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Literature summary for 1.13.11.45 extracted from

  • Wennman, A.; Oliw, E.H.
    Secretion of two novel enzymes, manganese 9S-lipoxygenase and epoxy alcohol synthase, by the rice pathogen Magnaporthe salvinii (2013), J. Lipid Res., 54, 762-775.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in Pichia pastoris Gaeumannomyces graminis

Protein Variants

Protein Variants Comment Organism
F347A site-directed mutagenesis, the mutant oxidizes octadeca-9,11-dienoic acid to 11-hydroperoxyoctadecadienoate/(13R)-hydroperoxyoctadecadienoate/(9S)-hydroperoxyoctadecadienoate in an initial ratio of 50/42/8 and with almost complete consumption of 11-hydroperoxyoctadecadienoate to a ratio of 2/84/14. The (9E,11Z,15E)-octadeca-9,11,15-trienoic acid is transformed to 11- and (13R)-hydroperoxyoctadecatrienoic acid and to traces of (9S)-hydroperoxyoctadecatrienoic acid, essentially as native 13R-MnLOX Gaeumannomyces graminis
F347L site-directed mutagenesis, (9E,11Z,15E)-octadeca-9,11,15-trienoic acid is oxidized to a 2:3 mixture of (9S)- and (13R)-dihydroxyoctadecatrienoic acid Gaeumannomyces graminis
F347V site-directed mutagenesis Gaeumannomyces graminis
additional information replacement Phe347 in 13R-MnLOX and changes the regiospecific oxidation of 18:2 n-6 in a consistent way, but the n-3 double bond of 18:3n-3 can reduce this effect. Mutations are designed to convert the pentamer motif to a hexamer motif to mimic FeLOX, but the mutants with the His-Val-Leu-Phe-Thr-His and His-Val-Leu-Phe-Gly-His motives are inactive, overview Gaeumannomyces graminis

General Stability

General Stability Organism
9S-LOX activity is less robust during expression and purification, possibly due to proteolysis, stability is not improved by addition of 0.001 mM pepstatin A, 0.001 mM leupeptin, or 1 mM EDTA to the growth medium Gaeumannomyces graminis

Metals/Ions

Metals/Ions Comment Organism Structure
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 Gaeumannomyces graminis

Organism

Organism UniProt Comment Textmining
Gaeumannomyces graminis
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Pichia pastoris by hydrophobic interaction chromatography, dialfiltration, and gel filtration Gaeumannomyces graminis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(9Z,12Z)-octadeca-9,12-dienoic acid + O2 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 Gaeumannomyces graminis (9S)-hydroperoxy-octadeca-10,12-dienoate
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?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoic acid + O2 gamma-linoleate is oxidized at C-9, C-11, and C-13 Gaeumannomyces graminis (10E,12E,14E)-9,16-dihydroxy-octadeca-10,12,14-trienoate
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?
additional information cf. EC 1.13.11.58, LC- and GC-MS analysis product analysis, overview Gaeumannomyces graminis ?
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?

Synonyms

Synonyms Comment Organism
13 R -MnLOX
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Gaeumannomyces graminis
manganese lipoxygenase
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Gaeumannomyces graminis

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
22
-
assay at Gaeumannomyces graminis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Gaeumannomyces graminis

General Information

General Information Comment Organism
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 Gaeumannomyces graminis
additional information 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 Gaeumannomyces graminis