BRENDA - Enzyme Database
show all sequences of 1.13.11.62

Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus

Jernerén, F.; Garscha, U.; Hoffmann, I.; Hamberg, M.; Oliw, E.H.; Biochim. Biophys. Acta 1801, 503-507 (2010)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
linoleate + O2
Aspergillus clavatus
the enzyme is involved in biosynthesis of oxylipins
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Aspergillus clavatus
Q4W941
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus clavatus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
linoleate + O2
the enzyme is involved in biosynthesis of oxylipins
714317
Aspergillus clavatus
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
linoleate + O2
abstraction of the pro-S hydrogen at C-8 and antarafacial dioxygenation at C-10 with double bond migration
714317
Aspergillus clavatus
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
10R-dioxygenase
-
Aspergillus clavatus
10R-DOX
-
Aspergillus clavatus
PpoC
-
Aspergillus clavatus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Aspergillus clavatus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Aspergillus clavatus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
linoleate + O2
Aspergillus clavatus
the enzyme is involved in biosynthesis of oxylipins
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mycelium
-
Aspergillus clavatus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
linoleate + O2
the enzyme is involved in biosynthesis of oxylipins
714317
Aspergillus clavatus
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
linoleate + O2
abstraction of the pro-S hydrogen at C-8 and antarafacial dioxygenation at C-10 with double bond migration
714317
Aspergillus clavatus
(8E,10R,12Z)-10-hydroperoxy-8,12-octadecadienoate
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Aspergillus clavatus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Aspergillus clavatus
Other publictions for EC 1.13.11.62
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
Synonyms
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)
744123
Han
Production of 10R-hydroxy uns ...
Aspergillus nidulans, Aspergillus nidulans ATCC 10074
Appl. Microbiol. Biotechnol.
100
7933-7944
2016
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1
1
-
1
-
-
-
-
-
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6
-
4
-
-
1
-
-
-
4
-
13
-
3
1
1
1
-
1
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-
-
-
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-
1
1
-
-
1
-
-
-
-
-
-
-
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6
-
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1
-
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4
-
13
-
1
1
1
-
1
-
-
-
-
1
1
-
-
-
714317
Jernerén
Reaction mechanism of 5,8-lino ...
Aspergillus clavatus
Biochim. Biophys. Acta
1801
503-507
2010
-
-
-
-
-
-
-
-
-
-
-
1
-
4
-
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1
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2
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3
1
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1
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1
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1
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2
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1
-
-
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1
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-
-
-
-
-
-
-
704475
Garscha
Leucine/valine residues direct ...
Aspergillus fumigatus
J. Biol. Chem.
284
13755-13765
2009
-
-
1
-
8
-
-
1
-
-
-
1
-
2
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-
-
-
-
-
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4
-
2
-
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-
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-
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-
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1
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-
8
-
-
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1
-
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1
-
-
-
-
-
-
-
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4
-
-
-
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-
-
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-
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1
1
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