Information on EC 5.2.1.5 - Linoleate isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.2.1.5
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RECOMMENDED NAME
GeneOntology No.
Linoleate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
9-cis,12-cis-octadecadienoate = 9-cis,11-trans-octadecadienoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cis-trans-isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Linoleic acid metabolism
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SYSTEMATIC NAME
IUBMB Comments
Linoleate DELTA12-cis-DELTA11-trans-isomerase
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-41-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LA-I activity in the whole ruminal fluid of cows is measured
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Manually annotated by BRENDA team
strain A38, a ruminal bacterium
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Manually annotated by BRENDA team
strain A38, a ruminal bacterium
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Manually annotated by BRENDA team
strain ATCC 25762
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Manually annotated by BRENDA team
strain L1
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strains B24 and JK205, a ruminal bacterium
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Manually annotated by BRENDA team
strain JW11, a ruminal bacterium
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Manually annotated by BRENDA team
strain JW11, a ruminal bacterium
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(9Z,12Z)-octadeca-9,12-dienoic acid
(9Z,11E)-octadeca-9,11-dienoic acid
show the reaction diagram
11-cis,14-cis-eicosadienoic acid
?
show the reaction diagram
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-
-
-
?
2,5-Octadecadienoic acid
3,5-Octadecadienoic acid
show the reaction diagram
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-
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6-cis,9-cis,12-cis,15-cis-octadecatetraenoic acid
?
show the reaction diagram
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i.e. stearidonic acid
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-
?
6-cis,9-cis,12-cis-octadecatrienoic acid
?
show the reaction diagram
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i.e. alpha-linolenic acid
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?
9-cis,11-trans-linoleic acid
9-trans,11-trans-linoleic acid
show the reaction diagram
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formation only under aerobic conditions
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?
9-cis,12-cis,15-cis-octadecatrienoic acid
?
show the reaction diagram
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i.e. gamma-linolenic acid
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?
9-cis,12-cis-linoleic acid
9-cis,11-trans-linoleic acid
show the reaction diagram
9-cis,12-cis-linoleic acid
9-cis,11-trans-linoleic acid + 9-trans,11-trans-linoleic acid
show the reaction diagram
9-cis,12-cis-linoleic acid
9-trans,11-trans-linoleic acid
show the reaction diagram
9-cis,12-cis-Octadecadienoate
9-cis,11-trans-Octadecadienoate
show the reaction diagram
9-cis,12-cis-Octadecadienoate
?
show the reaction diagram
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initial reaction of the biohydrogenation pathway
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cis-9,cis-12,cis-15-octadecatrienoic acid
cis-9,trans-11,cis-15-octadecatrienoic acid
show the reaction diagram
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linoleic acid
(9E,11E)-octadeca-9,11-dienoic acid
show the reaction diagram
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?
linoleic acid
(9Z,11E)-octadeca-9,11-dienoic acid
show the reaction diagram
linoleic acid
conjugated linoleic acid
show the reaction diagram
additional information
?
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substrate specificity, overview, the enzyme is specific for substrates containing cis double bonds at the c9 and c12 positions of C18 polyunsaturated fatty acids, a free carboxyl group is absolutely necessary for isomerization
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
9-cis,11-trans-linoleic acid
9-trans,11-trans-linoleic acid
show the reaction diagram
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formation only under aerobic conditions
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?
9-cis,12-cis-linoleic acid
9-cis,11-trans-linoleic acid
show the reaction diagram
9-cis,12-cis-linoleic acid
9-trans,11-trans-linoleic acid
show the reaction diagram
9-cis,12-cis-Octadecadienoate
9-cis,11-trans-Octadecadienoate
show the reaction diagram
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-
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?
9-cis,12-cis-Octadecadienoate
?
show the reaction diagram
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initial reaction of the biohydrogenation pathway
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no external cofactors are required for catalysis
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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metal ions such as Co2+, Ni2+, Fe3+, Cd3+, and Mn2+ restore conjugated linoleic acid productivity after inhibition with o-phenanthroline up to 56% of the original activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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reversible, noncompetitive
10,13-Octadecadienoic acid
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inhibits isomerization of 9,12-octadienoic acid
11,14-Octadecadienoic acid
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inhibits isomerization of 9,12-octadienoic acid
12,15-Octadecadienoic acid
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inhibits isomerization of 9,12-octadienoic acid
4,7-Octadecadienoic acid
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inhibits isomerization of 2,5-octadecadienoic acid and 9,12-octadecadienic acid
5,8-Octadecadienoic acid
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inhibits isomerization of 2,5-octadecadienoic acid and 9,12-octadecadienic acid
7,10-Octadecadienoic acid
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inhibits isomerization of 9,12-octadienoic acid
8,11-Octadecadienoic acid
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inhibits isomerization of 9,12-octadienoic acid
9-cis,12-cis-linoleic acid methyl ester
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i.e. methyl linoleate, 31% inhibition at 0.02 mM
9-cis,12-cis-octadecadien-1-ol
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i.e. linoleyl alcohol, 19% inhibition at 0.02 mM
cis,cis,3,6-Octadecadienoic acid
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inhibits isomerization of 2,5-octadecadienoic acid and 9,12-octadecadienic acid
cis-11,cis-14-Eicosadienic acid
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
cis-6,cis-9-Octadecadienic acid
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
cis-8,cis11-Heptadecadienic acid
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cis-9,trans-12-Octadecadienoic acid
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
cis-9-Octadecen-12-ynoic acid
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
EGTA
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93% residual activity at 3 mM
gamma-linolenic acid
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substrate inhibition at concentrations above 0.015 mM
iodoacetamide
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Linoleamide
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
linoleic acid
linolelaidic acid
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81% inhibition at 0.02 mM
linolenic acid
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substrate inhibition at concentrations above 0.04 mM
Linoleyl alcohol
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
linoleyl amine
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
Linoleyl hydrazide
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Linoleyl hydroxamate
