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Results 1 - 7 of 7
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.45evolution 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
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.45evolution 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
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.45evolution the predicted active site of all Mn-LOXs contains Phe except for Ser 348 in this position of Fo-MnLOX 743055
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.45more 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
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.45more pentamer motif His-Val-Leu-Phe-His in MnLOX, 13R-MnLOX3 catalyzes suprafacial hydrogen abstraction and oxygenation 725486
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.45more 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
Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.45more structure-function analysis 743055
Results 1 - 7 of 7