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Literature summary for 1.13.11.45 extracted from

  • Wennman, A.; Jerneren, F.; Magnuson, A.; Oliw, E.H.
    Expression and characterization of manganese lipoxygenase of the rice blast fungus reveals prominent sequential lipoxygenation of alpha-linolenic acid (2015), Arch. Biochem. Biophys., 583, 87-95 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene MGG_08499, DNA and amino acid sequence determination and analysis, recombinant expression and secretion of the enzyme in Pichia pastoris Pyricularia oryzae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kineticss Pyricularia oryzae

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ enzyme-bound, is eliminated by denaturation of the enzyme protein Pyricularia oryzae
Fe2+ required, low amount bound to the enzyme Pyricularia oryzae
Mn2+ required, high amount bound to the enzyme, exogenous Mn2+ does not enhance the enzyme activity Pyricularia oryzae

Organism

Organism UniProt Comment Textmining
Pyricularia oryzae G4NAP4
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the deglycosylation process reduces the recombinant enzyme activity, but more than 50% is retained Pyricularia oryzae

Purification (Commentary)

Purification (Comment) Organism
recombinant secreted enzyme 43fold from Pichia pastoris by hydrophobic interaction chromatography and gel filtration Pyricularia oryzae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
2.01
-
purified recombinant enzyme, pH 9.0, 21┬░C Pyricularia oryzae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-dilinoleoyl-phosphatidylcholine + O2 a poor substrate Pyricularia oryzae ?
-
?
1-linoleoyl-2-hydroxy-phosphatidylcholine + O2 an excellent substrate Pyricularia oryzae ?
-
?
linoleate + O2
-
Pyricularia oryzae (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
-
?
lyso-phosphatidylcholine + O2 substrate from soybean Pyricularia oryzae ?
-
?
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 Pyricularia oryzae ?
-
?

Subunits

Subunits Comment Organism
? x * 11000-130000, glycosylated recombinant enzyme, SDS-PAGE, x * 70000, about, deglycosylated recombinant enzyme, SDS-PAGE Pyricularia oryzae

Synonyms

Synonyms Comment Organism
manganese lipoxygenase
-
Pyricularia oryzae
MGG_08499
-
Pyricularia oryzae
MnLOX
-
Pyricularia oryzae
Mo-MnLOX
-
Pyricularia oryzae

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
21
-
assay at Pyricularia oryzae

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
60
-
the deglycosylation process slightly decreases the melting temperature of recombinant Mo-MnLOX from 60┬░C to 56┬░C Pyricularia oryzae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Pyricularia oryzae