BRENDA - Enzyme Database
show all sequences of 1.13.11.77

An ancient relative of cyclooxygenase in cyanobacteria is a linoleate 10S-dioxygenase that works in tandem with a catalase-related protein with specific 10S-hydroperoxide lyase activity

Brash, A.R.; Niraula, N.P.; Boeglin, W.E.; Mashhadi, Z.; J. Biol. Chem. 289, 13101-13111 (2014)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene Npun_R5469, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli
Nostoc punctiforme
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.013
-
alpha-linolenate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
0.063
-
linoleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
0.113
-
oleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
alpha-linolenate + O2
Nostoc punctiforme
-
(8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
?
linoleate + O2
Nostoc punctiforme
-
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
?
oleate + O2
Nostoc punctiforme
-
(8E,10S)-10-hydroperoxyoctadeca-8-enoate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Nostoc punctiforme
B2J5P4
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Nostoc punctiforme
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
alpha-linolenate + O2
-
745297
Nostoc punctiforme
(8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
linoleate + O2
-
745297
Nostoc punctiforme
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
linoleate + O2
racemic substrate, absolute stereospecific reaction, only formation of 10S product
745297
Nostoc punctiforme
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
additional information
enzyme Np-diox is best described as an oleate or linoleate dioxygenase, albeit with alpha-linolenic acid very competitive at low substrate concentrations
745297
Nostoc punctiforme
?
-
-
-
-
additional information
racemic 1-octen-3-ol is formed in reaction of linoleate 10S-hydroperoxide with hematin or ferrous ions
745297
Nostoc punctiforme
?
-
-
-
-
oleate + O2
-
745297
Nostoc punctiforme
(8E,10S)-10-hydroperoxyoctadeca-8-enoate
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
heme dioxygenase
-
Nostoc punctiforme
linoleate 10S-dioxygenase
-
Nostoc punctiforme
linoleate heme 10S-dioxygenase
-
Nostoc punctiforme
Np-diox
-
Nostoc punctiforme
Npun_R5469
-
Nostoc punctiforme
oleate heme 10S-dioxygenase
-
Nostoc punctiforme
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
31
-
alpha-linolenate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
135
-
linoleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
178
-
oleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Npun_R5469, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli
Nostoc punctiforme
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.013
-
alpha-linolenate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
0.063
-
linoleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
0.113
-
oleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
alpha-linolenate + O2
Nostoc punctiforme
-
(8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
?
linoleate + O2
Nostoc punctiforme
-
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
?
oleate + O2
Nostoc punctiforme
-
(8E,10S)-10-hydroperoxyoctadeca-8-enoate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
Nostoc punctiforme
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
alpha-linolenate + O2
-
745297
Nostoc punctiforme
(8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
-
-
-
?
linoleate + O2
-
745297
Nostoc punctiforme
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
linoleate + O2
racemic substrate, absolute stereospecific reaction, only formation of 10S product
745297
Nostoc punctiforme
(8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
-
-
-
?
additional information
enzyme Np-diox is best described as an oleate or linoleate dioxygenase, albeit with alpha-linolenic acid very competitive at low substrate concentrations
745297
Nostoc punctiforme
?
-
-
-
-
additional information
racemic 1-octen-3-ol is formed in reaction of linoleate 10S-hydroperoxide with hematin or ferrous ions
745297
Nostoc punctiforme
?
