BRENDA - Enzyme Database show
show all sequences of 1.14.19.39

Caenorhabditis elegans ?12-desaturase FAT-2 is a bifunctional desaturase able to desaturate a diverse range of fatty acid substrates at the DELTA12 and DELTA15 positions

Zhou, X.; Green, A.; Singh, S.; J. Biol. Chem. 286, 43644-43650 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene fat-2, sequence comparison and phylogenetic tree, expression in Saccharomyces cerevisiae strain S288C
Caenorhabditis elegans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Caenorhabditis elegans
G5EGA5
gene fat-2
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + AH2 + O2
-
725452
Caenorhabditis elegans
crepenynate + A + 2 H2O
-
-
-
?
additional information
the enzyme is able to desaturate C16 and C18 fatty acids. When recombinantly expressed in yeast cells, the enzyme can also catalyze DELTA15 desaturation. The recombinant enzyme can also produce C14:2DELTA9,12, C15:2DELTA9,12, C17:2DELTA9,12, and C18:4DELTA6,9,12,15 when C14:1DELTA9, C15:1DELTA9, C17:1DELTA9, and C18:3DELTA6,9,12 substrates are available in yeast cells, product mass spectrometry analysis
725452
Caenorhabditis elegans
?
-
-
-
-
oleate + AH2 + O2
recombinant enzyme
725452
Caenorhabditis elegans
linoleic acid + linolenic acid + A + 2 H2O
-
-
-
?
palmitoleic acid + O2
recombinant enzyme
725452
Caenorhabditis elegans
hexadecadienoic acid + hexadecatrienoic acid + A + 2 H2O
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
gene fat-2, sequence comparison and phylogenetic tree, expression in Saccharomyces cerevisiae strain S288C
Caenorhabditis elegans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + AH2 + O2
-
725452
Caenorhabditis elegans
crepenynate + A + 2 H2O
-
-
-
?
additional information
the enzyme is able to desaturate C16 and C18 fatty acids. When recombinantly expressed in yeast cells, the enzyme can also catalyze DELTA15 desaturation. The recombinant enzyme can also produce C14:2DELTA9,12, C15:2DELTA9,12, C17:2DELTA9,12, and C18:4DELTA6,9,12,15 when C14:1DELTA9, C15:1DELTA9, C17:1DELTA9, and C18:3DELTA6,9,12 substrates are available in yeast cells, product mass spectrometry analysis
725452
Caenorhabditis elegans
?
-
-
-
-
oleate + AH2 + O2
recombinant enzyme
725452
Caenorhabditis elegans
linoleic acid + linolenic acid + A + 2 H2O
-
-
-
?
palmitoleic acid + O2
recombinant enzyme
725452
Caenorhabditis elegans
hexadecadienoic acid + hexadecatrienoic acid + A + 2 H2O
-
-
-
?
Other publictions for EC 1.14.19.39
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)
745739
Dehghan Nayeri
Bioinformatics study of delta ...
Ricinus communis
Mol. Biol. Rep.
41
5077-5087
2014
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725452
Zhou
Caenorhabditis elegans ?12-des ...
Caenorhabditis elegans
J. Biol. Chem.
286
43644-43650
2011
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Blacklock
Functional diversity in fungal ...
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Nam
Cloning and transcriptional an ...
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Zhang
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Properties of two multifunctio ...
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