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Information on EC 2.5.1.148 - lycopaoctaene synthase
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2.5.1.148 lycopaoctaene synthaseIUBMB Comments
The enzyme, characterized from the green microalga Botryococcus braunii race L, in involved in biosynthesis of (14E,18E)-lycopadiene. In vitro, the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyse the condensation of two different substrate molecules, forming chimeric products. However, the use of these alternative substrates is not significant in vivo.
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Word Map
- 2.5.1.148
-
juice
-
pepsinogen
-
reflux
-
peptic
- histamine
- pentagastrin
-
duodenal
- gastrin
- collagen
- pepstatin
-
esophageal
-
hydrochloric
-
laryngopharyngeal
-
fistula
-
pouch
-
aspiration
-
proteinases
-
gastroesophageal
-
pentagastrin-stimulated
-
vagotomy
- hcl
-
laryngeal
- atropine
- chymosin
-
vagal
-
conscious
- papain
-
hydrolysate
-
intragastric
- secretin
-
zymogen
- cimetidine
-
fundic
-
fab\'2
- ranitidine
-
antisecretory
-
h2-receptors
- rennin
-
milk-clotting
-
pylorus-ligated
-
multichannel
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
lycopaoctaene synthase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LOS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 geranylgeranyl diphosphate + NADPH + H+ = lycopaoctaene + 2 diphosphate + NADP+
overall reaction
-
-
-
2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate
(1a)
-
-
-
prephytoene diphosphate + NADPH + H+ = lycopaoctaene + diphosphate + NADP+
(1b)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl diphosphate:geranylgeranyl diphosphate geranylgeranyltransferase
The enzyme, characterized from the green microalga Botryococcus braunii race L, in involved in biosynthesis of (14E,18E)-lycopadiene. In vitro, the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyse the condensation of two different substrate molecules, forming chimeric products. However, the use of these alternative substrates is not significant in vivo.
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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
(2E,6E)-farnesyl diphosphate + geranylgeranyl diphosphate + NADPH + H+
(6E,10E,14E,18E,22E)-2,6,10,14,19,23,27-heptamethyloctacosa-2,6,10,14,18,22,26-heptaene + NADP+ + 2 diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + phytyl diphosphate + NADPH + H+
squalene + (6E,10E,14E)-2,6,10,15,19,23,27-heptamethyloctacosa-2,6,10,14,tetraene + lycopadiene + NADP+
when LOS is supplied with (2E,6E)-farnesyl diphosphate and phythyl diphoshate, squalene production predominates with small amounts of (6E,10E,14E)-2,6,10,15,19,23,27-heptamethyloctacosa-2,6,10,14,tetraene and lycopadiene
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 farnesyl diphosphate + NADPH + H+
C30 squalene + 2 diphosphate + NADP+
-
-
-
?
2 geranylgeranyl diphosphate
diphosphate + prephytoene diphosphate
-
-
-
?
2 geranylgeranyl diphosphate + NADH + H+
lycopaoctaene + 2 diphosphate + NAD+
overall reaction. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene. The enzyme uses both NADH and NADPH as reducing agents for lycopaoctaene production, with preference for NADPH
-
-
?
geranylgeranyl diphosphate + farnesyl diphosphate + NADPH + H+
C35H58 hydrocarbon + 2 diphosphate + NADP+
-
-
-
?
geranylgeranyl diphosphate + geranylgeranyl diphosphate
prelycopersene diphosphate + diphosphate
-
-
-
?
geranylgeranyl diphosphate + NAD(P)H
lycopersene + NAD(P)+ + diphosphate
-
-
-
?
geranylgeranyl diphosphate + phytyl diphosphate + NADPH + H+
lycopaoctaene + lycopadiene + lycopapentaene + NADP+
LOS incubation with GGPP and phythyl diphoshate produces lycopadiene and lycopapentaene as minor products and lycopaoctaene as the major product
-
-
?