-
-
-
-
oleate + O2
-
745297
Nostoc punctiforme
(8E,10S)-10-hydroperoxyoctadeca-8-enoate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
31
-
alpha-linolenate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
135
-
linoleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
178
-
oleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
General Information
General Information
Commentary
Organism
evolution
linoleate 10S-dioxygenase is an ancient relative of cyclooxygenase in cyanobacteria, linoleate 10S-dioxygenase works in tandem with a catalase-related protein with specific 10S-hydroperoxide lyase activity. Neighboring cyanobacterial genes, dioxygenase and catalase, are identified as linoleate 10S-dioxygenase and 10Shydroperoxide lyase, respectively. The Nostoc linoleate 10S-dioxygenase, the sequence of which contains the signature catalytic sequence of cyclooxygenases and fungal linoleate dioxygenases (YRWH), appears to be a heme dioxygenase ancestor
Nostoc punctiforme
metabolism
the immediate downstream gene, Np-cat, encodes a specific linoleate 10S-hydroperoxide lyase (10S-hydroperoxyoleate being metabolized at only 3% of the rate) converting the product of Np-diox and working in tandem with it
Nostoc punctiforme
physiological function
enzyme Np-diox is an oleate and linoleate heme 10S-dioxygenase-alpha-linolenate is also efficiently metabolized at lower concentrations, but it much more rapidly leads to enzyme inactivation
Nostoc punctiforme
General Information (protein specific)
General Information
Commentary
Organism
evolution
linoleate 10S-dioxygenase is an ancient relative of cyclooxygenase in cyanobacteria, linoleate 10S-dioxygenase works in tandem with a catalase-related protein with specific 10S-hydroperoxide lyase activity. Neighboring cyanobacterial genes, dioxygenase and catalase, are identified as linoleate 10S-dioxygenase and 10Shydroperoxide lyase, respectively. The Nostoc linoleate 10S-dioxygenase, the sequence of which contains the signature catalytic sequence of cyclooxygenases and fungal linoleate dioxygenases (YRWH), appears to be a heme dioxygenase ancestor
Nostoc punctiforme
metabolism
the immediate downstream gene, Np-cat, encodes a specific linoleate 10S-hydroperoxide lyase (10S-hydroperoxyoleate being metabolized at only 3% of the rate) converting the product of Np-diox and working in tandem with it
Nostoc punctiforme
physiological function
enzyme Np-diox is an oleate and linoleate heme 10S-dioxygenase-alpha-linolenate is also efficiently metabolized at lower concentrations, but it much more rapidly leads to enzyme inactivation
Nostoc punctiforme
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1600
-
oleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
2100
-
linoleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
2400
-
alpha-linolenate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
1600
-
oleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
2100
-
linoleate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
2400
-
alpha-linolenate
recombinant enzyme, pH and temperature not specified in the publication
Nostoc punctiforme
Other publictions for EC
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)
744582
Kim
Production of 10S-hydroxy-8(E ...
Nostoc punctiforme
Biotechnol. Lett.
39
133-139
2017
1
-
1
-
1
-
-
3
-
-
-
3
-
4
-
-
1
-
-
-
3
-
4
1
-
1
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
3
-
-
-
3
-
-
-
1
-
-
3
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
744396
Mashhadi
Robust inhibitory effects of ...
Nostoc punctiforme
Biochim. Biophys. Acta
1851
1346-1352
2015
-
-
-
-
-
-
11
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
2
-
-
-
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-
-
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-
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-
-
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-
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11
-
-
-
-
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1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
745297
Brash
An ancient relative of cycloo ...
Nostoc punctiforme
J. Biol. Chem.
289
13101-13111
2014
-
-
1
-
-
-
-
3
-
-
-
3
-
6
-
-
1
-
-
-
-
-
6
-
6
-
-
-
3
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
3
-
-
-
1
-
-
-
-
6
-
-
-
-
3
-
-
-
-
-
3
3
-
3
3
725415
Martinez
Biochemical characterization o ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa 42A2
J. Biol. Chem.
285
9339-9345
2010
-
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
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-
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-
-
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1
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-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723962
Busquets
Isolation and characterization ...
Pseudomonas sp., Pseudomonas sp. 42A2
Antonie van Leeuwenhoek
85
129-139
2004
-
-
-
-
-
-
7
3
1
3
1
4
-
2
-
-
1
-
-
-
-
1
13
1
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
3
1
3
1
4
-
-
-
1
-
-
-
1
13
1
1
-
1
-
1
-
-
-
-
-
-
-
-
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