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Literature summary extracted from

  • 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 (2010), J. Integr. Plant Biol., 52, 289-297.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.19.6 expressed in Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum cells Synechocystis sp.
1.14.19.6 gene desA, recombinant expression of the desA-licBM3 hybrid in transgenic Escherichia coli strains XL1Blue and BL21 and Solanum tuberosum plants Synechocystis sp.
1.14.19.22 gene desA, expression profile analysis, construction of a hybrid of desA and reporter gene encoding thermostable lichenase, licBM3, and expression in Escherichia coli strain XL1blue and Solanum tuberosum cells, the latter via Agrobacterium tumefaciens strain AGLO transfection. The desaturase can enhance tolerance to cold stress in potato, and desaturase and lichenase retain their functionality in the structure of a recombinant hybrid protein where the enzymatic activity of target gene product is higher than in the case of reporter lichenase gene absence in the construction Synechocystis sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.14.19.6 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 Synechocystis sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.19.6 40500
-
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE Synechocystis sp.
1.14.19.6 66000
-
x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE Synechocystis sp.
1.14.19.6 66000
-
x * 66000, DesA As hybrid with lichenase LicBM3, SDS-PAGE Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.19.6 1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+ Synechocystis sp.
-
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.19.6 Synechocystis sp.
-
gene desA
-
1.14.19.6 Synechocystis sp. P20388
-
-
1.14.19.22 Synechocystis sp.
-
gene desA
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.19.6 1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
Synechocystis sp. 1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.14.19.6 ? x * 40500, DesA, SDS-PAGE, x * 66000, about, recombinant DesA-LicBM3 hybrid protein, SDS-PAGE Synechocystis sp.
1.14.19.6 ? x * 66000, DesA As hybrid with lichenase LicBM3, SDS-PAGE Synechocystis sp.

Synonyms

EC Number Synonyms Comment Organism
1.14.19.6 acyl-lipid DELTA12-desaturase
-
Synechocystis sp.
1.14.19.6 DesA
-
Synechocystis sp.
1.14.19.22 acyl-lipid DELTA12-desaturase
-
Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.19.6 Ferredoxin
-
Synechocystis sp.

General Information

EC Number General Information Comment Organism
1.14.19.6 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 Synechocystis sp.
1.14.19.22 physiological function functional recombinant hybird desaturase-lichenase protein can enhance tolerance to cold stress in transgenic potato, overview Synechocystis sp.