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

Oxidation of glycerolipids by maize 9-lipoxygenase and its A562G mutant

Chechetkin, I.R.; Osipova, E.V.; Antsygina, L.L.; Gogolev, Y.V.; Grechkin, A.N.; Chem. Phys. Lipids 164, 216-220 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS
Zea mays
Engineering
Amino acid exchange
Commentary
Organism
A562G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutation does not affect the relative yield of 13-hydroperoxide, but increases the proportion of (13R)-enantiomer compared to the wild-type enzyme
Zea mays
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + O2
Zea mays
-
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
?
linoleate + O2
Zea mays
-
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
?
additional information
Zea mays
both the wild type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine, the latter being a poor substrate. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits limited regio- and stereospecificity: the wild-type ZmLOX produces some predominance of (13S)-hydroperoxide. In contrast, the A562G mutant produces some excess of (9S)-hydroperoxide
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Zea mays
-
-
-
Zea mays
Q9AXG8
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
-
724736
Zea mays
?
-
-
-
?
1,2-di-O-alpha-linolenoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + O2
low activity with the wild-type enzyme, no activity with mutant A562G
724736
Zea mays
?
-
-
-
?
2-linoleoyl-sn-glycero-3-phosphorylcholine + O2
low activity of wild-type and A562G mutant. The wild-type enzyme predominantly produces (13S)-hydroperoxide. The A562G mutant form possesses lesser regio- and stereospecificity during the dioxygenation of lysoPC. It produces 28% of (10E,12Z)-9-hydroperoxide and 30% of (9Z,11E)-13-hydroperoxide along with 41% of (all-E)-hydroperoxides. While 9-hydroperoxide is present mainly (61%) as S-enantiomer, (9Z,11E)-13-hydroperoxide is nearly racemic
724736
Zea mays
?
-
-
-
?
2-linoleoyl-sn-glycero-3-phosphorylcholine + O2
the wild-type ZmLOX produces predominantly (13S)-hydroperoxide. In contrast, the A562G mutant produces excessively (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits the limited regio- and stereospecificity. But the A562G mutant form possesses lesser regio- and stereospecificity
724736
Zea mays
?
-
-
-
?
linoleate + O2
-
724736
Zea mays
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
?
linoleate + O2
-
724736
Zea mays
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
-
724736
Zea mays
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate
-
-
-
?
monolinolenoylglycerol + O2
isolated from flax leaves, both the wild-type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The A562G mutation does not affect the relative yield of 13-hydroperoxide, but increases the proportion of (13R)-enantiomer
724736
Zea mays
?
-
-
-
?
monolinolenoylglycerol + O2
wild-type enzyme and mutant A562G predominantly produce (9S)-hydroperoxide
724736
Zea mays
?
-
-
-
?
additional information
both the wild type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine, the latter being a poor substrate. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits limited regio- and stereospecificity: the wild-type ZmLOX produces some predominance of (13S)-hydroperoxide. In contrast, the A562G mutant produces some excess of (9S)-hydroperoxide
724736
Zea mays
?
-
-
-
-
additional information
Bulky polar heads of glycerolipids cannot penetrate into the LOX active site. Both (9S)- and (13S)-hydroperoxides can be produced when the substrate is arranged within LOX active site in the methyl end first orientation. 1-Linoleoyl-snglycero-3-phosphorylcholine is a poor substrate for both wild-type and A562G mutant. No activity of wild-type and mutant with 2-O-alpha-linolenoyl-3-O-beta-D-galactopyranosyl-sn-glycerol, dilinolenoylglycerol, and trilinolenoylglycerol
724736
Zea mays
?
-
-
-
-
phosphorylcholine + O2
activity with the wild-type enzyme, no activity with mutant A562G
724736
Zea mays
?
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Zea mays
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)pLysS
Zea mays
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A562G
the mutation does not affect the relative yield of 13-hydroperoxide, but increases the proportion of (13R)-enantiomer compared to the wild-type enzyme
Zea mays
A562G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
Zea mays
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleate + O2
Zea mays
-
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
?
linoleate + O2
Zea mays
-
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
?
additional information
Zea mays
both the wild type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine, the latter being a poor substrate. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits limited regio- and stereospecificity: the wild-type ZmLOX produces some predominance of (13S)-hydroperoxide. In contrast, the A562G mutant produces some excess of (9S)-hydroperoxide
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
-
724736
Zea mays
?
-
-
-
?
1,2-di-O-alpha-linolenoyl-3-O-beta-D-galactopyranosyl-sn-glycerol + O2
low activity with the wild-type enzyme, no activity with mutant A562G
724736
Zea mays
?
-
-
-
?
2-linoleoyl-sn-glycero-3-phosphorylcholine + O2
low activity of wild-type and A562G mutant. The wild-type enzyme predominantly produces (13S)-hydroperoxide. The A562G mutant form possesses lesser regio- and stereospecificity during the dioxygenation of lysoPC. It produces 28% of (10E,12Z)-9-hydroperoxide and 30% of (9Z,11E)-13-hydroperoxide along with 41% of (all-E)-hydroperoxides. While 9-hydroperoxide is present mainly (61%) as S-enantiomer, (9Z,11E)-13-hydroperoxide is nearly racemic
724736
Zea mays
?
