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show all sequences of 1.13.11.60

Characterization of a recombinant 7,8-linoleate diol synthase from Glomerella cingulate

Seo, M.J.; Shin, K.C.; An, J.U.; Kang, W.R.; Ko, Y.J.; Oh, D.K.; Appl. Microbiol. Biotechnol. 100, 3087-3099 (2016)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
DMSO
the whole enzyme activity is the highest using DMSO among the organic solvents tested, and its optimal concentration is 2.5% v/v
Colletotrichum gloeosporioides
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli; phylogenetic tree, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain ER2566
Colletotrichum gloeosporioides
Engineering
Amino acid exchange
Commentary
Organism
A891G
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
Colletotrichum gloeosporioides
C1038S
site-directed mutagenesis, the mutant produces a low amount of 7,8-DiHODE with the accumulation of 8-HPODE
Colletotrichum gloeosporioides
H1036A
site-directed mutagenesis, the mutant produces a low amount of 7,8-DiHODE with the accumulation of 8-HPODE
Colletotrichum gloeosporioides
H1036A/C1038S
site-directed mutagenesis, the double mutant converts linoleic acid to only 8-HPODE
Colletotrichum gloeosporioides
additional information
comparison of substrate specificities of wild-type an d mutant enzymes, overview
Colletotrichum gloeosporioides
N895D
site-directed mutagenesis, the mutant produces a reduced amount of 8-HPODE, compared to wild-type, without the accumulation of DiHODE
Colletotrichum gloeosporioides
N895L
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
Colletotrichum gloeosporioides
N895Q
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
Colletotrichum gloeosporioides
Q898E
site-directed mutagenesis, the mutant converts linoleic acid to 8,11-DiHODE as major product and 7,8-DiHODE as minor product
Colletotrichum gloeosporioides
Q898L
site-directed mutagenesis, the mutant converts linoleic acid to 8,11-DiHODE as major product and 7,8-DiHODE as minor product
Colletotrichum gloeosporioides
Y380F
site-directed mutagenesis, the mutant enzyme produces trace amount of 7,8-DiHODE without the accumulation of 8-HPODE when incubated with linoleic acid as substrate
Colletotrichum gloeosporioides
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0193
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0193
-
linoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.022
-
linoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0264
-
alpha-linolenate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0293
-
oleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0305
-
palmitoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0319
-
eicosadienoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0319
-
eicosadienoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0324
-
eicosenoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0324
-
eicosenoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0333
-
oleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0358
-
arachidonate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0358
-
arachidonic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0368
-
dihomo-gamma-linolenic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0369
-
dihomo-gamma-linolenate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0371
-
alpha-linolenate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.048
-
palmitoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
510000
-
gel filtration; recombinant enzyme, gel filtration
Colletotrichum gloeosporioides
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + O2
Colletotrichum gloeosporioides
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
?
Organic Solvent Stability
Organic Solvent
Commentary
Organism
DMSO
maximum activity in presence of 2.5% DMSO
Colletotrichum gloeosporioides
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Colletotrichum gloeosporioides
A0A0S2SWE4
bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6; i.e. Colletotrichum gloeosporioides
-
Colletotrichum gloeosporioides KACC 40961
A0A0S2SWE4
i.e. Colletotrichum gloeosporioides
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes 8fold from Escherichia coli strain ER2566 by nickel affinity chromatography
Colletotrichum gloeosporioides
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Colletotrichum gloeosporioides
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.39
-
purified recombinant enzyme, whole enzyme activity, substrate palmitoleate, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.48
-
purified recombinant enzyme, whole enzyme activity, substrate oleate, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.75
-
purified recombinant enzyme, whole enzyme activity, substrate alpha-linolenate, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.87
-
pH 6.5, 40°C; purified recombinant enzyme, whole enzyme activity, substrate (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.17
-
purified recombinant enzyme, N-terminal domain activity, substrate arachidate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.18
-
purified recombinant enzyme, N-terminal domain activity, substrate dihomo-gamma-linolenate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.2
-
purified recombinant enzyme, N-terminal domain activity, substrate eicosadienoate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.39
-
purified recombinant enzyme, N-terminal domain activity, substrate eicosenoate, pH 6.5, 40°C
Colletotrichum gloeosporioides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-linolenate + O2
-
741712
Colletotrichum gloeosporioides
(8R,9Z,12Z)-8-hydroperoxy-9,12,15-octadecatrienoate
-
-
-
?
