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show all sequences of 1.13.11.62

Production of 10R-hydroxy unsaturated fatty acids from hempseed oil hydrolyzate by recombinant Escherichia coli cells expressing PpoC from Aspergillus nidulans

Han, J.E.; Seo, M.J.; Shin, K.C.; Oh, D.K.; Appl. Microbiol. Biotechnol. 100, 7933-7944 (2016)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization
Aspergillus nidulans
Cloned(Commentary)
Commentary
Organism
functional recombinant expression of His-tagged enzyme in Escherichia coli strain ER2566
Aspergillus nidulans
Engineering
Amino acid exchange
Commentary
Organism
additional information
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization, optimization of concentrations of cells and substrate, pH and temperature, for the production of 10R-hydroxy unsaturated fatty acids, overview. Recombinant enzyme PpoC in Escherichia coli cells is more stable than the purified recombinant PpoC
Aspergillus nidulans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
alpha-linolenate + O2
Aspergillus nidulans
-
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
?
alpha-linolenate + O2
Aspergillus nidulans ATCC 10074
-
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
?
linoleate + O2
Aspergillus nidulans
-
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
?
linoleate + O2
Aspergillus nidulans ATCC 10074
-
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
?
additional information
Aspergillus nidulans
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
?
-
-
-
additional information
Aspergillus nidulans ATCC 10074
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aspergillus nidulans
-
-
-
Aspergillus nidulans ATCC 10074
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain ER2566 by nickel affinity chromatography and ultafiltration
Aspergillus nidulans
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.065
-
purified recombinant enzyme, substrate oleate, pH 8.0, 30°C
Aspergillus nidulans
0.108
-
purified recombinant enzyme, substrate palmitoleate, pH 8.0, 30°C
Aspergillus nidulans
0.485
-
purified recombinant enzyme, substrate alpha-linolenate, pH 8.0, 30°C
Aspergillus nidulans
0.761
-
purified recombinant enzyme, substrate linoleate, pH 8.0, 30°C
Aspergillus nidulans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-linolenate + O2
-
744123
Aspergillus nidulans
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
alpha-linolenate + O2
moderate activity
744123
Aspergillus nidulans
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
alpha-linolenate + O2
-
744123
Aspergillus nidulans ATCC 10074
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
alpha-linolenate + O2
moderate activity
744123
Aspergillus nidulans ATCC 10074
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
linoleate + O2
-
744123
Aspergillus nidulans
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
linoleate + O2
best substrate
744123
Aspergillus nidulans
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
linoleate + O2
-
744123
Aspergillus nidulans ATCC 10074
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
additional information
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
744123
Aspergillus nidulans
?
-
-
-
-
additional information
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
744123
Aspergillus nidulans
?
-
-
-
-
additional information
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
744123
Aspergillus nidulans ATCC 10074
?
-
-
-
-
additional information
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
744123
Aspergillus nidulans ATCC 10074
?
-
-
-
-
oleate + O2
low activity
744123
Aspergillus nidulans
8-hydroperoxy-9(Z)-octadecenoic acid
-
-
-
?
palmitoleate + O2
low activity
744123
Aspergillus nidulans
8-hydroperoxy-9(Z)-hexadecenoic acid
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
recombinant enzyme
Aspergillus nidulans
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
40
over 70% of maximal activity within this range
Aspergillus nidulans
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
40
half-lives of recombinant PpoC in Escherichia coli cells at 30°C, 35°C, and 40°C are 530, 315, and 97 min, respectively, while those of purified recombinant enzyme are 41, 29, and 18 min, respectively. The half-lives of the recombinant enzyme in Escherichia coli cells are 12.9, 10.9, and 5.4fold higher at 30°C, 35°C, and 40°C, respectively, than those of the purified recombinant enzyme, indicating that thermal stability of recombinant PpoC in expressing cells is higher than that of the purified recombinant PpoC
Aspergillus nidulans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
recombinant enzyme
Aspergillus nidulans
Application (protein specific)
Application
Commentary
Organism
synthesis
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization
Aspergillus nidulans
Cloned(Commentary) (protein specific)
Commentary
Organism
functional recombinant expression of His-tagged enzyme in Escherichia coli strain ER2566
Aspergillus nidulans
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization, optimization of concentrations of cells and substrate, pH and temperature, for the production of 10R-hydroxy unsaturated fatty acids, overview. Recombinant enzyme PpoC in Escherichia coli cells is more stable than the purified recombinant PpoC
Aspergillus nidulans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
alpha-linolenate + O2
Aspergillus nidulans
-
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
?