prephytoene diphosphate + NADPH + H+
lycopaoctaene + diphosphate + NADP+
lycopaoctaene i.e. 15,15'-dihydrophytoene i.e. (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
LOS catalyzes the condensation of two GGPP units in the first half reaction to form the cyclopropylcarbinyl diphosphate intermediate PLPP, with concomitant release of one molecule of inorganic diphosphate. In the second half reaction, the PLPP cyclopropyl ring is cleaved and rearranged to form a 1-1' linkage and further reduction by NADPH forms lycopaoctaene. Without NADPH only the reaction intermediate PLPP accumulates
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
the LOS reaction uses a cyclopropyl intermediate
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
the enzyme is involved in biosynthesis of (14E,18E)-lycopadiene overall reaction. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
the enzyme is involved in biosynthesis of (14E,18E)-lycopadiene. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
overall reaction. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene. The enzyme catalyzes the head-to-head condensation of two C20 geranylgeranyl diphosphate molecules to produce C40 lycopaoctaene
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
overall reaction. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene. The enzyme uses both NADH and NADPH as reducing agents for lycopaoctaene production, with preference for NADPH
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
overall reaction. Lycopaoctaene i.e. 15,15'-dihydrophytoene i.e. (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
Botryococcus braunii AC768
overall reaction. Lycopaoctaene i.e. 15,15'-dihydrophytoene i.e. (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
-
-
?
additional information
?
-
squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii
-
-
?
additional information
?
-
squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii
-
-
?
additional information
?
-
-
squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii
-
-
?
additional information
?
-
the enzyme also acts as lycopaoctaene synthase and uses alternative C15 and C20 prenyl diphosphate substrates to produce combinatorial hybrid hydrocarbons, but almost exclusively uses GGPP in vivo. Squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. Ozonolysis experiments suggest lycopatriene and lycopapentaene share an identical reduced C20 moiety with lycopadiene. NMR spectroscopy confirms identity and structure
-
-
?
additional information
?
-
the enzyme also acts as lycopaoctaene synthase and uses alternative C15 and C20 prenyl diphosphate substrates to produce combinatorial hybrid hydrocarbons, but almost exclusively uses GGPP in vivo. Squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. Ozonolysis experiments suggest lycopatriene and lycopapentaene share an identical reduced C20 moiety with lycopadiene. NMR spectroscopy confirms identity and structure
-
-
?
additional information
?
-
-
the enzyme also acts as lycopaoctaene synthase and uses alternative C15 and C20 prenyl diphosphate substrates to produce combinatorial hybrid hydrocarbons, but almost exclusively uses GGPP in vivo. Squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. Ozonolysis experiments suggest lycopatriene and lycopapentaene share an identical reduced C20 moiety with lycopadiene. NMR spectroscopy confirms identity and structure
-
-
?
additional information
?
-
detection of lycopaoctaene synthase activity from an algal homogenate in an assay similar to that of squalene synthase supports the notion that an lycopaoctaene synthase enzyme may be similar to a typical squalene synthase enzyme
-
-
?
additional information
?
-
detection of lycopaoctaene synthase activity from an algal homogenate in an assay similar to that of squalene synthase supports the notion that an lycopaoctaene synthase enzyme may be similar to a typical squalene synthase enzyme
-
-
?
additional information
?
-
-
detection of lycopaoctaene synthase activity from an algal homogenate in an assay similar to that of squalene synthase supports the notion that an lycopaoctaene synthase enzyme may be similar to a typical squalene synthase enzyme
-
-
?
additional information
?
-
the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyse the condensation of two different substrate molecules, forming chimeric products. However, the use of these alternative substrates is not significant in vivo
-
-
?
additional information
?
-
the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyse the condensation of two different substrate molecules, forming chimeric products. However, the use of these alternative substrates is not significant in vivo
-
-
?
additional information
?
-
-
the enzyme can accept (2E,6E)-farnesyl diphosphate and phytyl diphosphate as substrates, and is also able to catalyse the condensation of two different substrate molecules, forming chimeric products. However, the use of these alternative substrates is not significant in vivo
-
-
?
