BRENDA - Enzyme Database
show all sequences of 1.14.19.45

Identification of conserved domains in the DELTA12 desaturases of cyanobacteria

Sakamoto, T.; Wada, H.; Nishida, I.; Ohmori, M.; Murata, N.; Plant Mol. Biol. 24, 643-650 (1994)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40300
-
x * 40300, calculated from amino acid sequence
Synechocystis sp.
41300
-
x * 41300, calculated from amino acid sequence
Trichormus variabilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
Trichormus variabilis
-
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Synechocystis sp.
Q55230
-
-
Trichormus variabilis
Q79F72
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
734926
Synechocystis sp.
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
734926
Trichormus variabilis
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 40300, calculated from amino acid sequence
Synechocystis sp.
?
x * 41300, calculated from amino acid sequence
Trichormus variabilis
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Synechocystis sp.
Ferredoxin
-
Trichormus variabilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Synechocystis sp.
Ferredoxin
-
Trichormus variabilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40300
-
x * 40300, calculated from amino acid sequence
Synechocystis sp.
41300
-
x * 41300, calculated from amino acid sequence
Trichormus variabilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
Trichormus variabilis
-
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
734926
Synechocystis sp.
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-oleoyl-2-acyl-[glycerolipid] + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
734926
Trichormus variabilis
1-linoleoyl-2-acyl-[glycerolipid] + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40300, calculated from amino acid sequence
Synechocystis sp.
?
x * 41300, calculated from amino acid sequence
Trichormus variabilis
Other publictions for EC 1.14.19.45
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)
744244
Tezaki
DELTA12-fatty acid desaturase ...
Yarrowia lipolytica
Biochem. Biophys. Res. Commun.
488
165-170
2017
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1
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1
1
1
1
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-
744576
Cui
Identification and characteri ...
Rhodotorula kratochvilovae, Rhodotorula kratochvilovae YM25235
Biotechnol. Lett.
38
1155-1164
2016
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-
1
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3
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2
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1
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1
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5
1
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1
2
2
1
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744937
Diomande
Expression of the genes encod ...
Bacillus cereus, Bacillus cereus ATCC 14579
FEMS Microbiol. Lett.
363
fnw174
2016
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4
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2
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4
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745028
Sun
Identification of a DELTA12 f ...
Elaeis guineensis, Elaeis guineensis Jacq.
Gene
591
21-26
2016
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-
1
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2
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2
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1
1
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745061
Rodriguez-Rodriguez
-
Molecular cloning and charact ...
Camelina sativa
Ind. Crops Prod.
89
405-415
2016
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1
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3
1
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3
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5
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1
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3
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9
3
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15
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3
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3
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1
3
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746429
Gerasymenko
-
Characterization of Nicotiana ...
Synechocystis sp., Synechocystis sp. PCC 6803
Russ. J. Plant Physiol.
62
283-291
2015
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-
2
-
1
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1
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2
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1
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744454
Zagoskina N.V
-
Morphophysiological and bioch ...
Synechocystis sp. PCC 6803
Biol. Bull.
41
126-132
2014
-
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1
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1
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1
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745074
Haritos
Unexpected functional diversi ...
Tribolium castaneum
Insect Biochem. Mol. Biol.
51
62-70
2014
-
-
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1
-
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1
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746264
Bucek
DELTA12-Fatty acid desaturase ...
Candida parapsilosis, Candida parapsilosis CP-69
PLoS ONE
9
e93322
2014
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1
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2
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2
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6
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1
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2
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6
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1
1
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746428
Naraikina N.V
-
Changes in the activity of su ...
Synechocystis sp.
Russ. J. Plant Physiol.
61
332-338
2014
-
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1
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1
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1
1
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733169
Chazarreta Cifre
Exploring the biosynthesis of ...
Bacillus cereus, Bacillus cereus ATCC 14579
Appl. Environ. Microbiol.
79
6271-6279
2013
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1
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1
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1
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8
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2
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1
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728791
Demin
-
Integration of the cyanobacter ...
Synechocystis sp.
Russ. J. Plant Physiol.
58
660-666
2011
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1
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1
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1
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734926
Sakamoto
Identification of conserved do ...
Synechocystis sp., Trichormus variabilis
Plant Mol. Biol.
24
643-650
1994
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2
2
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2
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2
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2
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2
2
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2
2
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