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Information on EC 1.14.19.6 - acyl-CoA (9+3)-desaturase and Organism(s) Synechocystis sp. and UniProt Accession P20388
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1.14.19.6 acyl-CoA (9+3)-desaturaseIUBMB Comments
This microsomal enzyme introduces a cis double bond at position 12 of fatty-acyl-CoAs that contain a cis double bond at position 9. When acting on 19:1Delta10 fatty acyl-CoA the enzyme from the pathogenic protozoan Trypanosoma brucei introduces the new double bond at position 13, indicating that the new double bond is introduced three carbons from the existing cis double bond, towards the methyl-end of the fatty acid. Requires cytochrome b5 as the electron donor .
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Word Map
- 1.14.19.6
-
linoleic
-
desaturation
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oleic
-
polyunsaturated
- synechocystis
-
alpha-linolenic
- nutrition
The taxonomic range for the selected organisms is: Synechocystis sp.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
2
+
+
2
=
+
2
+
2
Synonyms
delta 12 desaturase, fad-2, delta-12 fatty acid desaturase, le-fad2, ptfad2, delta 12 fatty acid desaturases, ptfad6, klfad2, delta12-fad, egfad2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DesA
-
acyl-CoA (9+3)-desaturase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA,ferrocytochrome b5:oxygen oxidoreductase (12,13 cis-dehydrogenating)
This microsomal enzyme introduces a cis double bond at position 12 of fatty-acyl-CoAs that contain a cis double bond at position 9. When acting on 19:1Delta10 fatty acyl-CoA the enzyme from the pathogenic protozoan Trypanosoma brucei introduces the new double bond at position 13, indicating that the new double bond is introduced three carbons from the existing cis double bond, towards the methyl-end of the fatty acid. Requires cytochrome b5 as the electron donor [4].
CAS REGISTRY NUMBER
COMMENTARY
84628-81-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
oleic acid + reduced acceptor + O2
linoleic acid + acceptor + H2O
-
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
inserted heterologous desA gene for DELTA12 acyl-lipid desaturase in potato plants results in improved tolerance of transformants to oxidative stress due to the more efficient maintenance of stable cell membrane structure functioning, and this permits prevention of electron jump to oxygen and, as a result, of accelerated reactive oxygen species generation
additional information
physiological function
overexpression of the acyl-lipid DELTA12-desaturase in transformed potato plants promotes fatty acid polyunsaturation and presumably averts the accelerated generation of the superoxide anion, thus suppressing lipid peroxidation under low-temperature stress
physiological function
recombinant enzyme expression improves potato plant resistance to Phytophthora infestans infection
physiological function
Solanum tuberosum plants expressing Synechocystis DELTA12-acyl-lipid desaturase experience less severe thermal and oxidative stress upon cooling and can cope with the cold without considerable increase in the enzyme activity
physiological function
the enzyme increases the tolerance to low temperature
physiological function
the expression of DELTA12 acyl-lipid desaturase positively influences stabilization of not only structure but also functioning of chloroplast membranes in Solanum tuberosum, thus preventing a transfer of electrons from the electron transport chain to oxygen and subsequent reactive oxygen species generation at hypothermia
additional information
-
expression profile of desA gene from Synechocystis sp. PCC6803 and its effect on cell membrane lipid composition and cold tolerance in prokaryotic, Escherichia coli and eukaryotic, Solanum tuberosum cells, overview
additional information
expression profile of desA gene from Synechocystis sp. PCC6803 and its effect on cell membrane lipid composition and cold tolerance in prokaryotic, Escherichia coli and eukaryotic, Solanum tuberosum cells, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40500
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE
66000
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of a hybrid of desA and reporter gene encoding thermostable lichenase, licBM3. The desaturase can enhance tolerance to cold stress in potato, and desaturase and lichenase retain their functionality in the structure of the hybrid protein where the enzymatic activity of target gene product is higher than in the case of reporter lichenase gene absence in the construction, phenotypes, overview
additional information
construction of a hybrid of desA and reporter gene encoding thermostable lichenase, licBM3. The desaturase can enhance tolerance to cold stress in potato, and desaturase and lichenase retain their functionality in the structure of the hybrid protein where the enzymatic activity of target gene product is higher than in the case of reporter lichenase gene absence in the construction, phenotypes, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum cells
gene desA, recombinant expression of the desA-licBM3 hybrid in transgenic Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum plants
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
no enhancement of enzyme transcript is observed when cells are incubated in the dark at 22°C
the level of the enzyme transcript increases 10fold within 1 h upon a decrease in temperature from 36°C to 22°C
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Amiri, R.M.; Yureva, N.O.; Shimshilashvili, K.R.; Goldenkova-Pavlova, I.V.; Pchelkin, V.P.; Kuznitsova, E.I.; Tsydendambaev, V.D.; Trunova, T.I.; Los, D.A.; Jouzani, G.S.; Nosov, A.M.