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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
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
squalene + 2 diphosphate + NADP+
-
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
LOS catalyzes the condensation of two GGPP units in the first half reaction to form the cyclopropylcarbinyl diphosphate intermediate PLPP, with concomitant release of one molecule of inorganic diphosphate. In the second half reaction, the PLPP cyclopropyl ring is cleaved and rearranged to form a 1-1' linkage and further reduction by NADPH forms lycopaoctaene. Without NADPH only the reaction intermediate PLPP accumulates
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
the enzyme is involved in biosynthesis of (14E,18E)-lycopadiene overall reaction. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
-
-
?
2 geranylgeranyl diphosphate + NADPH + H+
lycopaoctaene + 2 diphosphate + NADP+
the enzyme is involved in biosynthesis of (14E,18E)-lycopadiene. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
-
-
?
additional information
?
-
squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii
-
-
?
additional information
?
-
squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii
-
-
?
additional information
?
-
-
squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii
-
-
?
additional information
?
-
the enzyme also acts as lycopaoctaene synthase and uses alternative C15 and C20 prenyl diphosphate substrates to produce combinatorial hybrid hydrocarbons, but almost exclusively uses GGPP in vivo. Squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. Ozonolysis experiments suggest lycopatriene and lycopapentaene share an identical reduced C20 moiety with lycopadiene. NMR spectroscopy confirms identity and structure
-
-
?
additional information
?
-
the enzyme also acts as lycopaoctaene synthase and uses alternative C15 and C20 prenyl diphosphate substrates to produce combinatorial hybrid hydrocarbons, but almost exclusively uses GGPP in vivo. Squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. Ozonolysis experiments suggest lycopatriene and lycopapentaene share an identical reduced C20 moiety with lycopadiene. NMR spectroscopy confirms identity and structure
-
-
?
additional information
?
-
-
the enzyme also acts as lycopaoctaene synthase and uses alternative C15 and C20 prenyl diphosphate substrates to produce combinatorial hybrid hydrocarbons, but almost exclusively uses GGPP in vivo. Squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. Ozonolysis experiments suggest lycopatriene and lycopapentaene share an identical reduced C20 moiety with lycopadiene. NMR spectroscopy confirms identity and structure
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
the enzyme uses both NADH and NADPH as reducing agents for lycopaoctaene production, with preference for NADPH
NADPH
the enzyme uses both NADH and NADPH as reducing agents for lycopaoctaene production, with preference for NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
Mn2+ or Mg2+ are effective at low concentration as cofactors for synthesis of lycopersene, for the synthesis of prelycopersene diphosphate, Mn2+ is most effective at very low concentrations, Mg2+ is more effective at higher concentrations
Mn2+
-
Mn2+ or Mg2+ are effective at low concentration as cofactors for synthesis of lycopersene, for the synthesis of prelycopersene diphosphate, Mn2+ is most effective at very low concentrations, Mg2+ is more effective at higher concentrations
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
(2E,6E)-farnesyl diphosphate
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0205
(2E,6E)-farnesyl diphosphate
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.162
(2E,6E)-farnesyl diphosphate
pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
lycopaoctaene synthase (LOS) activity is localized to a membrane system, possibly the endoplasmic reticulum as is seen for squalene synthase
brenda
lycopaoctaene synthase (LOS) activity is localized to a membrane system, possibly the endoplasmic reticulum as is seen for squalene synthase
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
