BRENDA - Enzyme Database
show all sequences of 1.3.1.96

Structure-function mapping of key determinants for hydrocarbon biosynthesis by squalene and squalene synthase-like enzymes from the green alga Botryococcus braunii race B

Bell, S.A.; Niehaus, T.D.; Nybo, S.E.; Chappell, J.; Biochemistry 53, 7570-7581 (2014)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
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)
Botryococcus braunii
Engineering
Protein Variants
Commentary
Organism
Y168A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Botryococcus braunii
Y168F
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Botryococcus braunii
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound
Botryococcus braunii
16020
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Botryococcus braunii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Botryococcus braunii
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
?
-
-
?
presqualene diphosphate + NADPH + H+
Botryococcus braunii
-
squalene + diphosphate + NADP+
-
-
r
Organism
Organism
UniProt
Commentary
Textmining
Botryococcus braunii
G0Y287
race B
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
analysis of substrate specificity, overview
741903
Botryococcus braunii
?
-
-
-
?
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
741903
Botryococcus braunii
?
-
-
-
?
presqualene diphosphate + NADPH + H+
-
741903
Botryococcus braunii
squalene + diphosphate + NADP+
-
-
-
r
Synonyms
Synonyms
Commentary
Organism
SSL-2
-
Botryococcus braunii
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Botryococcus braunii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Botryococcus braunii
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Botryococcus braunii
NADPH
-
Botryococcus braunii
Cloned(Commentary) (protein specific)
Commentary
Organism
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)
Botryococcus braunii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Botryococcus braunii
NADPH
-
Botryococcus braunii
Engineering (protein specific)
Protein Variants
Commentary
Organism
Y168A
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Botryococcus braunii
Y168F
site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type
Botryococcus braunii
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
bound
Botryococcus braunii
16020
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Botryococcus braunii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Botryococcus braunii
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
?
-
-
?
presqualene diphosphate + NADPH + H+
Botryococcus braunii
-
squalene + diphosphate + NADP+
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
analysis of substrate specificity, overview
741903
Botryococcus braunii
?
-
-
-
?
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
741903
Botryococcus braunii
?
-
-
-
?
presqualene diphosphate + NADPH + H+
-
741903
Botryococcus braunii
squalene + diphosphate + NADP+
-
-
-
r
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Botryococcus braunii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Botryococcus braunii
General Information
General Information
Commentary
Organism
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
Botryococcus braunii
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
Botryococcus braunii
General Information (protein specific)
General Information
Commentary
Organism
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
Botryococcus braunii
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
Botryococcus braunii
Other publictions for EC 1.3.1.96
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
741903
Bell
Structure-function mapping of ...
Botryococcus braunii
Biochemistry
53
7570-7581
2014
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1
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2
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1
1
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2
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1
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3
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1
1
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1
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1
2
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2
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1
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3
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1
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1
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2
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720061
Niehaus
Functional identification of t ...
Botryococcus braunii
J. Biol. Chem.
287
8163-8173
2012
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4
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720917
Niehaus
Identification of unique mecha ...
Botryococcus braunii
Proc. Natl. Acad. Sci. USA
108
12260-12265
2011
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5
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1
1
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718688
Okada
Characterization of botryococc ...
Botryococcus braunii, Botryococcus braunii Berkeley (Showa)
Arch. Biochem. Biophys.
422
110-118
2004
1
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3
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1
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3
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489850
Okada
Molecular characterization of ...
Botryococcus braunii, Botryococcus braunii Berkeley
Arch. Biochem. Biophys.
373
307-317
2000
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