BRENDA - Enzyme Database show
show all sequences of 2.5.1.96

Directed evolution of squalene synthase for dehydrosqualene biosynthesis

Furubayashi, M.; Li, L.; Katabami, A.; Saito, K.; Umeno, D.; FEBS Lett. 588, 3375-3381 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene ysqs, recombinant expression of the engineered mutant enzyme in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
Saccharomyces cerevisiae
recombinant expression of the endgineered enzymes in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
Homo sapiens
recombinant expression of the engineered mutant enzyme in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
Thermosynechococcus elongatus
Engineering
Amino acid exchange
Commentary
Organism
G856A/G1125A/T1128C/T1176C
directed evolution of squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by mutation of gene ysqs
Saccharomyces cerevisiae
additional information
directed evolution of squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by mutation gene tsqs replacement with the human gene mutant Q33R/D34N/S38N/G856A/G1125A/T1128C/T1176C
Thermosynechococcus elongatus
Q33R/D34N/S38N
directed evolution of human Q33R/D34N/S38N mutant squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by replacement of hsqs in pAC-hsqs with the Saccharomyces mutant gene ysqs G856A/G1125A/T1128C/T1176C
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2E,6E)-farnesyl diphosphate
Homo sapiens
-
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
?
(2E,6E)-farnesyl diphosphate
Saccharomyces cerevisiae
-
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
?
(2E,6E)-farnesyl diphosphate
Thermosynechococcus elongatus
-
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
?
additional information
Homo sapiens
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
?
-
-
-
additional information
Saccharomyces cerevisiae
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
?
-
-
-
additional information
Thermosynechococcus elongatus
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-
Thermosynechococcus elongatus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2E,6E)-farnesyl diphosphate
-
738235
Homo sapiens
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
-
738235
Saccharomyces cerevisiae
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
-
738235
Thermosynechococcus elongatus
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
additional information
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
738235
Homo sapiens
?
-
-
-
-
additional information
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
738235
Saccharomyces cerevisiae
?
-
-
-
-
additional information
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
738235
Thermosynechococcus elongatus
?
-
-
-
-
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of the endgineered enzymes in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
Homo sapiens
gene ysqs, recombinant expression of the engineered mutant enzyme in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
Saccharomyces cerevisiae
recombinant expression of the engineered mutant enzyme in Escherichia coli strain XL1-Blue, coexpression with gene crtN encoding DSQ desaturase from Staphylococcus aureus in Escherichia coli results in carotinoid production and accumulation of C30 carotenoid pigments, which does not happen with coexpression of gene crtI encoding Pantoea ananatis phytoene desaturase, carotenoid pigment analysis, overview
Thermosynechococcus elongatus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
G856A/G1125A/T1128C/T1176C
directed evolution of squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by mutation of gene ysqs
Saccharomyces cerevisiae
additional information
directed evolution of squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by mutation gene tsqs replacement with the human gene mutant Q33R/D34N/S38N/G856A/G1125A/T1128C/T1176C
Thermosynechococcus elongatus
Q33R/D34N/S38N
directed evolution of human Q33R/D34N/S38N mutant squalene synthase, EC 2.5.1.21, in an attempt to mimic the activity of dehydroqsqualene synthase, EC 2.5.1.96, by replacement of hsqs in pAC-hsqs with the Saccharomyces mutant gene ysqs G856A/G1125A/T1128C/T1176C
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2E,6E)-farnesyl diphosphate
Homo sapiens
-
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
?
(2E,6E)-farnesyl diphosphate
Saccharomyces cerevisiae
-
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
?
(2E,6E)-farnesyl diphosphate
Thermosynechococcus elongatus
-
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
?
additional information
Homo sapiens
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
?
-
-
-
additional information
Saccharomyces cerevisiae
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
?
-
-
-
additional information
Thermosynechococcus elongatus
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2E,6E)-farnesyl diphosphate
-
738235
Homo sapiens
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
-
738235
Saccharomyces cerevisiae
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate
-
738235
Thermosynechococcus elongatus
15-cis-4,4'-diapophytoene + 2 diphosphate
-
-
-
?
additional information
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
738235
Homo sapiens
?
-
-
-
-
additional information
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
738235
Saccharomyces cerevisiae
?
-
-
-
-
additional information
reaction mechanism of squalene and dehydrosqualene formation and their conversion into carotenoid pigments, overview
738235
Thermosynechococcus elongatus
?
-
-
-
-
General Information
General Information
Commentary
Organism
malfunction
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
Homo sapiens
malfunction
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
Saccharomyces cerevisiae
malfunction
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
Thermosynechococcus elongatus
General Information (protein specific)
General Information
Commentary
Organism
malfunction
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
Homo sapiens
malfunction
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
Saccharomyces cerevisiae
malfunction
a mutant of squalene synthase is converted to a dehydrosqualene synthase, the various mutations are lustered around the residues that are proposed to be important for NADPH binding
Thermosynechococcus elongatus
Other publictions for EC 2.5.1.96
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
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)
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Directed evolution of squalene ...
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FEBS Lett.
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3375-3381
2014
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3
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Binding modes of zaragozic aci ...
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18750-18757
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722921
Lin
Head-to-head prenyl tranferase ...
Staphylococcus aureus
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3
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2
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715199
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Lactobacillus plantarum
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140
34-39
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-
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1
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1
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1
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715673
Kahlon
Molecular docking studies to m ...
Staphylococcus aureus
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28
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2010
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1
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2
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716765
Lin
Mechanism of action and inhibi ...
Staphylococcus aureus
Proc. Natl. Acad. Sci. USA
107
21337-21342
2010
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1
1
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713989
Koecher
Structure, function and biosyn ...
Halobacillus halophilus, Halobacillus halophilus DSM 2266T
Arch. Microbiol.
191
95-104
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1
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4
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715841
Song
Phosphonosulfonates are potent ...
Staphylococcus aureus
J. Med. Chem.
52
976-988
2009
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1
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7
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1
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7
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716919
Liu
A cholesterol biosynthesis inh ...
Staphylococcus aureus
Science
319
1391-1394
2008
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1
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4
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713819
Ku
Preparation, characterization, ...
Staphylococcus aureus
Appl. Environ. Microbiol.
71
6578-6583
2005
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1
1
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715351
Umeno
Evolution of a pathway to nove ...
Staphylococcus aureus, Staphylococcus aureus ATCC 35556
J. Bacteriol.
186
1531-1536
2004
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1
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10
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715332
Wieland
Genetic and biochemical analys ...
Staphylococcus aureus, Staphylococcus aureus Newman
J. Bacteriol.
176
7719-7726
1994
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1
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