1.14.19.45: sn-1 oleoyl-lipid 12-desaturase
This is an abbreviated version!
For detailed information about sn-1 oleoyl-lipid 12-desaturase, go to the full flat file.
Word Map on EC 1.14.19.45
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1.14.19.45
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linoleic
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unsaturated
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oleic
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sativa
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oilseed
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polyunsaturated
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camelina
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desaturases
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polyploid
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cereus
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acclimation
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arachis
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monounsaturated
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hypogaea
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crispr-cas9
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fluidity
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hexaploid
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high-oleic
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peanut
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desaturation
- 1.14.19.45
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linoleic
- unsaturated
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oleic
- sativa
-
oilseed
-
polyunsaturated
- camelina
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desaturases
-
polyploid
- cereus
-
acclimation
-
arachis
-
monounsaturated
- hypogaea
-
crispr-cas9
-
fluidity
-
hexaploid
-
high-oleic
- peanut
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desaturation
Reaction
+ 2 reduced ferredoxin [iron-sulfur] cluster + + 2 H+ = + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
Synonyms
acyl-lipid DELTA12 desaturase, bifunctional DELTA12/DELTA15-fatty acid desaturase, CpFAD2, CsFAD2, DELTA(12) fatty acid desaturase, DELTA12 acyl-lipid desaturase, DELTA12 desaturase, DELTA12 fatty acid desaturase, DELTA12-acyl-lipid desaturase, DELTA12-desaturase, DELTA12-fatty acid desaturase, DELTA5 Des, DELTA5 desaturase, DesA, DesA desaturase, FAD2, FAD2-1, FAD2-2, FAD2-3, More, oleate DELTA12desaturase, RKD12, TcasZ12, YALI0B10153g
ECTree
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General Information
General Information on EC 1.14.19.45 - sn-1 oleoyl-lipid 12-desaturase
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evolution
metabolism
physiological function
bifunctional DELTA12/DELTA15-desaturases are widely found in fungi species belonging to Ascomycota and Basidiomycota. Enzyme RKD12 shares higher homology to the Cop-odeA, it only exhibits DELTA12 and DELTA15 desaturation activity on C18 substrates without preference
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)
evolution
Rhodotorula kratochvilovae YM25235
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bifunctional DELTA12/DELTA15-desaturases are widely found in fungi species belonging to Ascomycota and Basidiomycota. Enzyme RKD12 shares higher homology to the Cop-odeA, it only exhibits DELTA12 and DELTA15 desaturation activity on C18 substrates without preference
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Solanum tuberosum L., cv. Desnitsa plants of wild type are transformed with desA gene of DELTA12-acyl-lipid desaturase from Synechocystis sp. PCC 6803. The transformed plants differ from the wild-type by elevated polyunsaturated fatty acids content in membrane lipids and greater resistance to oxidative stress under hypothermia
metabolism
the enzyme is involved in the biosynthesis of linoleic acid
DELTA12-fatty acid desaturase CpFAD2 from Candida parapsilosis is a multifunctional desaturase producing a range of polyunsaturated and hydroxylated fatty acids
physiological function
for better adaptation to low temperatures, YM25235 may have evolved some adaptative mechanisms that might include the alteration of unsaturation levels of fatty acids in membrane lipids involving th enzyme
physiological function
increased RKD12 mRNA expression level and PUFAs content at low temperature might be helpful for the cold adaptation of Rhodosporidium kratochvilovae YM25235
physiological function
the enzyme is involved in growth of Yarrowia lipolytica at low temperature
physiological function
Candida parapsilosis CP-69
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DELTA12-fatty acid desaturase CpFAD2 from Candida parapsilosis is a multifunctional desaturase producing a range of polyunsaturated and hydroxylated fatty acids
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physiological function
Rhodotorula kratochvilovae YM25235
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for better adaptation to low temperatures, YM25235 may have evolved some adaptative mechanisms that might include the alteration of unsaturation levels of fatty acids in membrane lipids involving th enzyme
-
physiological function
Rhodotorula kratochvilovae YM25235
-
increased RKD12 mRNA expression level and PUFAs content at low temperature might be helpful for the cold adaptation of Rhodosporidium kratochvilovae YM25235
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