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Information on EC 1.13.11.45 - linoleate 11-lipoxygenase
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1.13.11.45 linoleate 11-lipoxygenaseIUBMB Comments
The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn2+. It also acts on alpha-linolenate, whereas gamma-linolenate is a poor substrate. Oleate and arachidonate are not substrates.
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Word Map
- 1.13.11.45
- oxylipins
- graminis
-
bis-allylic
-
gaeumannomyces
-
suprafacial
-
take-all
-
antarafacial
-
atlox2
-
lipoxygenation
-
hydroperoxy
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
lipoxygenase 2, manganese lipoxygenase, mn-lo, mnlox, csplox2, 13r-mnlox, mo-mnlox, fo-mnlox, mn-lox, cg-mnlox, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
linoleate dioxygenase
-
-
-
-
manganese lipoxygenase
manganese LOX
Mn-LO
manganese lipoxygenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
mechanism via suprafacial migration of O2
-
linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
reaction mechanism, tail-first model with rearrangement at C13 at the end of lipoxygenation, influenced by double bond configuration and the chain length of fatty acids, overview
-
linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
the LOX reaction is always catalyzed at a 1Z,4Z-pentadiene system of a polyunsaturated fatty acid. In the initial step, a hydrogen atom is abstracted from the central bis-allylic methylene group by the non-heme iron or in few cases manganese in the active site. During this rate-limiting step, Fe(III) is reduced to Fe(II) in the former case and a substrate radical is formed which rapidly delocalizes over the five carbon unit. Addition of dioxygen yields a peroxyl radical, which is finally reduced to the hydroperoxide product
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
oxidation
possesses also 1% of hydroperoxide isomerase activity
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
linoleate:oxygen 11S-oxidoreductase
The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn2+. It also acts on alpha-linolenate, whereas gamma-linolenate is a poor substrate. Oleate and arachidonate are not substrates.
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CAS REGISTRY NUMBER
COMMENTARY
9029-60-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(10Z,13Z,16Z)-nonadeca-10,13,16-trienoic acid + O2
?
-
oxidation at the n-6 carbon and at the bis-allylic position n-8
-
-
?
(11Z,14Z)-eicosa-11,14-dienoic acid + O2
?
-
LC-MS analysis shows that Fo-MnLOX oxidizes (11Z,14Z)-eicosa-11,14-dienoic acid efficiently at both C-15 and C-11
-
-
?
(11Z,14Z)-eicosadienoic acid + O2
15-hydroxyperoxy-(9Z,11E)-eicosadienoic acid
-
-
-
-
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
15-hydroxyperoxy-11Z,13E,17Z-eicosatrienoic acid
-
via 11-hydroperoxyoctadecadienoic acid, 13-hydroperoxyoctadecadienoic acid and 15-hydroperoxyoctadecadienoic acid
-
-
?
(13R)-hydroperoxylinolenic acid + O2
13-ketolinolenic acid + epoxyalcohols
only mutant enzyme G316A
erythro- and threo-11-hydroxy-(12R,13R)-epoxy-(9Z,15Z)-octadecadienoic acids and one of the corresponding cis-epoxides as major products
-
?
(5E,8E,11E,14E)-icosa-5,8,11,14-tetraenoic acid + O2
(5Z,8Z,11S,12E,14Z)-11-hydroperoxyicosa-5,8,12,14-tetraenoic acid + (5Z,8Z,11Z,13E,15R)-15-hydroperoxyicosa-5,8,11,13-tetraenoic acid
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oxidation at the n-6 carbon and at the bis-allylic position n-8
-
-
?
(5Z,8Z,11Z,14Z,17Z)-docosa-5,8,11,14,17-pentaenoate + O2
?
-
oxidation at the n-6 carbon and at the bis-allylic position n-8
-
-
?
(7Z,10Z,13Z,16Z,19Z)-docosa-7,10,13,16,19-pentaenoate + O2
?
-
oxidation at the n-6 carbon and at the bis-allylic position n-8
-
-
?
(9E,12Z)-octadeca-9,12-dienoic acid + O2
?
-
sLOX-1 oxidizes (9E,12Z)18:2 to 9-hydroperoxyoctadecadienoic acid in an R/S ratio of 60/40 and to 13-hydroperoxyoctadecadienoic acid
-
-
?
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate + O2
(9Z,11E, 13R)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate + O2
(9Z,11E,13R)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
(9Z,12E)-octadeca-9,12-dienoic acid + O2
?
-
sLOX-1 oxidizes (9Z,12E)18:2 slowly to the 9-hydroperoxy metabolite with 10E,12E configuration as the main product (65%) and to 13-hydroperoxyoctadecadienoic acid
-
-
?
