BRENDA - Enzyme Database show
show all sequences of 1.14.19.39

Synthesis and conformational studies of a transmembrane domain from a diverged microsomal DELTA12-desaturase

Minto, R.E.; Gibbons, W.J., Jr.; Cardon, T.B.; Lorigan, G.A.; Anal. Biochem. 308, 134-140 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
chemical in vitro synthesis of a segment of the amino-proximate transmembrane domain TM-A, overview
Crepis alpina
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Crepis alpina
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + reduced acceptor + O2
Crepis alpina
first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters
crepenynate + acceptor + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Crepis alpina
-
-
-
Purification (Commentary)
Commentary
Organism
chemically constructed segment of the amino-proximate transmembrane domain TM-A by reversed phase chromatography
Crepis alpina
Source Tissue
Source Tissue
Commentary
Organism
Textmining
seed
-
Crepis alpina
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + reduced acceptor + O2
-
657528
Crepis alpina
crepenynate + acceptor + H2O
-
-
-
?
linoleate + reduced acceptor + O2
first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters
657528
Crepis alpina
crepenynate + acceptor + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
secondary structure of the enzyme in a membrane bilayer, modeling, conformational studies of the recombinant segment of transmembrane domain TM-A, a hydrophobic peptide, which mainly folds into an alpha-helical structure, the helical content of the structure is increased in 40-80% 2,2,2-trifluoroethanol, overview
Crepis alpina
Cloned(Commentary) (protein specific)
Commentary
Organism
chemical in vitro synthesis of a segment of the amino-proximate transmembrane domain TM-A, overview
Crepis alpina
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Crepis alpina
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + reduced acceptor + O2
Crepis alpina
first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters
crepenynate + acceptor + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
chemically constructed segment of the amino-proximate transmembrane domain TM-A by reversed phase chromatography
Crepis alpina
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
seed
-
Crepis alpina
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + reduced acceptor + O2
-
657528
Crepis alpina
crepenynate + acceptor + H2O
-
-
-
?
linoleate + reduced acceptor + O2
first committed step in the biosynthesis of fatty acid-derived acetylenic secondary natural products, e.g. matricaria esters
657528
Crepis alpina
crepenynate + acceptor + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
secondary structure of the enzyme in a membrane bilayer, modeling, conformational studies of the recombinant segment of transmembrane domain TM-A, a hydrophobic peptide, which mainly folds into an alpha-helical structure, the helical content of the structure is increased in 40-80% 2,2,2-trifluoroethanol, overview
Crepis alpina
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 ...
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Mol. Biol. Rep.
41
5077-5087
2014
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2
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728074
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725452
Zhou
Caenorhabditis elegans ?12-des ...
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J. Biol. Chem.
286
43644-43650
2011
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715539
Blacklock
Functional diversity in fungal ...
Cantharellus formosus
J. Biol. Chem.
285
28442-28449
2010
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1
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8
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3
3
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675151
Nam
Cloning and transcriptional an ...
Crepis alpina, Helianthus annuus
J. Exp. Bot.
58
1421-1432
2007
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6
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679861
Zhang
Identification of a novel bifu ...
Coprinopsis cinerea, Coprinopsis cinerea TD#822-2
FEBS Lett.
581
315-319
2007
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684454
Harwood
Temperature stress: reacting a ...
Acanthamoeba castellanii
Ann. N. Y. Acad. Sci.
1113
52-57
2007
1
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1
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1
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4
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658641
Carlsson
Properties of two multifunctio ...
Crepis alpina
Eur. J. Biochem.
271
2991-2997
2004
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1
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7
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657528
Minto
Synthesis and conformational s ...
Crepis alpina
Anal. Biochem.
308
134-140
2002
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1
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285468
Lee
Identification of non-heme dii ...
Crepis alpina
Science
280
915-918
1998
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