BRENDA - Enzyme Database show
show all sequences of 1.14.19.39

Temperature stress: reacting and adapting: lessons from poikilotherms

Harwood, J.L.; Ann. N. Y. Acad. Sci. 1113, 52-57 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
the enzyme is independently induced by oxygen, and temperature, while chilling alone is not sufficient to raise the enzyme activity. Chilling and lowered temperature cause an increase in desaturase activity, increased membrane unsaturation and subsequently fluidity, followed by phagocytosis, overview
Acanthamoeba castellanii
Cloned(Commentary)
Commentary
Organism
expression in Saccharomyces cerevisiae
Acanthamoeba castellanii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Acanthamoeba castellanii
key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acanthamoeba castellanii
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
cell growth between 4°C and 32°C
Acanthamoeba castellanii
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
684454
Acanthamoeba castellanii
?
-
-
-
-
additional information
substrate specificity, the recombinant enzyme catalyzes also the DELTA15-desaturation of fatty acids, and is capable of producing very unusual n-1 polyunsaturated products, overview
684454
Acanthamoeba castellanii
?
-
-
-
-
oleate + AH2 + O2
oxygenation at the sn-2 position
684454
Acanthamoeba castellanii
linoleate + A + H2O
-
-
-
?
palmitoleoate + AH2 + O2
via intermediate DELTA9,12 hexadecadienoate
684454
Acanthamoeba castellanii
9,12,15-hexadecatrienoate + A + H2O
the product is n-1 polyunsaturated
-
-
?
phosphatidylcholine + AH2 + O2
-
684454
Acanthamoeba castellanii
?
-
-
-
?
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
the enzyme is independently induced by oxygen, and temperature, while chilling alone is not sufficient to raise the enzyme activity. Chilling and lowered temperature cause an increase in desaturase activity, increased membrane unsaturation and subsequently fluidity, followed by phagocytosis, overview
Acanthamoeba castellanii
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Saccharomyces cerevisiae
Acanthamoeba castellanii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Acanthamoeba castellanii
key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
cell growth between 4°C and 32°C
Acanthamoeba castellanii
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
key enzyme in adaptation to low temperature, sequential changes in fatty acid composition on lowering environmental temperature, overview
684454
Acanthamoeba castellanii
?
-
-
-
-
additional information
substrate specificity, the recombinant enzyme catalyzes also the DELTA15-desaturation of fatty acids, and is capable of producing very unusual n-1 polyunsaturated products, overview
684454
Acanthamoeba castellanii
?
-
-
-
-
oleate + AH2 + O2
oxygenation at the sn-2 position
684454
Acanthamoeba castellanii
linoleate + A + H2O
-
-
-
?
palmitoleoate + AH2 + O2
via intermediate DELTA9,12 hexadecadienoate
684454
Acanthamoeba castellanii
9,12,15-hexadecatrienoate + A + H2O
the product is n-1 polyunsaturated
-
-
?
phosphatidylcholine + AH2 + O2
-
684454
Acanthamoeba castellanii
?
-
-
-
?
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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41
5077-5087
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725452
Zhou
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286
43644-43650
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715539
Blacklock
Functional diversity in fungal ...
Cantharellus formosus
J. Biol. Chem.
285
28442-28449
2010
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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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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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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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