BRENDA - Enzyme Database show
show all sequences of 1.13.11.61

Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms

Andreou, A.Z.; Vanko, M.; Bezakova, L.; Feussner, I.; Phytochemistry 69, 1832-1837 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant carboxy-terminal domain is purified after expression in Escherichia coli
Nostoc sp.
Engineering
Amino acid exchange
Commentary
Organism
A162G
the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)
Nostoc sp.
A162I
the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)
Nostoc sp.
A162V
the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)
Nostoc sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0044
-
linoleate
pH 7.5, 22°C, wild-type enzyme
Nostoc sp.
0.005
-
linoleate
pH 7.5, 22°C, mutant enzyme A162V
Nostoc sp.
0.0056
-
linoleate
pH 7.5, 22°C, mutant enzyme A162I
Nostoc sp.
0.0089
-
linoleate
pH 7.5, 22°C, mutant enzyme A162G
Nostoc sp.
0.026
-
alpha-linolenate
pH 7.5, 22°C, wild-type enzyme
Nostoc sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Nostoc sp.
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant carboxy-terminal domain is purified after expression in Escherichia coli
Nostoc sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-linolenate + O2
i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
716450
Nostoc sp.
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
-
-
?
linoleate + O2
i.e. (9Z,12Z)-octadeca-9,12-dienoate
716450
Nostoc sp.
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
configuration of the 9-hydroperoxide is primarily R (93%). (13S)-Hydroperoxy octadecadienoic acid is detected in small amounts as by-product
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant carboxy-terminal domain is purified after expression in Escherichia coli
Nostoc sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A162G
the recombinant carboxy-terminal domain of the wild-type enzyme and of mutant enzyme A162G produce primarily (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate from linoleate. The stereochemistry of the hydroperoxide is almost exclusively R (93-94%)
Nostoc sp.
A162I
the recombinant carboxy-terminal domain of the mutant enzyme A162I produces almost exlusively (13S)-hydroperoxy octadecadienoic acid (90%)
Nostoc sp.
A162V
the recombinant carboxy-terminal domain of the mutant enzyme A162V converts linoleate primarily to (13S)-hydroperoxy octadecadienoic acid (64%) and to a lesser extent to (9R,10EZ,12Z)-9-hydroperoxy-10,12-octadecadienoate (36%)
Nostoc sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0044
-
linoleate
pH 7.5, 22°C, wild-type enzyme
Nostoc sp.
0.005
-
linoleate
pH 7.5, 22°C, mutant enzyme A162V
Nostoc sp.
0.0056
-
linoleate
pH 7.5, 22°C, mutant enzyme A162I
Nostoc sp.
0.0089
-
linoleate
pH 7.5, 22°C, mutant enzyme A162G
Nostoc sp.
0.026
-
alpha-linolenate
pH 7.5, 22°C, wild-type enzyme
Nostoc sp.
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant carboxy-terminal domain is purified after expression in Escherichia coli
Nostoc sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
alpha-linolenate + O2
i.e. (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
716450
Nostoc sp.
(9R,10E,12Z,15Z)-9-hydroperoxy-10,12,15-octadecatrienoate
-
-
-
?
linoleate + O2
i.e. (9Z,12Z)-octadeca-9,12-dienoate
716450
Nostoc sp.
(9R,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
configuration of the 9-hydroperoxide is primarily R (93%). (13S)-Hydroperoxy octadecadienoic acid is detected in small amounts as by-product
-
-
?
Other publictions for EC 1.13.11.61
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)
743826
Newie
Lipoxygenase 2 from Cyanothec ...
Cyanothece sp. PCC 8801
Sci. Rep.
7
2069
2017
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-
1
1
3
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1
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1
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2
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1
1
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3
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1
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1
1
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1
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3
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1
1
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743586
Kim
Selective production of 9R-hy ...
Nostoc sp., Nostoc sp. SAG 25.82
PLoS ONE
10
e0137785
2015
5
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1
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7
4
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1
6
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4
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1
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3
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10
1
1
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3
1
1
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5
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1
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7
-
4
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1
6
-
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1
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3
-
10
1
1
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3
1
1
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3
3
713948
Jernerén
Linoleate 9R-dioxygenase and a ...
Aspergillus terreus
Arch. Biochem. Biophys.
495
67-73
2010
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3
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1
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1
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2
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1
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684995
Lang
A lipoxygenase with linoleate ...
Nostoc sp.
Biochem. J.
410
347-357
2008
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1
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1
2
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6
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4
1
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1
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1
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1
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4
1
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1
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716450
Andreou
Properties of a mini 9R-lipoxy ...
Nostoc sp.
Phytochemistry
69
1832-1837
2008
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1
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3
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5
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3
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1
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