(9Z,12Z)-octadeca-9,12-dienoic acid + O2
(9S)-hydroperoxy-octadeca-10,12-dienoate
-
alpha-linoleate is converted via two intermediates, (11S)-hydroperoxy-(9Z,12Z)-octadecenoate and (13R)-hydroperoxy-(9Z,11E)-octadecadienoate, which are isomerized to the end product, probably after oxidation to peroxyl radicals, beta-fragmentation, and oxygen insertion at C-9
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(10E,12E,14E)-9,16-dihydroxy-octadeca-10,12,14-trienoate
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gamma-linoleate is oxidized at C-9, C-11, and C-13
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-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
(13R)-hydroperoxyoctadecadienoic acid
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via bis-allylic 11S-hydroperoxy fatty acid
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-
?
1,2-dilinoleoyl-sn-glycero-3-phosphocholine + O2
?
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main products with 14% and 10%, no production of 11-hydroxyoctadecanoic acid
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?
1-linoleoyl-2-hydroxy-phosphatidylcholine + O2
?
an excellent substrate
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-
?
1-linoleyl-lyso-glycerophosphatidylcholine + O2
11-hydroxyoctadecanoic acid + 13-hydroxyoctadecanoic acid
-
via formation of the 13-hydroxyperoxy metabolite
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-
?
11-(11R)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
9-(9R)-hydroperoxy-octadecadienoic acid
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slow
-
-
?
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid methyl ester
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid methyl ester
-
-
-
-
?
11-hydroperoxyoctadecadienoic acid + O2
11,18-dihydroxy-12E,14Z,16E-eicosatrienoic acid
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-
two diastereoisomers
-
?
alpha-linolenic acid + O2
(13R)-hydroperoxy octadecadienoic acid + 9-hydroperoxyoctadecadienoic acid
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-
-
-
?
alpha-linolenic acid + O2
(9Z,11E,15Z)-(13)-hydroperoxyoctadecatrienoic acid
-
-
-
-
?
gamma-linolenic acid + O2
(6Z,9Z,11E)-(13)-hydroperoxyoctadecatrienoic acid + (6Z,9Z,12Z)-(11)-hydroperoxyoctadecatrienoic acid
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-
-
-
?
linoleate + O2
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid + (9Z,12Z)-(11S)-hydroperoxyoctadecadienoic acid
-
-
-
ir
linolenate + O2
(11R)-hydroperoxyoctadecadienoic acid + 13S-hydroperoxyoctadecadienoic acid + 9(S/R)-hydroperoxyoctadecadienoic acid
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Fo-MnLOX, with support of Ser348, binds linoleic acid so that the pro R rather than the pro S hydrogen at C-11 interacts with the metal center, but retains the suprafacial oxygenation mechanism observed in other MnLOXs
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-
?
linolenate + O2
(11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid
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-
-
-
?
linolenic acid + O2
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
-
-
-
-
?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
?
-
oxidation at the n-6 carbon and at the bis-allylic position n-8
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
?
-
oxidation at the bis-allylic n-5 carbon and at positions n-3, n-7, and n-6
-
-
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2
?
-
oxidation at the n-3 position
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-
?
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid
-
47% the rate of conversion of linolenic acid
-
-
?
11-(11S)-hydroperoxy-(9Z,12Z)-octadecadienoic acid
13-(13R)-hydroperoxy-(9Z,11E)-octadecadienoic acid
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rapid
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-
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
via bis-allylic 11S-hydroperoxy fatty acid
-
-
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
analysis of substrate conformation and environment, overview
-
-
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
-
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
-
-
-
?
linoleic acid + O2
(9Z,11E)-(13R)-hydroperoxyoctadecadienoic acid
-
-
-
-
?
lyso-phosphatidylcholine + O2
?
-
substrate from soybean
-
-
?
additional information
?
-
-
the 11-hydroperoxide does not undergo the rapid beta-fragmentation observed with 13R-MnLOX. Oxidation of [11S-2H]-linoleic acid by Cg-MnLOX is accompanied by loss of deuterium and a large kinetic isotope effect. Substrate specificity, overview
-
-
?
additional information
?
-
-
the 11-hydroperoxide does not undergo the rapid beta-fragmentation observed with 13R-MnLOX. No significant oxidation of (7Z,10Z,13Z)-hexadeca-7,10,13-trienoic acid, (6Z,9Z,12Z)-octadeca-6,9,12-trienoic acid, and arachidonic acid. The alpha-linolenic acid, which forms 11R-hydro(pero)xy-9Z,12Z,15Z-octadecatrienoic acid as a main metabolite, is oxidized to 9- and 13R-hydro(pero)xy-9Z,11E,15Z-octadecatrienoic acid at a much lower rate compared with linoleic acid, (11Z,14Z)-eicosa-11,14-dienoic acid, and (11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid. Substrate specificity, overview
-
-
?
additional information
?