alpha-linolenate + O2
via (9Z,12Z,15Z)-8-hydroperoxyoctadeca-9,12,15-trienoic acid, best substrate with respect to whole enzyme activity
741712
Colletotrichum gloeosporioides
(9Z,12Z,15Z)-7,8-dihydroxyoctadeca-9,12,15-trienoic acid
-
-
-
?
arachidonate + O2
-
741712
Colletotrichum gloeosporioides
(5Z,8Z,11Z,14Z)-8-hydroxyeicosa-5,8,11,14-tetraenoic acid
-
-
-
?
arachidonic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxyarachidonic acid
-
-
-
?
dihomo-gamma-linolenate + O2
-
741712
Colletotrichum gloeosporioides
(8Z,11Z,12Z)-8-hydroxyeicosa-8,11,12-trienoic acid
-
-
-
?
dihomo-gamma-linolenic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxydihomo-gamma-linolenic acid
-
-
-
?
eicosadienoate + O2
-
741712
Colletotrichum gloeosporioides
(11Z,14Z)-8-hydroxyeicosa-11,14-dienoic acid
-
-
-
?
eicosadienoic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxyeicosadienoic acid
-
-
-
?
eicosenoate + O2
-
741712
Colletotrichum gloeosporioides
(11Z)-8-hydroxyeicosa-11-enoic acid
-
-
-
?
eicosenoic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxyeicosenoic acid
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides KACC 40961
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(7S,8S)-7,8-dihydroxy-(9Z,12Z)-octadecadienoic acid
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoic acid
-
-
-
?
additional information
bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6
741712
Colletotrichum gloeosporioides
?
-
-
-
-
additional information
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (9Z,12Z)-7S,8S-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5R,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
741712
Colletotrichum gloeosporioides
?
-
-
-
-
additional information
bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6
741712
Colletotrichum gloeosporioides KACC 40961
?
-
-
-
-
additional information
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (9Z,12Z)-7S,8S-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5R,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
741712
Colletotrichum gloeosporioides KACC 40961
?
-
-
-
-
oleate + O2
-
741712
Colletotrichum gloeosporioides
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
oleate + O2
-
741712
Colletotrichum gloeosporioides KACC 40961
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
oleate + O2
via (9Z)-8-hydroperoxyoctadeca-9-enoic acid
741712
Colletotrichum gloeosporioides
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
-
-
-
?
palmitoleate + O2
-
741712
Colletotrichum gloeosporioides
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
palmitoleate + O2
-
741712
Colletotrichum gloeosporioides KACC 40961
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
palmitoleate + O2
via (9Z)-dihydroperoxyhexadeca-9-enoate
741712
Colletotrichum gloeosporioides
(9Z)-5,8-dihydroxyhexadeca-9-enoic acid
-
-
-
?