-
-
-
?
2-linoleoyl-sn-glycero-3-phosphorylcholine + O2
the wild-type ZmLOX produces predominantly (13S)-hydroperoxide. In contrast, the A562G mutant produces excessively (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits the limited regio- and stereospecificity. But the A562G mutant form possesses lesser regio- and stereospecificity
724736
Zea mays
?
-
-
-
?
linoleate + O2
-
724736
Zea mays
(9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
-
-
-
?
linoleate + O2
-
724736
Zea mays
(9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
?
linoleate + O2
-
724736
Zea mays
(9S,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate
-
-
-
?
monolinolenoylglycerol + O2
isolated from flax leaves, both the wild-type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The A562G mutation does not affect the relative yield of 13-hydroperoxide, but increases the proportion of (13R)-enantiomer
724736
Zea mays
?
-
-
-
?
monolinolenoylglycerol + O2
wild-type enzyme and mutant A562G predominantly produce (9S)-hydroperoxide
724736
Zea mays
?
-
-
-
?
additional information
both the wild type ZmLOX and A562G mutant dioxygenate monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine, the latter being a poor substrate. Both oxidize the monolinolenoylglycerol predominantly into (9S)-hydroperoxide. The oxidation of 2-linoleoyl-sn-glycero-3-phosphorylcholine exhibits limited regio- and stereospecificity: the wild-type ZmLOX produces some predominance of (13S)-hydroperoxide. In contrast, the A562G mutant produces some excess of (9S)-hydroperoxide
724736
Zea mays
?
-
-
-
-
additional information
Bulky polar heads of glycerolipids cannot penetrate into the LOX active site. Both (9S)- and (13S)-hydroperoxides can be produced when the substrate is arranged within LOX active site in the methyl end first orientation. 1-Linoleoyl-snglycero-3-phosphorylcholine is a poor substrate for both wild-type and A562G mutant. No activity of wild-type and mutant with 2-O-alpha-linolenoyl-3-O-beta-D-galactopyranosyl-sn-glycerol, dilinolenoylglycerol, and trilinolenoylglycerol
724736
Zea mays
?
-
-
-
-
phosphorylcholine + O2
activity with the wild-type enzyme, no activity with mutant A562G
724736
Zea mays
?
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Zea mays
General Information
General Information
Commentary
Organism
additional information
the bulky polar heads of glycerolipids like monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine cannot penetrate into the LOX active site. Thus, both (9S)- and (13S)-hydroperoxides can be produced when substrate is arranged within LOX active site in the methyl end first orientation
Zea mays
General Information (protein specific)
General Information
Commentary
Organism
additional information
the bulky polar heads of glycerolipids like monolinolenoylglycerol and 2-linoleoyl-sn-glycero-3-phosphorylcholine cannot penetrate into the LOX active site. Thus, both (9S)- and (13S)-hydroperoxides can be produced when substrate is arranged within LOX active site in the methyl end first orientation
Zea mays
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
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Secretion of two novel enzymes ...
Nakataea oryzae, Nakataea oryzae CBS 288.54
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2
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725856
Jerneren
Linolenate 9R-dioxygenase and ...
Lasiodiplodia theobromae, Lasiodiplodia theobromae 2334, Lasiodiplodia theobromae CBS 117454, Lasiodiplodia theobromae CBS 122127
Lipids
47
65-73
2012
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17
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1
1
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724736
Chechetkin
Oxidation of glycerolipids by ...
Zea mays
Chem. Phys. Lipids
164
216-220
2011
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12
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1
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1
1
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702431
Palmieri-Thiers
A lipoxygenase with dual posit ...
Olea europaea
Biochim. Biophys. Acta
1791
339-346
2009
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1
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2
2
1
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2
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1
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1
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2
706122
Hornung
Identification of an amino aci ...
Momordica charantia
Phytochemistry
69
2774-2780
2008
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1
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2
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1
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1
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706252
Wang
A novel lipoxygenase gene from ...
Oryza sativa
Plant Mol. Biol.
66
401-414
2008
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1
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1
2
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674388
Cho
Biochemical characterization o ...
Zea mays
J. Biochem. Mol. Biol.
40
100-106
2007
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706289
Veronico
A novel lipoxygenase in pea ro ...
Pisum sativum
Plant Physiol.
141
1045-1055
2006
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1
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1
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703538
Santino
Biochemical and molecular char ...
Corylus avellana
Eur. J. Biochem.
270
4365-4375
2003
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1
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706251
Kim
Dual positional specificity an ...
Zea mays
Plant Mol. Biol.
52
1203-1213
2003
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1
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396190
Hughes
Probing a novel potato lipoxyg ...
Solanum tuberosum
Biochem. J.
353
345-355
2001
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1
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3
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1
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7
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1
1
703535
Hughes
Mutagenesis and modelling of l ...
Pisum sativum
Eur. J. Biochem.
268
1030-1040
2001
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1
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8
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706250
Burow
A peanut seed lipoxygenase res ...
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706645
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Structure of soybean lipoxygen ...
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702394
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Soybean lipoxygenase-1 enzymic ...
Glycine max
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1989
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