BRENDA - Enzyme Database
show all sequences of 1.14.19.39

Identification and functional characterization of two DELTA12-fatty acid desaturases associated with essential linoleic acid biosynthesis in Physcomitrella patens

Chodok, P.; Eiamsa-ard, P.; Cove, D.J.; Quatrano, R.S.; Kaewsuwan, S.; J. Ind. Microbiol. Biotechnol. 40, 901-913 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene PpFAD2-2, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Saccharomyces cerevisiae strain INVSc1; genes PpFAD2-1, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Saccharomyces cerevisiae strain INVSc1
Physcomitrella patens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
the transmembrane protein PpFAD2-1 contains three conserved histidine-rich motifs: the HXXXH motif from amino acid residue 99 to 103 (HECGH), the HXXHH motif from amino acid residue 135 to 139 (HRRHH), and the HXXHH motif from amino acid residue 309 to 313 (HVAHH) in the C-terminus; the transmembrane protein PpFAD2-2 contains three conserved histidine-rich motifs: the HXXXH motif from amino acid residue 99 to 103 (HECGH), the HXXHH motif from amino acid residue 135 to 139 (HRRHH), and the HXXHH motif from amino acid residue 309 to 313 (HVAHH) in the C-terminus
Physcomitrella patens
5789
-
microsome
;
Physcomitrella patens
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phosphatidylcholine + reduced cytochrome b5 + O2
Physcomitrella patens
with NADH
? + cytochrome b5 + 2 H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Physcomitrella patens
A9RQ27
FAD2-2; gene PpFAD2-2
-
Physcomitrella patens
A9RV06
FAD2-1; gene PpFAD2-1 encoding two isozymes
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphatidylcholine + reduced cytochrome b5 + O2
with NADH
728074
Physcomitrella patens
? + cytochrome b5 + 2 H2O
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
gene PpFAD2-2, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Saccharomyces cerevisiae strain INVSc1
Physcomitrella patens
genes PpFAD2-1, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, expression in Saccharomyces cerevisiae strain INVSc1
Physcomitrella patens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
the transmembrane protein PpFAD2-1 contains three conserved histidine-rich motifs: the HXXXH motif from amino acid residue 99 to 103 (HECGH), the HXXHH motif from amino acid residue 135 to 139 (HRRHH), and the HXXHH motif from amino acid residue 309 to 313 (HVAHH) in the C-terminus
Physcomitrella patens
5789
-
endoplasmic reticulum membrane
the transmembrane protein PpFAD2-2 contains three conserved histidine-rich motifs: the HXXXH motif from amino acid residue 99 to 103 (HECGH), the HXXHH motif from amino acid residue 135 to 139 (HRRHH), and the HXXHH motif from amino acid residue 309 to 313 (HVAHH) in the C-terminus
Physcomitrella patens
5789
-
microsome
-
Physcomitrella patens
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
phosphatidylcholine + reduced cytochrome b5 + O2
Physcomitrella patens
with NADH
? + cytochrome b5 + 2 H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
phosphatidylcholine + reduced cytochrome b5 + O2
with NADH
728074
Physcomitrella patens
? + cytochrome b5 + 2 H2O
-
-
-
?
General Information
General Information
Commentary
Organism
evolution
the microsomal DELTA12-fatty acid desaturase (FAD2) is located in the endoplasmic reticulum and uses phosphatidylcholine as acyl substrate and NADH, NADH-cytochrome b5 reductase, and cytochrome b5 as electron donors. This reaction involves concomitant reduction of molecular oxygen to water. In contrast, the plastidial DELTA12-fatty acid desaturase (FAD6) is located in the chloroplast and uses primarily glycolipids as acyl carriers and NAD(P)H, ferredoxin-NAD(P) reductase, and ferredoxin as electron donors; the microsomal DELTA12-fatty acid desaturase (FAD2) is located in the endoplasmic reticulum and uses phosphatidylcholine as acyl substrate and NADH, NADH-cytochrome b5 reductase, and cytochrome b5 as electron donors. This reaction involves concomitant reduction of molecular oxygen to water. In contrast, the plastidial DELTA12-fatty acid desaturase (FAD6) is located in the chloroplast and uses primarily glycolipids as acyl carriers and NAD(P)H, ferredoxin-NAD(P) reductase, and ferredoxin as electron donors
Physcomitrella patens
additional information
the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes; the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes
Physcomitrella patens
General Information (protein specific)
General Information
Commentary
Organism
evolution
the microsomal DELTA12-fatty acid desaturase (FAD2) is located in the endoplasmic reticulum and uses phosphatidylcholine as acyl substrate and NADH, NADH-cytochrome b5 reductase, and cytochrome b5 as electron donors. This reaction involves concomitant reduction of molecular oxygen to water. In contrast, the plastidial DELTA12-fatty acid desaturase (FAD6) is located in the chloroplast and uses primarily glycolipids as acyl carriers and NAD(P)H, ferredoxin-NAD(P) reductase, and ferredoxin as electron donors
Physcomitrella patens
additional information
the isozyme contains the three histidine clusters typical of the catalytic domains of DELTA12-desaturase enzymes
Physcomitrella patens
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
-
-
1
-
-
-
-
-
3
-
-
-
-
2
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
728074
Chodok
Identification and functional ...
Physcomitrella patens
J. Ind. Microbiol. Biotechnol.
40
901-913
2013
-
-
1
-
-
-
-
-
2
-
-
2
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
4
-
-
-
725452
Zhou
Caenorhabditis elegans ?12-des ...
Caenorhabditis elegans
J. Biol. Chem.
286
43644-43650
2011
-
-
1
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
715539
Blacklock
Functional diversity in fungal ...
Cantharellus formosus
J. Biol. Chem.
285
28442-28449
2010
-
-
1
-
-
-
-
-
-
1
-
1
-
8
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
675151
Nam
Cloning and transcriptional an ...
Crepis alpina, Helianthus annuus
J. Exp. Bot.
58
1421-1432
2007
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679861
Zhang
Identification of a novel bifu ...
Coprinopsis cinerea, Coprinopsis cinerea TD#822-2
FEBS Lett.
581
315-319
2007
-
-
1
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684454
Harwood
Temperature stress: reacting a ...
Acanthamoeba castellanii
Ann. N. Y. Acad. Sci.
1113
52-57
2007
1
-
1
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
658641
Carlsson
Properties of two multifunctio ...
Crepis alpina
Eur. J. Biochem.
271
2991-2997
2004
-
-
1
-
-
-
-
-
-
-
-
-
-
7
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657528
Minto
Synthesis and conformational s ...
Crepis alpina
Anal. Biochem.
308
134-140
2002
-
-
1
-
-
-
-
-
1
-
-
1
-
2
-
-
1
-
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285468
Lee
Identification of non-heme dii ...
Crepis alpina
Science
280
915-918
1998
-
-
1
-
-
-
1
-
2
-
-
1
-
1
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
2
-
-
1
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-