BRENDA - Enzyme Database show
show all sequences of 1.13.11.B6

A lipoxygenase with dual positional specificity is expressed in olives (Olea europaea L.) during ripening

Palmieri-Thiers, C.; Canaan, S.; Brunini, V.; Lorenzi, V.; Tomi, F.; Desseyn, J.L.; Garscha, U.; Oliw, E.H.; Berti, L.; Maury, J.; Biochim. Biophys. Acta 1791, 339-346 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Olea europaea
Inhibitors
Inhibitors
Commentary
Organism
Structure
nordihydroguaiaretic acid
noncompetitive
Olea europaea
propyl gallate
competitive
Olea europaea
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.175
-
linoleate
25°C
Olea europaea
0.344
-
linolenate
25°C
Olea europaea
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
likely confined to the cytosol, because it contains neither consensus targeting nor retention signals for any organelles
Olea europaea
5829
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
98000
-
x * 98000, SDS-PAGE
Olea europaea
98400
-
x * 98400, calculated from sequence
Olea europaea
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Olea europaea
B6D1W5
L., Leccino variety
-
Purification (Commentary)
Commentary
Organism
-
Olea europaea
Source Tissue
Source Tissue
Commentary
Organism
Textmining
fruit
detected in all olive developmental and ripening stages from green small fruits to black or senescent fruits. Mainly expressed at late developmental stages
Olea europaea
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
23.4
-
-
Olea europaea
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + O2
the catalytic efficiency of the recombinant olive LOX was significantly higher for linoleic acid hydroperoxidation than for linolenic acid hydroperoxidation
702431
Olea europaea
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
dual positional specificity: the enzyme forms (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate in a 2:1 ratio, the products are predominantly in 9S and 13R configuration
-
-
?
linolenate + O2
the catalytic efficiency of the recombinant olive LOX is significantly higher for linoleic acid hydroperoxidation than for linolenic acid hydroperoxidation
702431
Olea europaea
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 98000, SDS-PAGE; x * 98400, calculated from sequence
Olea europaea
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
47.8
-
linolenate
25°C
Olea europaea
48.6
-
linoleate
25°C
Olea europaea
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Olea europaea
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00188
-
propyl gallate
25°C
Olea europaea
0.00409
-
nordihydroguaiaretic acid
25°C
Olea europaea
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Olea europaea
calculated from sequence
-
5.95
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Olea europaea
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
nordihydroguaiaretic acid
noncompetitive
Olea europaea
propyl gallate
competitive
Olea europaea
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00188
-
propyl gallate
25°C
Olea europaea
0.00409
-
nordihydroguaiaretic acid
25°C
Olea europaea
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.175
-
linoleate
25°C
Olea europaea
0.344
-
linolenate
25°C
Olea europaea
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
likely confined to the cytosol, because it contains neither consensus targeting nor retention signals for any organelles
Olea europaea
5829
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
98000
-
x * 98000, SDS-PAGE
Olea europaea
98400
-
x * 98400, calculated from sequence
Olea europaea
Purification (Commentary) (protein specific)
Commentary
Organism
-
Olea europaea
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
fruit
detected in all olive developmental and ripening stages from green small fruits to black or senescent fruits. Mainly expressed at late developmental stages
Olea europaea
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
23.4
-
-
Olea europaea
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleate + O2
the catalytic efficiency of the recombinant olive LOX was significantly higher for linoleic acid hydroperoxidation than for linolenic acid hydroperoxidation
702431
Olea europaea
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate + (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate
dual positional specificity: the enzyme forms (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E,13R)-13-hydroperoxy-9,11-octadecadienoate in a 2:1 ratio, the products are predominantly in 9S and 13R configuration
-
-
?
linolenate + O2
the catalytic efficiency of the recombinant olive LOX is significantly higher for linoleic acid hydroperoxidation than for linolenic acid hydroperoxidation
702431
Olea europaea
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 98000, SDS-PAGE; x * 98400, calculated from sequence
Olea europaea
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
47.8
-
linolenate
25°C
Olea europaea
48.6
-
linoleate
25°C
Olea europaea
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Olea europaea
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Olea europaea
calculated from sequence
-
5.95
General Information
General Information
Commentary
Organism
physiological function
the 9/13-LOX is associated with the ripening and senescence processes. Due to its dual positional specificity and its expression pattern, its contribution to the elaboration of the olive oil aroma might be considered
Olea europaea
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the 9/13-LOX is associated with the ripening and senescence processes. Due to its dual positional specificity and its expression pattern, its contribution to the elaboration of the olive oil aroma might be considered
Olea europaea
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
139
-
linolenate
25°C
Olea europaea
278
-
linoleate
25°C
Olea europaea
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
139
-
linolenate
25°C
Olea europaea
278
-
linoleate
25°C
Olea europaea
Other publictions for EC 1.13.11.B6
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)
742627
Schiller
A dual positional specific li ...