Subunits
Subunits
Commentary
Organism
homotetramer
4 * 127000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 127413, sequence calculation
Colletotrichum gloeosporioides
More
the enzyme diol synthase is a fusion protein, consisting of an N-terminal dioxygenase domain and a C-terminal cytochrome P450/hydroperoxide isomerase domain
Colletotrichum gloeosporioides
trimer
3 * 127000, SDS-PAGE, 3 * 127413, calculated
Colletotrichum gloeosporioides
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
maximum of 8-diogenase reaction; N-terminal domain activity
Colletotrichum gloeosporioides
40
-
maximum of whole enzyme; whole enzyme activity
Colletotrichum gloeosporioides
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
50
purified recombinant enzyme, 2 h, the activities of whole 7,8-LDS and 8-dioxygenase in the N-terminal domain decrease as temperature increases. The N-terminal domain demonstrates a greater thermal stability than the C-terminal domain. The whole enzyme activity presentes 72% of the initial activity at 40°C after 2 h, while 8-dioxygenase activity in the N-terminal domain is 90%
Colletotrichum gloeosporioides
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.86
-
palmitoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
5.62
-
oleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
6.58
-
linoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
10.5
-
alpha-linolenate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.2
-
dihomo-gamma-linolenate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.2
-
dihomo-gamma-linolenic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.7
-
eicosadienoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.7
-
eicosadienoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
18.2
-
arachidonate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
18.2
-
arachidonic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
21.2
-
palmitoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
22
-
eicosenoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
22
-
eicosenoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
24.7
-
oleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
25.1
-
alpha-linolenate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
25.2
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
35
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
35
-
linoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the maximum activity for the conversion of linoleic acid to (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) by 8-dioxygenase in the N-terminal domain of 7,8-LDS is observed at pH 7.0 and 20°C, whereas that for the conversion of linoleic acid to (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by the whole enzyme is observed at pH 6.5 and 40°C
Colletotrichum gloeosporioides
6.5
-
maximum of bifunctional enzyme; whole enzyme activity
Colletotrichum gloeosporioides
7
-
maximum of 8-diogenase reaction; N-terminal domain activity
Colletotrichum gloeosporioides
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
DMSO
the whole enzyme activity is the highest using DMSO among the organic solvents tested, and its optimal concentration is 2.5% v/v
Colletotrichum gloeosporioides
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli; phylogenetic tree, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain ER2566
Colletotrichum gloeosporioides
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A891G
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
Colletotrichum gloeosporioides
C1038S
site-directed mutagenesis, the mutant produces a low amount of 7,8-DiHODE with the accumulation of 8-HPODE
Colletotrichum gloeosporioides
H1036A
site-directed mutagenesis, the mutant produces a low amount of 7,8-DiHODE with the accumulation of 8-HPODE
Colletotrichum gloeosporioides
H1036A/C1038S
site-directed mutagenesis, the double mutant converts linoleic acid to only 8-HPODE
Colletotrichum gloeosporioides
additional information
comparison of substrate specificities of wild-type an d mutant enzymes, overview
Colletotrichum gloeosporioides
N895D
site-directed mutagenesis, the mutant produces a reduced amount of 8-HPODE, compared to wild-type, without the accumulation of DiHODE
Colletotrichum gloeosporioides
N895L
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
Colletotrichum gloeosporioides
N895Q
site-directed mutagenesis, the mutant converts linoleic acid to 7,8-DiHODE as major product and 8,11-DiHODE as minor product, which is the similar pattern as the wild-type enzyme
Colletotrichum gloeosporioides
Q898E
site-directed mutagenesis, the mutant converts linoleic acid to 8,11-DiHODE as major product and 7,8-DiHODE as minor product
Colletotrichum gloeosporioides
Q898L
site-directed mutagenesis, the mutant converts linoleic acid to 8,11-DiHODE as major product and 7,8-DiHODE as minor product
Colletotrichum gloeosporioides
Y380F
site-directed mutagenesis, the mutant enzyme produces trace amount of 7,8-DiHODE without the accumulation of 8-HPODE when incubated with linoleic acid as substrate
Colletotrichum gloeosporioides
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0193
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0193
-
linoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.022
-
linoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0264
-
alpha-linolenate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0293
-
oleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0305
-
palmitoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0319
-
eicosadienoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0319
-
eicosadienoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0324
-
eicosenoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0324
-
eicosenoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0333
-
oleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0358
-
arachidonate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0358
-
arachidonic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0368
-
dihomo-gamma-linolenic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0369
-
dihomo-gamma-linolenate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.0371
-
alpha-linolenate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.048
-
palmitoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
510000
-
gel filtration; recombinant enzyme, gel filtration
Colletotrichum gloeosporioides
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + O2
Colletotrichum gloeosporioides
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
?