-
-
Mn-LO likely binds fatty acids tail-first and oxygenates many C16, C18, C20, and C22 fatty acids to significant amounts of bis-allylic hydroperoxides. Unsaturated C16-C22 fatty acids, other than 18:3n-3, 18:2n-6, or 17:3n-3, are poor substrates, possibly because of ineffective enzyme activation through Mn2+ to Mn3+ by the produced hydroperoxides, substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the rearrangement of bis-allylic S-hydroxyperoxides to allylic R-hydroperoxides, and the oxygenation of 18:2n-6 by suprafacial hydrogen abstraction at C11 and O2 insertion at the bis-allylic position C11 and, with double bond migation, at the allylic position C13, overview, 20:4n-6 is a poor substrate, substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
13R-MnLOX forms (11S)-hydroperoxyoctadecadienoic acid and (11R)-hydroperoxyoctadecatrienoic acid as intermediates during the linear phase of oxidation and the (13R)-hydroperoxides as main end products
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-
?
additional information
?
-
-
cf. EC 1.13.11.58, LC- and GC-MS analysis product analysis, overview
-
-
?
additional information
?
-
-
oxidation of 18:1 n-6 is performed by 13R-MnLOX
-
-
?
additional information
?
-
-
(9Z,12E)18:2 is not oxidized at a detectable rate. sLOX-1 oxidizes (9E,12Z)18:2 more efficiently than (9Z,12E)18:2
-
-
?
additional information
?
-
the enzyme can also convert linoleate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate, cf. linoleate 9S-lipoxygenase/EC 1.13.11.58 and linoleate 13R-lipoxygenase. Oxygen consumption monitoring
-
-
?
additional information
?
-
-
the enzyme can also convert linoleate to (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate and (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate, cf. linoleate 9S-lipoxygenase/EC 1.13.11.58 and linoleate 13R-lipoxygenase. Oxygen consumption monitoring
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate + O2
(9Z,11E, 13R)-13-hydroperoxyoctadeca-9,11-dienoate
-
-
-
-
?
linoleate + O2
(9Z,11S,12Z)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
-
?
linoleate + O2
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
-
-
?
additional information
?
-
-
13R-MnLOX forms (11S)-hydroperoxyoctadecadienoic acid and (11R)-hydroperoxyoctadecatrienoic acid as intermediates during the linear phase of oxidation and the (13R)-hydroperoxides as main end products
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iron cofactor
coordination of the iron cofactor, overview
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
enzyme-bound, is eliminated by denaturation of the enzyme protein
Fe2+
Fe3+
non-heme iron, required. The catalytic non-heme iron, deeply buried in the CspLOX2 active site, is coordinated by three invariant histidines (His257, His262, His449), Asn453 and the carboxy group of the C-terminal Ile569. The sixth ligand of the octahedrally coordinated iron, which is positioned towards the putative substrate binding channel, is a water (Fe2+-H2O) or hydroxide molecule (Fe3+-OH) acting as a catalytic base for hydrogen abstraction during catalysis, coordination of the iron cofactor, overview
Mn2+
additional information
Mn2+
-
enzyme-bound, has catalytic function, but does not activate the enzyme exogenously
Mn2+
-
manganese 13R-lipoxygenase contains catalytic manganese, the catalytic domain of 13R-MnLOX contains a pentamer motif flanked by two His metal ligands, His-Val-Leu-Phe-His, in the presumed manganese binding region
Mn2+
required, high amount bound to the enzyme, exogenous Mn2+ does not enhance the enzyme activity
additional information
-
determination of metal contents by EPR analysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-(3-phenoxycinnamyl) acetohydroxamic acid
0.3 mM, complete inhibition
N-(3-phenoxycinnamyl)acetohydroxamic acid
-
50% of control activity at 0.05 mM
Tween 20
-
inhibition of Ca2+-activated enzyme at pH 7.5 and 6.4, no inhibition at pH 6.4 in the absence of Ca2+
additional information
-
no inhibition by lipoxygenase inhibitors zileuton, esculetin and ICI 230487
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Manganese lipoxygenase oxidizes bis-allylic hydroperoxides and octadecenoic acids by different mechanisms.
Infections
Ecological adaptations influence the susceptibility of plants in the genus Zantedeschia to soft rot Pectobacterium spp.
