Information on EC 1.3.1.97 - botryococcene synthase

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The expected taxonomic range for this enzyme is: Botryococcus braunii

EC NUMBER
COMMENTARY hide
1.3.1.97
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RECOMMENDED NAME
GeneOntology No.
botryococcene synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
C30 botryococcene + NADP+ + diphosphate = presqualene diphosphate + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
botryococcenes and methylated squalene biosynthesis
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
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+
botryococcene + diphosphate + NADP+
show the reaction diagram
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-
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-
?
presqualene diphosphate + NADPH + H+
C30 botryococcene + NADP+ + diphosphate
show the reaction diagram
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
show the reaction diagram
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mutant SSL-3
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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+
botryococcene + diphosphate + NADP+
show the reaction diagram
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-
-
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?
presqualene diphosphate + NADPH + H+
C30 botryococcene + NADP+ + diphosphate
show the reaction diagram
G0Y288
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?
presqualene diphosphate + NADPH + H+
squalene + diphosphate + NADP+
show the reaction diagram
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mutant SSL-3
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required for activity
additional information
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no enzyme activity is evident with Co2+ or Mn2+ as a cofactor
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
squalestatin
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Triton X-100
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Tween 80
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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
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at pH 7.3 and 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52500
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x * 52500, estimated from amino acid sequence and SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Saccharomyces cerevisiae strain TN7
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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)
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N171A/G207Q
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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
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site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Y166F
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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
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