is preferential during rapid growth
-
gene expression is preferential during rapid growth. Enzyme activity is initially low in the cells, but rises greater than 10fold to a maximum by day 3, and then decreases gradually to almost undetectable levels by the end of the culture period
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
an expression system for production of high levels of botryococcene in Nicotiana tabacum plants can be used involving the recombinant chimeric enzyme, trichome-specific expression of botryococcene metabolism, overview
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
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 (G0Y288), 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 (G0Y288)
Manually annotated by BRENDA team
Jiang, Z.; Kempinski, C.; Bush, C.J.; Nybo, S.E.; Chappell, J.
Engineering triterpene and methylated triterpene production in plants provides biochemical and physiological insights into terpene metabolism
Plant Physiol.
170
702-716
2016
Botryococcus braunii (G0Y288)
Manually annotated by BRENDA team
Hsu, S.; Browne, D.; Tatli, M.; Devarenne, T.; Stern, D.
N-terminal sequences affect expression of triterpene biosynthesis enzymes in Chlamydomonas chloroplasts
Algal Res.
44
101662
2019
Botryococcus braunii
-
Manually annotated by BRENDA team
Hirano, K.; Hara, T.; Ardianor, T.; Nugroho, R.A.; Segah, H.; Takayama, N.; Sulmin, G.; Komai, Y.; Okada, S.; Kawamura, K.
Detection of the oil-producing microalga Botryococcus braunii in natural freshwater environments by targeting the hydrocarbon biosynthesis gene SSL-3
Sci. Rep.
9
16974
2019
Botryococcus braunii, Botryococcus braunii Showa
Manually annotated by BRENDA team