alpha-linolenate + O2
Aspergillus nidulans ATCC 10074
-
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
?
linoleate + O2
Aspergillus nidulans
-
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
?
linoleate + O2
Aspergillus nidulans ATCC 10074
-
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
?
additional information
Aspergillus nidulans
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
?
-
-
-
additional information
Aspergillus nidulans ATCC 10074
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain ER2566 by nickel affinity chromatography and ultafiltration
Aspergillus nidulans
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.065
-
purified recombinant enzyme, substrate oleate, pH 8.0, 30°C
Aspergillus nidulans
0.108
-
purified recombinant enzyme, substrate palmitoleate, pH 8.0, 30°C
Aspergillus nidulans
0.485
-
purified recombinant enzyme, substrate alpha-linolenate, pH 8.0, 30°C
Aspergillus nidulans
0.761
-
purified recombinant enzyme, substrate linoleate, pH 8.0, 30°C
Aspergillus nidulans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-linolenate + O2
-
744123
Aspergillus nidulans
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
alpha-linolenate + O2
moderate activity
744123
Aspergillus nidulans
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
alpha-linolenate + O2
-
744123
Aspergillus nidulans ATCC 10074
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
alpha-linolenate + O2
moderate activity
744123
Aspergillus nidulans ATCC 10074
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
linoleate + O2
-
744123
Aspergillus nidulans
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
linoleate + O2
best substrate
744123
Aspergillus nidulans
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
linoleate + O2
-
744123
Aspergillus nidulans ATCC 10074
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
additional information
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
744123
Aspergillus nidulans
?
-
-
-
-
additional information
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
744123
Aspergillus nidulans
?
-
-
-
-
additional information
the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate
744123
Aspergillus nidulans ATCC 10074
?
-
-
-
-
additional information
assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview
744123
Aspergillus nidulans ATCC 10074
?
-
-
-
-
oleate + O2
low activity
744123
Aspergillus nidulans
8-hydroperoxy-9(Z)-octadecenoic acid
-
-
-
?
palmitoleate + O2
low activity
744123
Aspergillus nidulans
8-hydroperoxy-9(Z)-hexadecenoic acid
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
recombinant enzyme
Aspergillus nidulans
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
40
over 70% of maximal activity within this range
Aspergillus nidulans
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
40
half-lives of recombinant PpoC in Escherichia coli cells at 30°C, 35°C, and 40°C are 530, 315, and 97 min, respectively, while those of purified recombinant enzyme are 41, 29, and 18 min, respectively. The half-lives of the recombinant enzyme in Escherichia coli cells are 12.9, 10.9, and 5.4fold higher at 30°C, 35°C, and 40°C, respectively, than those of the purified recombinant enzyme, indicating that thermal stability of recombinant PpoC in expressing cells is higher than that of the purified recombinant PpoC
Aspergillus nidulans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
recombinant enzyme
Aspergillus nidulans
General Information
General Information
Commentary
Organism
evolution
Psi-producing oxygenases (Ppo enzymes) are classified as three enzyme types: PpoA (5,8-diol synthase), PpoB (suggested as 8,11-diol synthase), and PpoC (10R-dioxygenase)
Aspergillus nidulans
General Information (protein specific)
General Information
Commentary
Organism
evolution
Psi-producing oxygenases (Ppo enzymes) are classified as three enzyme types: PpoA (5,8-diol synthase), PpoB (suggested as 8,11-diol synthase), and PpoC (10R-dioxygenase)
Aspergillus nidulans
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
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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13
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1
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714317
Jernerén
Reaction mechanism of 5,8-lino ...
Aspergillus clavatus
Biochim. Biophys. Acta
1801
503-507
2010
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4
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704475
Garscha
Leucine/valine residues direct ...
Aspergillus fumigatus
J. Biol. Chem.
284
13755-13765
2009
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8
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