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show all sequences of 1.14.19.13

Molecular cloning and characterization of the genes encoding a microsomal oleate DELTA12 desaturase (CsFAD2) and linoleate DELTA15 desaturase (CsFAD3) from Camelina sativa

Rodriguez-Rodriguez, M.; Salas, J.; Venegas-Caleron, M.; Garces, R.; Martinez-Force, E.; Ind. Crops Prod. 89, 405-415 (2016)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene CsFAD3, variant FAD3-1, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview; gene CsFAD3, variant FAD3-2, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview; gene CsFAD3, variant FAD3-3, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview
Camelina sativa
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
-
Camelina sativa
5783
-
membrane
integral membrane enzyme; integral membrane enzyme; integral membrane enzyme
Camelina sativa
16020
-
microsome
-
Camelina sativa
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
two Fe2+ ions bound in the His box; two Fe2+ ions bound in the His box; two Fe2+ ions bound in the His box
Camelina sativa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Camelina sativa
A0A059V6T7
FAD3-2
-
Camelina sativa
A0A059V8B3
FAD3-3
-
Camelina sativa
A0A059V8R1
FAD3-1
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cotyledon
-
Camelina sativa
-
hypocotyl
-
Camelina sativa
-
leaf
-
Camelina sativa
-
root
-
Camelina sativa
-
seed
developing, high expression level, particularly from 6 to 12 days after flowering and from 18 to 24 days after flowering, corresponding with the phases of seed expansion and oil accumulation respectively; developing, high expression level, particularly from 6 to 12 days of flowering and from 18 to 24 days of flowering, corresponding with the phases of seed expansion and oil accumulation respectively; developing, high expression level, particularly from 6 to 12 days of flowering and from 18 to 24 days of flowering, corresponding with the phases of seed expansion and oil accumulation respectively
Camelina sativa
-
Subunits
Subunits
Commentary
Organism
?
x * 44300, about, sequence calculation; x * 44400, about, sequence calculation; x * 44500, about, sequence calculation
Camelina sativa
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Camelina sativa
sequence calculation; sequence calculation; sequence calculation
-
8.4
Cloned(Commentary) (protein specific)
Commentary
Organism
gene CsFAD3, variant FAD3-1, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview
Camelina sativa
gene CsFAD3, variant FAD3-2, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview
Camelina sativa
gene CsFAD3, variant FAD3-3, DNA and amino acid sequence determination and analysis, genetic structure, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, subcloning in Escherichia coli strain XL1-Blue, and functional recombinant expression in Saccharomyces cerevisiae strain W303-1A. The conversion driven by recombinant CsFAD3 is enhanced 5fold at 22C compared to 30C, although it is not able to desaturate 16:2DELTA9,12. Fatty acid composition of Saccharomyces cerevisiae cells overexpressing CsFAD3 microsomal desaturase and grown at two different temperatures, overview
Camelina sativa
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum
-
Camelina sativa
5783
-
membrane
integral membrane enzyme
Camelina sativa
16020
-
microsome
-
Camelina sativa
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
two Fe2+ ions bound in the His box
Camelina sativa
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cotyledon
-
Camelina sativa
-
hypocotyl
-
Camelina sativa
-
leaf
-
Camelina sativa
-
root
-
Camelina sativa
-
seed
developing, high expression level, particularly from 6 to 12 days of flowering and from 18 to 24 days of flowering, corresponding with the phases of seed expansion and oil accumulation respectively
Camelina sativa
-
seed
developing, high expression level, particularly from 6 to 12 days after flowering and from 18 to 24 days after flowering, corresponding with the phases of seed expansion and oil accumulation respectively
Camelina sativa
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 44300, about, sequence calculation
Camelina sativa
?
x * 44500, about, sequence calculation
Camelina sativa
?
x * 44400, about, sequence calculation
Camelina sativa
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Camelina sativa
sequence calculation
-
8.4
General Information
General Information
Commentary
Organism
evolution
three different copies of the genes FAD2 and FAD3 are identified, which contain three histidine rich motifs (HXCGHX, HRXHH andHVXHH) and six highly conserved transmembrane domains. Comparing their sequences, the CsFAD2copies accommodate four conservative changes (E36D, R48H, V97A, and A177P) and two semi-conservative ones (V63I and L249M), whereas only one semi-conservative change (A327S) is detected in CsFAD3 but with two extra amino acids (H147 and G148); three different copies of the genes FAD2 and FAD3 are identified, which contain three histidine rich motifs (HXCGHX, HRXHH andHVXHH) and six highly conserved transmembrane domains. Comparing their sequences, the CsFAD2copies accommodate four conservative changes (E36D, R48H, V97A, and A177P) and two semi-conservative ones (V63I and L249M), whereas only one semi-conservative change (A327S) is detected in CsFAD3 but with two extra amino acids (H147 and G148); three different copies of the genes FAD2 and FAD3 are identified, which contain three histidine rich motifs (HXCGHX, HRXHH andHVXHH) and six highly conserved transmembrane domains. Comparing their sequences, the CsFAD2copies accommodate four conservative changes (E36D, R48H, V97A, and A177P) and two semi-conservative ones (V63I and L249M), whereas only one semi-conservative change (A327S) is detected in CsFAD3 but with two extra amino acids (H147 and G148)
Camelina sativa
General Information (protein specific)
General Information
Commentary
Organism
evolution
three different copies of the genes FAD2 and FAD3 are identified, which contain three histidine rich motifs (HXCGHX, HRXHH andHVXHH) and six highly conserved transmembrane domains. Comparing their sequences, the CsFAD2copies accommodate four conservative changes (E36D, R48H, V97A, and A177P) and two semi-conservative ones (V63I and L249M), whereas only one semi-conservative change (A327S) is detected in CsFAD3 but with two extra amino acids (H147 and G148)
Camelina sativa
Other publictions for EC 1.14.19.13
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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