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
DMSO
maximum activity in presence of 2.5% DMSO
Colletotrichum gloeosporioides
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged wild-type and mutant enzymes 8fold from Escherichia coli strain ER2566 by nickel affinity chromatography
Colletotrichum gloeosporioides
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Colletotrichum gloeosporioides
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.39
-
purified recombinant enzyme, whole enzyme activity, substrate palmitoleate, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.48
-
purified recombinant enzyme, whole enzyme activity, substrate oleate, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.75
-
purified recombinant enzyme, whole enzyme activity, substrate alpha-linolenate, pH 6.5, 40°C
Colletotrichum gloeosporioides
0.87
-
pH 6.5, 40°C; purified recombinant enzyme, whole enzyme activity, substrate (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.17
-
purified recombinant enzyme, N-terminal domain activity, substrate arachidate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.18
-
purified recombinant enzyme, N-terminal domain activity, substrate dihomo-gamma-linolenate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.2
-
purified recombinant enzyme, N-terminal domain activity, substrate eicosadienoate, pH 6.5, 40°C
Colletotrichum gloeosporioides
1.39
-
purified recombinant enzyme, N-terminal domain activity, substrate eicosenoate, pH 6.5, 40°C
Colletotrichum gloeosporioides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-linolenate + O2
-
741712
Colletotrichum gloeosporioides
(8R,9Z,12Z)-8-hydroperoxy-9,12,15-octadecatrienoate
-
-
-
?
alpha-linolenate + O2
via (9Z,12Z,15Z)-8-hydroperoxyoctadeca-9,12,15-trienoic acid, best substrate with respect to whole enzyme activity
741712
Colletotrichum gloeosporioides
(9Z,12Z,15Z)-7,8-dihydroxyoctadeca-9,12,15-trienoic acid
-
-
-
?
arachidonate + O2
-
741712
Colletotrichum gloeosporioides
(5Z,8Z,11Z,14Z)-8-hydroxyeicosa-5,8,11,14-tetraenoic acid
-
-
-
?
arachidonic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxyarachidonic acid
-
-
-
?
dihomo-gamma-linolenate + O2
-
741712
Colletotrichum gloeosporioides
(8Z,11Z,12Z)-8-hydroxyeicosa-8,11,12-trienoic acid
-
-
-
?
dihomo-gamma-linolenic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxydihomo-gamma-linolenic acid
-
-
-
?
eicosadienoate + O2
-
741712
Colletotrichum gloeosporioides
(11Z,14Z)-8-hydroxyeicosa-11,14-dienoic acid
-
-
-
?
eicosadienoic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxyeicosadienoic acid
-
-
-
?
eicosenoate + O2
-
741712
Colletotrichum gloeosporioides
(11Z)-8-hydroxyeicosa-11-enoic acid
-
-
-
?
eicosenoic acid + O2
-
741712
Colletotrichum gloeosporioides
8-hydroxyeicosenoic acid
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides KACC 40961
(8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(7S,8S)-7,8-dihydroxy-(9Z,12Z)-octadecadienoic acid
-
-
-
?
linoleate + O2
-
741712
Colletotrichum gloeosporioides
(R)-8-hydroperoxy-(9Z,12Z)-octadecadienoic acid
-
-
-
?
additional information
bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6
741712
Colletotrichum gloeosporioides
?
-
-
-
-
additional information
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (9Z,12Z)-7S,8S-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5R,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
741712
Colletotrichum gloeosporioides
?
-
-
-
-
additional information
bifunctional enzyme, the second domain isomerizes the product (8R,9Z,12Z)-8-hydroperoxy-9,12-octadecadienoate to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate, cf. EC 5.4.4.6
741712
Colletotrichum gloeosporioides KACC 40961
?
