1.13.11.45: linoleate 11-lipoxygenase
This is an abbreviated version!
For detailed information about linoleate 11-lipoxygenase, go to the full flat file.
Word Map on EC 1.13.11.45
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1.13.11.45
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oxylipins
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graminis
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bis-allylic
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gaeumannomyces
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suprafacial
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take-all
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antarafacial
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atlox2
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lipoxygenation
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hydroperoxy
- 1.13.11.45
- oxylipins
- graminis
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bis-allylic
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gaeumannomyces
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suprafacial
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take-all
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antarafacial
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atlox2
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lipoxygenation
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hydroperoxy
Reaction
Synonyms
13 R -MnLOX, 13R-MnLOX, Cg-MnLOX, CspLOX2, Fo-MnLOX, linoleate dioxygenase, lipoxygenase 2, LOX-1, manganese lipoxygenase, manganese LOX, MGG_08499, Mn-LO, Mn-LOX, MnLOX, Mo-MnLOX
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General Information
General Information on EC 1.13.11.45 - linoleate 11-lipoxygenase
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evolution
additional information
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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
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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
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the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX
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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