two SSL cDNAs are identified and named based on the function of their encoded proteins as detailed below: Squalene synthase from race L (LSS) and synthase (LOS). Both the LSS and LOS proteins contain all five conserved activity domains, the transmembrane domain and the NADPH-binding residues found in typical squalene synthase enzymes. As LOS may have arisen from an SS paralogue that evolved to accept GGPP as substrate for lycopaoctaene production, LOS may have retained the ability to use (2E,6E)-farnesyl diphosphate to produce squalene. LSS is a true squalene synthase enzyme, whereas LOS appears to be a promiscuous squalene synthase-like (SSL) enzyme with broader substrate chain length and saturation specificity
evolution
two SSL cDNAs are identified and named based on the function of their encoded proteins as detailed below: Squalene synthase from race L (LSS) and synthase (LOS). Both the LSS and LOS proteins contain all five conserved activity domains, the transmembrane domain and the NADPH-binding residues found in typical squalene synthase enzymes. LSS is a true squalene synthase enzyme, whereas LOS appears to be a promiscuous squalene synthase-like (SSL) enzyme with broader substrate chain length and saturation specificity
metabolism
lycopadiene biosynthesis from C20 prenyl diphosphate intermediates can proceed via two possible biosynthetic routes: the first entails C20 geranylgeranyl diphosphate (GGPP) reduction by GGPP reductase to produce C20 phytyl diphosphate. Two molecules of phythyl diphoshate then undergo head-to-head condensation (1-1' linkage) to produce lycopadiene. The second possibility is the head-to-head condensation of two GGPP molecules to produce lycopaoctaene, followed by stepwise enzymatic reduction to produce lycopadiene
metabolism
the enzyme is involved in biosynthesis of (14E,18E)-lycopadiene. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
metabolism
the enzyme is involved in biosynthesis of (14E,18E)-lycopadiene. Lycopaoctaene i.e. 15,15'-dihydrophytoene = (6E,10E,14E,18E,22E,26E)-2,6,10,14,19,23,27,31-octamethyldotriaconta-2,6,10,14,18,22,26,30-octaene
physiological function
squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. trans,trans-Lycopadiene is the predominant hydrocarbon (98% of total hydrocarbons) produced by race L, with a small amount of lycopatriene
physiological function
the enzyme also acts as lycopaoctaene synthase and uses alternative C15 and C20 prenyl diphosphate substrates to produce combinatorial hybrid hydrocarbons, but almost exclusively uses GGPP in vivo, detailed overview. Squalene synthase enzyme diversification results in the production of specialized tetraterpenoid oils in race L of Botryococcus braunii. Race L produces the C40 tetraterpenoid hydrocarbon lycopadiene. trans,trans-Lycopadiene is the predominant hydrocarbon (98% of total hydrocarbons) produced by race L, with a small amount of lycopatriene
additional information
there are three different races of Botryococcus braunii based on the hydrocarbons synthesized. Race A produces fatty acid-derived C23-C33 alkadienes and alkatrienes. Races B and L produce isoprenoid-derived hydrocarbons: methylsqualenes and C30-C37 botryococcene triterpenoids in race B and the C40 tetraterpenoid lycopadiene in race L
additional information
there are three different races of Botryococcus braunii based on the hydrocarbons synthesized. Race A produces fatty acid-derived C23-C33 alkadienes and alkatrienes. Races B and L produce isoprenoid-derived hydrocarbons: methylsqualenes and C30-C37 botryococcene triterpenoids in race B and the C40 tetraterpenoid lycopadiene in race L
additional information
-
there are three different races of Botryococcus braunii based on the hydrocarbons synthesized. Race A produces fatty acid-derived C23-C33 alkadienes and alkatrienes. Races B and L produce isoprenoid-derived hydrocarbons: methylsqualenes and C30-C37 botryococcene triterpenoids in race B and the C40 tetraterpenoid lycopadiene in race L
additional information
there are three different races of Botryococcus braunii based on the hydrocarbons synthesized. Race A produces fatty acid-derived C23-C33 alkadienes and lkatrienes. Races B and L produce isoprenoid-derived hydrocarbons: methylsqualenes and C30-C37 botryococcene triterpenoids in race B and the C40 tetraterpenoid lycopadiene in race L
additional information
there are three different races of Botryococcus braunii based on the hydrocarbons synthesized. Race A produces fatty acid-derived C23-C33 alkadienes and lkatrienes. Races B and L produce isoprenoid-derived hydrocarbons: methylsqualenes and C30-C37 botryococcene triterpenoids in race B and the C40 tetraterpenoid lycopadiene in race L