-
-
-
-
additional information
the bifunctional enzyme converts linoleic acid to a product, identified as (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) and nuclear magnetic resonance (NMR) spectroscopy. The specific activity and catalytic efficiency (kcat/Km) of 7,8-diol synthase for the conversion of fatty acid to dihydroxy fatty acid follows the descending order linoleic acid, alpha-linolenic acid, oleic acid, and palmitoleic acid, indicating that the enzyme is a 7,8-linoleate diol synthase (7,8-LDS). Substrate specificity, overview. The reaction via (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) as an intermediate and the accumulation of 8-HPODE is due to a higher 8-dioxygenase activity in the N-terminal domain than hydroperoxide isomerase activity in the C-terminal domain, EC 5.4.4.6. 8-HPODE is subsequently isomerized to (9Z,12Z)-7S,8S-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) or (5R,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoic acid (5,8-DiHODE) by the C-terminal hydroperoxide isomerase domain of diol synthase. No activity with conjugated linoleic acid, docosapentaenoic acid, and docosahexaenoic acid, and no isomerase activity and no whole enzyme acitivity, but dioxygenase activity with eicosenoic acid, eicosadienoic acid, dihomo-gamma-linolenic acid, and arachidonic acid
741712
Colletotrichum gloeosporioides KACC 40961
?
-
-
-
-
oleate + O2
-
741712
Colletotrichum gloeosporioides
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
oleate + O2
-
741712
Colletotrichum gloeosporioides KACC 40961
(9Z)-8-hydroperoxyoctadec-9-enoate
-
-
-
?
oleate + O2
via (9Z)-8-hydroperoxyoctadeca-9-enoic acid
741712
Colletotrichum gloeosporioides
(9Z)-7,8-dihydroxyoctadeca-9-enoic acid
-
-
-
?
palmitoleate + O2
-
741712
Colletotrichum gloeosporioides
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
palmitoleate + O2
-
741712
Colletotrichum gloeosporioides KACC 40961
(9Z)-8-hydroperoxyhexadec-9-enoate
-
-
-
?
palmitoleate + O2
via (9Z)-dihydroperoxyhexadeca-9-enoate
741712
Colletotrichum gloeosporioides
(9Z)-5,8-dihydroxyhexadeca-9-enoic acid
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homotetramer
4 * 127000, recombinant His-tagged enzyme, SDS-PAGE, 4 * 127413, sequence calculation
Colletotrichum gloeosporioides
More
the enzyme diol synthase is a fusion protein, consisting of an N-terminal dioxygenase domain and a C-terminal cytochrome P450/hydroperoxide isomerase domain
Colletotrichum gloeosporioides
trimer
3 * 127000, SDS-PAGE, 3 * 127413, calculated
Colletotrichum gloeosporioides
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
maximum of 8-diogenase reaction; N-terminal domain activity
Colletotrichum gloeosporioides
40
-
maximum of whole enzyme; whole enzyme activity
Colletotrichum gloeosporioides
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
20
50
purified recombinant enzyme, 2 h, the activities of whole 7,8-LDS and 8-dioxygenase in the N-terminal domain decrease as temperature increases. The N-terminal domain demonstrates a greater thermal stability than the C-terminal domain. The whole enzyme activity presentes 72% of the initial activity at 40°C after 2 h, while 8-dioxygenase activity in the N-terminal domain is 90%
Colletotrichum gloeosporioides
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.86
-
palmitoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
5.62
-
oleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
6.58
-
linoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
10.5
-
alpha-linolenate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.2
-
dihomo-gamma-linolenate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.2
-
dihomo-gamma-linolenic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.7
-
eicosadienoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
17.7
-
eicosadienoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
18.2
-
arachidonate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
18.2
-
arachidonic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
21.2
-
palmitoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
22
-
eicosenoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
22
-
eicosenoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
24.7
-
oleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C; recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
25.1
-
alpha-linolenate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
25.2
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
35
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
35
-
linoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
the maximum activity for the conversion of linoleic acid to (9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoic acid (8-HPODE) by 8-dioxygenase in the N-terminal domain of 7,8-LDS is observed at pH 7.0 and 20°C, whereas that for the conversion of linoleic acid to (9Z,12Z)-7,8-dihydroxyoctadeca-9,12-dienoic acid (7,8-DiHODE) by the whole enzyme is observed at pH 6.5 and 40°C
