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Literature summary for 1.13.11.45 extracted from

  • Wennman, A.; Magnuson, A.; Hamberg, M.; Oliw, E.H.
    Manganese lipoxygenase of F. oxysporum and the structural basis for biosynthesis of distinct 11-hydroperoxy stereoisomers (2015), J. Lipid Res., 56, 1606-1615 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.45

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic tree of two LOX prototypes from different species, recombinant expression and secretion of wild-type and mutant enzymes in Pichia pastoris Fusarium oxysporum

Protein Variants

Protein Variants Comment Organism
L530R site-directed mutagenesis Fusarium oxysporum
additional information replacement of a single amino acid in the active site of LOXs can alter the product profile Fusarium oxysporum
S348F site-directed mutagenesis, the mutant enzyme shows altered reaction stereospecificity compared to the wild-type enzyme Fusarium oxysporum

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ enzyme-bound Colletotrichum gloeosporioides
Cu2+ enzyme-bound, inhibits linoleate oxidation Fusarium oxysporum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Colletotrichum gloeosporioides
additional information
-
 additional information Michaelis-Menten kinetics Fusarium oxysporum
0.0106
-
 (11Z,14Z)-eicosa-11,14-dienoic acid pH 9.0, temperature not specified in the publication, recombinant enzyme Fusarium oxysporum
0.0112
-
 (11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid pH 9.0, temperature not specified in the publication, recombinant enzyme Fusarium oxysporum
0.0122
-
 linolenate pH 9.0, temperature not specified in the publication, recombinant enzyme Fusarium oxysporum

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Fusarium oxysporum
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme-bound Colletotrichum gloeosporioides
Fe2+ enzyme-bound Fusarium oxysporum
Mn2+ enzyme-bound, has catalytic function Colletotrichum gloeosporioides
Mn2+ enzyme-bound, has catalytic function, but does not activate the enzyme exogenously Fusarium oxysporum
additional information determination of metal contents by EPR analysis Colletotrichum gloeosporioides
additional information determination of metal contents by EPR analysis Fusarium oxysporum

Organism

Organism UniProt Comment Textmining
Colletotrichum gloeosporioides
-
-
-
Fusarium oxysporum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant secreted wild-type and mutant enzymes from Pichia pastoris by hydrophobic interaction chromatography, ultrafiltration, and gel filtration Fusarium oxysporum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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 Fusarium oxysporum ?
-
 ?
(11Z,14Z,17Z)-eicosa-11,14,17-trienoic acid + O2
-
 Fusarium oxysporum ?
-
 ?
1-linoleoyl-2-lyso-phosphatidylcholine + O2
-
 Fusarium oxysporum ?
-
 ?
linolenate + O2
-
 Colletotrichum gloeosporioides (11S)-hydroperoxyoctadecadienoic acid + (13R)-hydroperoxyoctadecadienoic acid + (9S)-hydroperoxyoctadecadienoic acid
-
 ?
linolenate + O2 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 Fusarium oxysporum (11R)-hydroperoxyoctadecadienoic acid + 13S-hydroperoxyoctadecadienoic acid + 9(S/R)-hydroperoxyoctadecadienoic acid
-
 ?
lyso-phosphatidylcholine + O2 substrate from soybean Colletotrichum gloeosporioides ?
-
 ?
lyso-phosphatidylcholine + O2 substrate from soybean Fusarium oxysporum ?
-
 ?
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 Fusarium oxysporum ?
-
 ?
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 Colletotrichum gloeosporioides ?
-
 ?

Synonyms

Synonyms Comment Organism
Cg-MnLOX
-
 Colletotrichum gloeosporioides
Fo-MnLOX
-
 Fusarium oxysporum
manganese lipoxygenase
-
 Colletotrichum gloeosporioides
manganese lipoxygenase
-
 Fusarium oxysporum
manganese LOX
-
 Colletotrichum gloeosporioides
manganese LOX
-
 Fusarium oxysporum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0122
-
 linolenate pH 9.0, temperature not specified in the publication, recombinant enzyme Fusarium oxysporum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
 assay at Fusarium oxysporum

General Information

General Information Comment Organism
evolution the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX Fusarium oxysporum
additional information structure-function analysis Colletotrichum gloeosporioides
additional information structure-function analysis Fusarium oxysporum