EC Number |
General Information |
Reference |
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1.13.11.45 | 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 |
725658 |
1.13.11.45 | 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 |
725486 |
1.13.11.45 | evolution |
the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX |
743055 |
1.13.11.45 | more |
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 |
725658 |
1.13.11.45 | more |
pentamer motif His-Val-Leu-Phe-His in MnLOX, 13R-MnLOX3 catalyzes suprafacial hydrogen abstraction and oxygenation |
725486 |
1.13.11.45 | more |
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 |
743826 |
1.13.11.45 | more |
structure-function analysis |
743055 |