Malus domestica
Hortic. Res.
2
15003-15015
2015
-
-
1
-
7
-
-
1
1
-
-
4
-
4
-
-
1
-
-
2
-
-
6
1
2
2
-
-
2
2
-
-
-
-
-
-
-
2
-
-
8
-
-
-
-
2
2
-
-
4
-
-
-
2
-
4
-
-
6
2
2
2
-
-
2
2
-
-
-
4
7
-
-
-
725658
Wennman
Secretion of two novel enzymes ...
Nakataea oryzae, Nakataea oryzae CBS 288.54
J. Lipid Res.
54
762-775
2013
-
-
1
-
2
1
-
1
1
3
1
-
-
5
-
-
1
-
-
1
-
1
8
1
1
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
2
1
-
-
-
1
1
3
1
-
-
-
-
1
-
1
-
1
8
1
1
-
-
1
1
-
-
-
-
2
2
-
1
1
725856
Jerneren
Linolenate 9R-dioxygenase and ...
Lasiodiplodia theobromae, Lasiodiplodia theobromae 2334, Lasiodiplodia theobromae CBS 117454, Lasiodiplodia theobromae CBS 122127
Lipids
47
65-73
2012
-
-
-
-
-
-
-
-
1
-
-
13
-
6
-
-
-
-
-
1
-
-
17
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
13
-
-
-
-
-
1
-
-
17
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
724736
Chechetkin
Oxidation of glycerolipids by ...
Zea mays
Chem. Phys. Lipids
164
216-220
2011
-
-
1
-
1
-
-
-
-
-
-
3
-
2
-
-
-
-
-
-
-
-
12
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
12
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
702431
Palmieri-Thiers
A lipoxygenase with dual posit ...
Olea europaea
Biochim. Biophys. Acta
1791
339-346
2009
-
-
1
-
-
-
2
2
1
-
2
-
-
1
-
-
1
-
-
1
1
-
2
1
-
-
-
2
1
-
-
-
2
1
-
-
-
1
-
-
-
-
-
2
2
2
1
-
2
-
-
-
-
1
-
1
1
-
2
1
-
-
-
2
1
-
-
1
-
1
1
-
2
2
706122
Hornung
Identification of an amino aci ...
Momordica charantia
Phytochemistry
69
2774-2780
2008
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
706252
Wang
A novel lipoxygenase gene from ...
Oryza sativa
Plant Mol. Biol.
66
401-414
2008
-
-
1
-
-
-
-
-
-
-
1
1
-
5
-
-
-
-
-
3
-
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
3
-
-
2
1
-
-
-
-
1
-
-
-
2
1
1
2
-
-
674388
Cho
Biochemical characterization o ...
Zea mays
J. Biochem. Mol. Biol.
40
100-106
2007
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
706289
Veronico
A novel lipoxygenase in pea ro ...
Pisum sativum
Plant Physiol.
141
1045-1055
2006
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
3
1
-
-
-
-
-
-
-
-
1
1
1
1
-
-
703538
Santino
Biochemical and molecular char ...
Corylus avellana
Eur. J. Biochem.
270
4365-4375
2003
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
706251
Kim
Dual positional specificity an ...
Zea mays
Plant Mol. Biol.
52
1203-1213
2003
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
396190
Hughes
Probing a novel potato lipoxyg ...
Solanum tuberosum
Biochem. J.
353
345-355
2001
-
-
1
-
3
-
-
1
-
-
-
-
-
7
-
-
1
-
-
1
1
-
2
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
1
-
1
1
-
2
-
-
-
-
1
1
1
-
-
-
-
-
-
1
1
703535
Hughes
Mutagenesis and modelling of l ...
Pisum sativum
Eur. J. Biochem.
268
1030-1040
2001
-
-
1
-
8
-
-
1
-
-
1
-
-
4
-
-
1
-
-
-
-
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
8
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
1
1
706250
Burow
A peanut seed lipoxygenase res ...
Arachis hypogaea
Plant Mol. Biol.
42
689-701
2000
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
396184
Hughes
-
Characterization of authentic ...
Pisum sativum
Biochem. J.
333
33-43
1998
-
-
1
-
-
-
-
3
-
-
4
-
-
2
-
-
1
2
-
1
4
-
2
1
-
-
-
3
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
3
-
-
4
-
-
-
-
2
-
2
4
-
2
2
-
-
-
3
3
-
-
-
-
-
-
-
3
3
706645
Skrzypczak-Jankun
Structure of soybean lipoxygen ...
Glycine max
Proteins
29
15-31
1997
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
702394
Gardner
Soybean lipoxygenase-1 enzymic ...
Glycine max
Biochim. Biophys. Acta
1001
274-281
1989
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-