Colletotrichum gloeosporioides
6.5
-
maximum of bifunctional enzyme; whole enzyme activity
Colletotrichum gloeosporioides
7
-
maximum of 8-diogenase reaction; N-terminal domain activity
Colletotrichum gloeosporioides
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
100
-
palmitoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
170
-
oleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
340
-
alpha-linolenate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
370
-
linoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
466.1
-
dihomo-gamma-linolenate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
470
-
dihomo-gamma-linolenic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
508.4
-
arachidonate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
510
-
arachidonic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
554.9
-
eicosadienoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
560
-
eicosadienoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
679
-
eicosenoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
680
-
eicosenoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
690
-
palmitoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
695.1
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
840
-
oleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
843
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
950
-
alpha-linolenate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
954.54
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
1813.5
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
1820
-
linoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
100
-
palmitoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
170
-
oleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
340
-
alpha-linolenate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
370
-
linoleate
bifunctional enzyme, pH 6.5, 40°C
Colletotrichum gloeosporioides
466.1
-
dihomo-gamma-linolenate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
470
-
dihomo-gamma-linolenic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
508.4
-
arachidonate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
510
-
arachidonic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
554.9
-
eicosadienoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
560
-
eicosadienoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
679
-
eicosenoate
recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
680
-
eicosenoic acid
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
690
-
palmitoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
695.1
-
palmitoleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
840
-
oleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
843
-
oleate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
950
-
alpha-linolenate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
954.54
-
alpha-linolenate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
1813.5
-
(8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
recombinant enzyme, whole enzyme activity, pH 6.5, 40°C
Colletotrichum gloeosporioides
1820
-
linoleate
N-terminal 8-dioxygenase domain, pH 6.5, 40°C
Colletotrichum gloeosporioides
Other publictions for EC 1.13.11.60
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)
741712
Seo
Characterization of a recombi ...
Colletotrichum gloeosporioides, Colletotrichum gloeosporioides KACC 40961
Appl. Microbiol. Biotechnol.
100
3087-3099
2016
1
-
1
-
11
-
-
17
-
-
1
1
1
5
-
-
1
-
-
1
8
-
25
3
2
-
1
18
3
-
-
-
-
-
-
1
-
1
-
-
11
-
-
-
-
17
-
-
1
1
1
-
-
1
-
1
8
-
25
3
2
-
1
18
3
-
-
-
-
-
-
-
20
20
742730
Seo
Production of 7,8-dihydroxy u ...
Colletotrichum gloeosporioides, Colletotrichum gloeosporioides KACC 40961
J. Agric. Food Chem.
64
8555-8562
2016
1
1
1
-
1
-
-
-
-
-
-
2
-
6
-
-
1
-
-
1
-
-
14
-
1
-
-
-
1
-
-
-
-
-
-
1
1
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
1
-
1
-
-
14
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
743200
Sooman
Discovery of a novel linoleat ...
Colletotrichum graminicola, Colletotrichum graminicola M1.001, Colletotrichum graminicola M1.001 / M2 / FGSC 10212, Fusarium oxysporum, Fusarium oxysporum Fo5176
Lipids
50
1243-1252
2015
-
-
1
-
-
-
-
-
-
-
-
5
-
12
-
-
-
-
-
-
-
-
29
-
2
2
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
29
-
2
2
-
-
-
-
-
-
-
2
2
-
-
-
724132
Hoffmann
7,8- and 5,8-linoleate diol sy ...
Aspergillus fumigatus, Gaeumannomyces graminis
Arch. Biochem. Biophys.
539
87-91
2013
-
-
2
-
7
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
5
2
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
2
-
-
-
-
-
-
-
-
-
2
2
-
-
-
711024
Hoffmann
Expression of 5,8-LDS of Asper ...
Aspergillus fumigatus, Gaeumannomyces graminis
Arch. Biochem. Biophys.