additional information
-
there are three different races of Botryococcus braunii based on the hydrocarbons synthesized. Race A produces fatty acid-derived C23-C33 alkadienes and lkatrienes. Races B and L produce isoprenoid-derived hydrocarbons: methylsqualenes and C30-C37 botryococcene triterpenoids in race B and the C40 tetraterpenoid lycopadiene in race L
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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). LOS_BOTBR
444
2
50278
Swiss-Prot
other Location (Reliability: 2)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A288F
significant loss of lycopaoctaene production when compared to wild-type. Increased residue size in the mutant blocks binding of geranylgeranyl diphosphate in the S1 pocket
S276Y
significant loss of lycopaoctaene production when compared to wild-type. Increased residue size in the mutant blocks binding of geranylgeranyl diphosphate in the S1 pocket
S276Y/A288F
mutant shows a drastic reduction in the ability to produce lycopaoctaene and C35H58 compared to wild-type enzyme
T65V/A288F
when comparing the M7 double mutant to the parent A288F background, T65V/A288F does not show a difference in lycopaoctaene production, but C35H58 production is slightly increased and squalene formation is significantly reduced
T65V/M180L
activity of the mutant enzyme is similar to that of the wild-type enzyme
T65V/M180L/A288F
mutant shows activity similar to that of the M4 parent background
T65V/M180L/S276Y A288F
in comparison to the M9 parent background, the mutant enzyme shows a further reduction in C35H58 production and no significant change in lycopaoctaene and squalene formation
T65V/M180L/S276Y/A288F/V289C
in comparison to the M9 parent background, the mutant enzyme shows a further reduction in C35H58 production and no significant change in lycopaoctaene and squalene formation
V289C/S276Y
for the V289C/S276Y double mutant, in comparison to the S276Y parent background, a small increase in C35H58 production is observed, whereas the activities for lycopaoctaene and squalene production remain the same
additional information
additional information
mutating Ser276 and Ala288 residues to those found in human squalene synthase largely converts LOS from lycopaoctaene production to C30 squalene production
additional information
-
mutating Ser276 and Ala288 residues to those found in human squalene synthase largely converts LOS from lycopaoctaene production to C30 squalene production
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the enzyme in Escherichia coli
recombinant expression of the enzyme in Escherichia coli, LOS coexpression in Saccharomyces cerevisiae with Arabidopsis thaliana GGPP synthase-11 (AtGGPPS11) resulting in lycopaoctaene production, which is undetectable when AtGGPPS11 is expressed without LOS. Recombinantly expressed in a Saccharomyces cerevisiae SS knockout strain, LOS restores ergosterol prototrophy, indicating its ability to produce squalene in vivo
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Qureshi, A.A.; Barnes, F.J.; Semmler, E.J.; Porter, J.W.
Biosynthesis of prelycopersene pyrophosphate and lycopersene by squalene synthetase
J. Biol. Chem.
248
2755-2767
1973
Saccharomyces cerevisiae
brenda
Thapa, H.R.; Naik, M.T.; Okada, S.; Takada, K.; Molnar, I.; Xu, Y.; Devarenne, T.P.
A squalene synthase-like enzyme initiates production of tetraterpenoid hydrocarbons in Botryococcus braunii Race L
Nat. Commun.
7
11198
2016
Botryococcus braunii (A0A142ZC57), Botryococcus braunii (A0A144YEA5), Botryococcus braunii
brenda
Thapa, H.R.; Tang, S.; Sacchettini, J.C.; Devarenne, T.P.
Tetraterpene Synthase Substrate and Product Specificity in the Green Microalga Botryococcus braunii Race L
ACS Chem. Biol.
12
2408-2416
2017
Botryococcus braunii (A0A142ZC57), Botryococcus braunii
brenda
Zhang, X.; Wen, F.; Xu, Z.; Sun, D.; Chew, W.; Liu, J.
De novo transcriptomic analysis of the oleaginous alga Botryococcus braunii AC768 (Chlorophyta)
J. Appl. Phycol.
31
255-267
2018
Botryococcus braunii (A0A2R2X3A9), Botryococcus braunii AC768 (A0A2R2X3A9)
-
brenda
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Release 2023.1 (January 2023)
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