BRENDA - Enzyme Database show
show all sequences of 1.14.19.39

Properties of two multifunctional plant fatty acid acetylenase/desaturase enzymes

Carlsson, A.S.; Thomaeus, S.; Hamberg, M.; Stymne, S.; Eur. J. Biochem. 271, 2991-2997 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene CREP1, expression in Arabidopsis thaliana and in Saccharomyces cerevisiae, determination and identification of fatty acid content of transgenic plant lines and yeast strains
Crepis alpina
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Crepis alpina
-
gene and enzyme CREP1
-
Reaction
Reaction
Commentary
Organism
linoleoyl-[glycerolipid] + 2 ferrocytochrome b5 + O2 + 2 H+ = crepenynyl-[glycerolipid] + 2 ferricytochrome b5 + 2 H2O
stereochemical mechanism in reaction with oleate
Crepis alpina
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + reduced acceptor + O2
enzyme is equally efficient with linoleate and oleate
658641
Crepis alpina
crepenynate + acceptor + H2O
-
-
-
?
oleate + reduced acceptor + O2
enzyme is equally efficient with linoleate and oleate, via intermediates 9(Z),12(E)-octadecadienoate and 9,12(Z)-octadecadienoate, only the latter of which is further catalysed to give crepenynate, i.e. 9(Z)-octadecen-12-ynoate
658641
Crepis alpina
crepenynate + acceptor + H2O
product enantiomers in a ration of 3:1
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
gene CREP1, expression in Arabidopsis thaliana and in Saccharomyces cerevisiae, determination and identification of fatty acid content of transgenic plant lines and yeast strains
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
enzyme is equally efficient with linoleate and oleate
658641
Crepis alpina
crepenynate + acceptor + H2O
-
-
-
?
oleate + reduced acceptor + O2
enzyme is equally efficient with linoleate and oleate, via intermediates 9(Z),12(E)-octadecadienoate and 9,12(Z)-octadecadienoate, only the latter of which is further catalysed to give crepenynate, i.e. 9(Z)-octadecen-12-ynoate
658641
Crepis alpina
crepenynate + acceptor + H2O
product enantiomers in a ration of 3:1
-
-
?
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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728074
Chodok
Identification and functional ...
Physcomitrella patens
J. Ind. Microbiol. Biotechnol.
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901-913
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725452
Zhou
Caenorhabditis elegans ?12-des ...
Caenorhabditis elegans
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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675151
Nam
Cloning and transcriptional an ...
Crepis alpina, Helianthus annuus
J. Exp. Bot.
58
1421-1432
2007
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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
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658641
Carlsson
Properties of two multifunctio ...
Crepis alpina
Eur. J. Biochem.
271
2991-2997
2004
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657528
Minto
Synthesis and conformational s ...
Crepis alpina
Anal. Biochem.
308
134-140
2002
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285468
Lee
Identification of non-heme dii ...
Crepis alpina
Science
280
915-918
1998
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