506
216-222
2010
-
-
2
-
6
-
-
2
-
-
-
3
-
4
-
-
-
-
-
2
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
7
-
-
-
-
2
-
-
-
3
-
-
-
-
-
2
-
-
10
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
714317
Jernerén
Reaction mechanism of 5,8-lino ...
Aspergillus clavatus
Biochim. Biophys. Acta
1801
503-507
2010
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
704466
Brodhun
Identification of PpoA from As ...
Aspergillus nidulans
J. Biol. Chem.
284
11792-11805
2009
-
-
1
-
2
-
1
4
-
-
2
1
-
1
-
-
1
-
-
-
1
-
7
1
1
-
-
4
1
-
-
2
-
-
-
-
-
1
2
-
2
-
-
1
-
4
-
-
2
1
-
-
-
1
-
-
1
-
7
1
1
-
-
4
1
-
-
-
-
-
-
-
4
4
704475
Garscha
Leucine/valine residues direct ...
Gaeumannomyces graminis
J. Biol. Chem.
284
13755-13765
2009
-
-
1
-
4
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
702018
Garscha
Pichia expression and mutagene ...
Gaeumannomyces graminis, Gaeumannomyces graminis var. avenae
Biochem. Biophys. Res. Commun.
373
579-583
2008
-
-
1
-
3
-
-
-
-
-
-
2
-
4
-
1
1
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
2
-
-
1
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
703700
Garscha
Critical amino acids for the 8 ...
Gaeumannomyces graminis
FEBS Lett.
582
3547-3551
2008
-
-
1
-
11
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285246
Hörnsten
Cloning of linoleate diol synt ...
Gaeumannomyces graminis
J. Biol. Chem.
274
28219-28224
1999
-
-
1
-
-
-
-
-
-
1
1
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285251
Oliw
Catalytic properties of linole ...
Gaeumannomyces graminis
Adv. Exp. Med. Biol.
469
679-685
1999
2
-
-
-
-
-
2
-
-
-
1
1
-
2
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
1
-
-
-
2
-
-
1
-
-
-
-
2
-
-
-
-
1
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285244
Su
A protein radical and ferryl i ...
Gaeumannomyces graminis
J. Biol. Chem.
273
20744-20751
1998
-
-
-
-
-
-
1
-
-
-
-
2
-
3
-
-
1
-
-
1
-
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
2
-
-
-
-
-
2
-
-
-
2
-
2
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285243
Su
Purification and characterizat ...
Gaeumannomyces graminis
J. Biol. Chem.
271
14112-14118
1996
-
-
-
-
-
2
2
2
-
-
2
1
1
1
-
-
1
-
-
1
1
1
2
1
-
-
-
1
1
-
-
1
-
1
-
-
-
-
1
-
-
2
-
2
-
2
-
-
2
1
1
-
-
1
-
1
1
1
2
1
-
-
-
1
1
-
-
1
-
-
-
-
-
-
285249
Su
Studies on linoleic acid 8R-di ...
Gaeumannomyces graminis
Lipids
30
43-50
1995
-
-
-
-
-
1
16
-
-
-
-
1
-
3
-
-
1
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
1
-
16
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
285247
Brodowsky
BW A4C and other hydroxamic ac ...
Gaeumannomyces graminis
Eur. J. Pharmacol.
254
43-47
1994
-
-
-
-
-
-
12
-
-
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
1
-
-
-
6
-
-
-
-
-
-
-
6
12
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
285248
Brodowsky
Linoleic acid 8R-dioxygenase a ...
Gaeumannomyces graminis
Ann. N. Y. Acad. Sci.
744
314-316
1994
-
-
-
-
-
-
5
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
5
5
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285250
Hamberg
Sequential oxygenation of lino ...
Gaeumannomyces graminis
Arch. Biochem. Biophys.
309
77-80
1994
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285245
Brodowsky
A linoleic acid (8R)-dioxygena ...
Gaeumannomyces graminis
J. Biol. Chem.
267
14738-14745
1992
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-