Infections
Magnaporthe oryzae defeats rice defense by inducing miR319b and suppressing Jasmonic acid signaling.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0106
(11Z,14Z)-eicosa-11,14-dienoic acid
-
pH 9.0, temperature not specified in the publication, recombinant enzyme
0.0112
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid
-
pH 9.0, temperature not specified in the publication, recombinant enzyme
0.0122
linolenate
-
pH 9.0, temperature not specified in the publication, recombinant enzyme
0.0005
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
-
pH 9.0, temperature not specified in the publication, wild-type enzyme
0.0027
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
-
pH 9.0, temperature not specified in the publication, mutant L336V
0.0036
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
-
pH 9.0, temperature not specified in the publication, mutants L336A and L336F
0.0065
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
-
pH 9.0, temperature not specified in the publication, mutant L336V
0.0073
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid
-
pH 9.0, temperature not specified in the publication, mutant F337I
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kineticss
-
additional information
additional information
-
Michaelis-Menten kineticss
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0122
linolenate
-
pH 9.0, temperature not specified in the publication, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 11
-
at pH 5.0 64% of maximum activity, at pH 11 69% of maximum activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12 - 60
-
8.8% of maximal activity at 12°C and 100% of maximal activity at 60°C, activity decreases sharply at 63°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
additional information
evolution
-
9S-LOX contains catalytic manganese, and its sequence can be aligned with 77% identity to 13R-LOX with catalytic manganese lipoxygenase of the Take-all fungus. Alterations in the Sloane determinant of 9S-LOX and 13R-MnLOX with larger and smaller hydrophobic residues interconvert the regiospecific oxidation of 18:2n-6, presumably by altering the substrate position in relation to oxygen insertion
evolution
-
overview of possible lipoxygenation positions of linoleic acid and partial alignment of 13R-MnLOX, sLOX-1, 8R-LOX, human 5-LOX, and rabbit 15-LOX covering an important region for regio- and stereospecificity. A few LOXs, including 9S-MnLOX, deviate from this rule of R/S stereospecificity
evolution
-
the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX
additional information
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alterations in the Sloane determinant of 9S-LOX and 13R-MnLOX with larger and smaller hydrophobic residues interconvert the regiospecific oxidation of 18:2n-6, presumably by altering the substrate position in relation to oxygen insertion. The catalytic domain of 13R-MnLOX contains a pentamer motif flanked by two His metal ligands, His-Val-Leu-Phe-His, in the presumed manganese binding region. 9S-MnLOX, EC 1.13.11.58, catalyzes hydrogen abstraction at C-11 and oxygenation at C-9 and C-11 in a suprafacial manner in analogy with 13R-MnLOX
additional information
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pentamer motif His-Val-Leu-Phe-His in MnLOX, 13R-MnLOX3 catalyzes suprafacial hydrogen abstraction and oxygenation
additional information
residues around the active site direct dioxygen to a preferred carbon atom and stereo configuration in the substrate fatty acid. An active site clamp fixing the pentadiene system of the substrate together with steric shielding controls the stereo- and regiospecific positioning of dioxygen at all positions of the reacting pentadiene system of substrate fatty acids. The restricted space in the kink region is required for effective 11-HPODE formation by CspLOX2, as a tight and kinked substrate-binding channel might induce slight distorsions in the reacting pentadiene system, thus altering the reactivity, structure-activity analysis, modeling, overview. Crucial residues in the direct environment of the narrow active site that form a clamp-like structure include Leu304, Leu258, Ile296, Ala300, Leu502 and Leu506. Molecular dynamics simulations support a major role of steric shielding of active site clamp
Show AA Sequence and Transmembrane Helices (343 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 11000-130000, glycosylated recombinant enzyme, SDS-PAGE, x * 70000, about, deglycosylated recombinant enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
the deglycosylation process reduces the recombinant enzyme activity, but more than 50% is retained
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme CspLOX2, sitting drop vapor diffusion method, from well solution of 10% PEG 4000, 0.1 M MES/imidazole pH 6.5, 20% glycerol and 0.02% alcohols (1,6-hexanediol, 1-butanol, 1,2-propanediol, 2-propanol, 1,4-butanediol, and 1,3-propanediol), 10 days, purified recombinant CspLOX2 mutant enzymes by hanging drop vapour diffusion method, from well solution of 12.5-15 PEG 4000, 8-12% glycerol, 0.1 M MES/imidazole pH 6.1, and 0-600 mM NaCl, X-ray diffraction structure determination and analysis at 1.8 A resolution. Crystals of a CspLOX2 substrate complex are not obtained
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S348F
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site-directed mutagenesis, the mutant enzyme shows altered reaction stereospecificity compared to the wild-type enzyme
F337I
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site-directed mutagenesis, replacement of Phe337 with Ile changes the stereochemistry of the 13-hydroperoxy metabolites of 18:2n-6 and 18:3n-3 (from 100% R to 69-74% S) with little effect on regiospecificity. The abstraction of the pro-S hydrogen of 18:2n-6 is retained, suggesting antarafacial hydrogen abstraction and oxygenation. The mutant shows highly reduced activity compared to the wild-type enzyme