Expression of acyl-lipid Delta12-desaturase gene in prokaryotic and eukaryotic cells and its effect on cold stress tolerance of potato
J. Integr. Plant Biol.
52
289-297
2010
Synechocystis sp., Synechocystis sp. (P20388)
Demin, I.; Naraikina, N.; Tsydendambaev, V.; Moshkov, I.; Trunova, T.
The effect of potato plant transformation with the gene encoding DELTA12-acyl-lipid desaturase on the CO2 exchange and activities of antioxidant enzymes under hypothermia
Russ. J. Plant Physiol.
60
367-374
2013
Synechocystis sp.
-
Demin I, D.I.; Shimshilashvili C, S.C.; YurEva N, Y.N.; Naraykina N, N.N.; Goldenkova-Pavlova I, G.I.; Los D, L.D.; Nosov A, N.A.; Trunova T, T.T.
Overexpression of the acyl-lipid DELTA12-desaturase gene protects potato plants from low temperature damage
Acta Agron. Hung.
59
87-99
2011
Synechocystis sp. (P20388)
-
Los D.; Horvath I.; Vigh L.; Murata N.
The temperature-dependent expression of the desaturase gene desA in Synechocystis PCC6803
FEBS Lett.
318
57-60
1993
Synechocystis sp. (P20388)
Avelange-Macherel M.-H.; Macherel D.; Wada H.; Murata N.
Site-directed mutagenesis of histidine residues in the DELTA12 acyl-lipid desaturase of Synechocystis
FEBS Lett.
361
111-114
1995
Synechocystis sp. (P20388), Synechocystis sp.
Wada, H.; Gombos, Z.; Murata, N.
Enhancement of chilling tolerance of a cyanobacterium by genetic manipulation of fatty acid desaturation
Nature
347
200-203
1990
Synechocystis sp. (P20388)
Sakamoto, T.; Wada, H.; Nishida, I.; Ohmori, M.; Murata, N.
Identification of conserved domains in the DELTA12 desaturases of cyanobacteria
Plant Mol. Biol.
24
643-650
1994
Synechocystis sp. (P20388), Synechococcus sp. (Q55231)
Demin, I.; Deryabin, A.; Sinkevich, M.; Trunova, T.
Insertion of cyanobacterial desA gene coding for DELTA12-acyl-lipid desaturase increases potato plant resistance to oxidative stress induced by hypothermia
Russ. J. Plant Physiol.
55
639-648
2008
Synechocystis sp. (P20388)
-
Astakhova, N.V.; Demin, I.N.; Naraikina, N.V.; Trunova, T.I.
Effect of the desA gene encoding DELTA12 acyl-lipid desaturase on the chloroplast structure and tolerance to hypothermia of potato plants
Russ. J. Plant Physiol.
58
18-23
2011
Synechocystis sp. (P20388)
-
Yureva, N.O.; Kirsanova, S.N.; Kukushkina, L.N.; Pchelkin, V.P.; Sobolkova, G.I.; Nikiforova, K.R.; Goldenkova-Pavlova, I.V.; Nosov, A.M.; Tsydendambaev, V.D.
Expression of the gene encoding DELTA12 acyl-lipid desaturase from Synechocystis sp. PCC 6803 improves potato plant resistance to late blight infection
Russ. J. Plant Physiol.
61
672-678
2014
Synechocystis sp. (P20388)
-
Gerasymenko, I.M.; Sakhno, L.A.; Kyrpa, T.N.; Ostapchuk, A.M.; Hadjiev, T.A.; Goldenkova-Pavlova, I.V.; Sheludko, Y.V.
Characterization of Nicotiana tabacum plants expressing hybrid genes of cyanobacterial DELTA9 or DELTA12 acyl-lipid desaturases and thermostable lichenase
Russ. J. Plant Physiol.
62
283-291
2015
Synechocystis sp. (P20388)
-
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