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
Linoleyl methyl ether
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
Linoleyl methyl ketone
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weak inhibition
Linoleyl oxime
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
methyl linoleate
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weak inhibition
methyl oleate
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
o-phenanthroline
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10% residual activity at 3 mM
oleic acid
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75% inhibition at 0.02 mM
oleyl alcohol
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
oleyl amine
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
p-hydroxymercuribenzoate
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palmitoleic acid
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72% inhibition at 0.02 mM
stearidonic acid
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substrate inhibition at concentrations above 0.120 mM
trans-11-Octadecen-9-ynoic acid
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
trans-3,cis-5-Octadecadienoic acid
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inhibits isomerization of 2,5-octadecadienoic acid
trans-9,cis-12-Octadecadienoic acid
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
trans-9,trans-12-Octadecadienoic acid
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inhibits isomerization of 9-cis,12-cis-octadecadienoate
additional information
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no effects by DTT, ATP, ADP, NAD+, NADH, NADPH or CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
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125% activity at 3 mM
8-hydroxyquinoline
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118% activity at 3 mM
alpha-alpha'-bipyridyl
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125% activity at 3 mM
FAD
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the addition of 5 mM NADH plus FAD to the reaction mixture with dialyzed high molecular fraction of the soluble fraction restores activity to 101%
K2MoO4
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422% activity at 5 mM, in the presence of o-phenanthroline
K2WO4
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149% activity at 5 mM, in the presence of o-phenanthroline
Na2MnO4
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427% activity at 5 mM, in the presence of o-phenanthroline
Na2WO4
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157% activity at 5 mM, in the presence of o-phenanthroline
Na3VO4
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264% activity at 5 mM, in the presence of o-phenanthroline
NADH
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the addition of 5 mM NADH plus FAD to the reaction mixture with dialyzed high molecular fraction of the soluble fraction restores activity to 101%
NADPH
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the addition of 5 mM NADPH to the reaction mixture with dialyzed high molecular fraction of the soluble fraction restores activity to 98%
NaVO3
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209% activity at 5 mM, in the presence of o-phenanthroline
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additional information
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no effects by DTT, ATP, ADP, NAD+, NADH, NADPH or CoA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034
6-cis,9-cis,12-cis,15-cis-octadecatetraenoic acid
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pH 7.5, 22C
0.0258
6-cis,9-cis,12-cis-octadecatrienoic acid
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pH 7.5, 22C
0.0077
9-cis,12-cis,15-cis-octadecatrienoic acid
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pH 7.5, 22C
0.0119 - 0.0619
9-cis,12-cis-linoleic acid
0.012
9-cis,12-cis-octadecadienoate
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0.023
cis-9,-cis-12,cis-15-octadecatrienoic acid
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additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00016
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strain JK205
0.00047
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strain A38
0.00059
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strain JW11
0.00076
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strain B24
0.4
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purified enzyme
3.8
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crude extract, at pH 6.5, 30C
353.5
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after 93.3fold purification, at pH 6.5, 30C
additional information
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higher enzyme activity and more tolerant to linoleic acid than other strains examined
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
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calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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4 * 45000, SDS-PAGE
67910
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x * 67910, calculated from amino acid sequence
190000
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native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 45000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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the residual activity of the free and immobilized linoleic acid isomerase is 100% at pH 6.5 and 7.0, respectively. The immobilized linoleic acid isomerase remains more than 60% of its initial activity in the pH range of 5.5-8.0 and more than 80% of its initial activity in the pH range of 6.0-8.0, while the free linoleic acid isomerase remains more than 60% of its initial activity in the pH range of 5.5-7.0 and more than 80% of its initial activity in the pH range of 6.0-7.0
714488
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
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the immobilized enzyme is more stable than the free enzyme at 30-60C, more than 85% of its initial activity is retained after incubation for 3 h. The residual activity of the free and immobilized LA isomerase is 100% at 20C. The free and immobilized enzymes are highly stable below 30C. However, the activity of the free enzyme rapidly decreases with the increased temperature, and the immobilized enzyme retains its activity above 30C. The immobilized enzyme has 81% activity at 50C, whereas the free enzyme loses 51% of its activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is very unstable, especially after being solubilized by detergents, increasing glycerol concentration to 30% and salt concentration to 0.5 M improves isomerase stability, resulting in a near full retention of activity in crude extracts for 1 week
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the immobilized enzyme has high operational stability and retains high enzymatic activity after seven cycles of reuse at 37C. After incubation for 3 h, the immobilized linoleic acid isomerase retains 85% of its initial activity, and then its activity is slowly decreased to 45% within 24 h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is very unstable, especially after being solubilized by detergents, increasing glycerol concentration to 30% and salt concentration to 0.5 M improves isomerase stability, resulting in a near full retention of activity in crude extracts for 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography and Sephadex G-100 gel filtration
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native enzyme 364fold by anion exchange chromatography, chromatofocusing, and gel filtration, method optimization for purification of the very unstable enzyme, overview
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partially, optimization of the cell lysis and enzyme solubilization methods, overview
ultracentrifugation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
synthesis