1.13.11.34 1-oleoyl-2-acetyl-sn-glycerol both Ca2+ and glyceride, e.g. 1-oleoyl-2-acetyl-sn-glycerol, might decrease the concentration of lipid hydroperoxide needed for activation of 5-LO, enabling cellular 5-LO product formation at a low redox tone 690170 1.13.11.34 Ba2+ 45% of the activation with Ca2+ 439461 1.13.11.34 Ca2+ - 684399, 688512, 689841 1.13.11.34 Ca2+ 0.1 mM 676811 1.13.11.34 Ca2+ 5-lipoxygenase product formation in arachidonic acid-stimulated polymorphonuclear leukocytes is independent of Ca2+ 659654 1.13.11.34 Ca2+ 5-lipoxygenase product formation in arachidonic acid-stimulated polymorphonuclear leukocytes is independent of Ca2+. Ca2+ and 5-lipoxygenase phosphorylation seem to be required for arachidonic acid-induced 5-lipoxygenase product formation 659654 1.13.11.34 Ca2+ 5-LOX is recruited to the nuclear membrane upon cellular Ca2+ influx. Calcium binds to allosteric sites in the 5-LOX N-terminal polycystin-1/lipoxygenase/alpha-toxin (PLAT) domain, promoting attachment to the membrane via conserved tryptophan residues that embed into the lipid bilayer 741898 1.13.11.34 Ca2+ above 0.1 mM, required for maximal activity 439438 1.13.11.34 Ca2+ activates 684672, 704997, 711134 1.13.11.34 Ca2+ activates, Ca2+ induces the translocation of 5-LO from a soluble compartment to nuclear structures, where 5-LO co-localizes with 5-LO activating protein, FLAP 689872 1.13.11.34 Ca2+ addition of Ca2+ increases catalytic activity of wild-type nzyme by 50% 726804 1.13.11.34 Ca2+ allosteric modulator involved in membrane binding by the enzyme 741961 1.13.11.34 Ca2+ binds at the C2-like domain, stimulates and induces enzyme translocation from the nuclear soluble to the envelope fraction, both Ca2+ and glyceride might decrease the concentration of lipid hydroperoxide needed for activation of 5-LO, enabling cellular 5-LO product formation at a low redox tone 690170 1.13.11.34 Ca2+ Ca2+ is required for 5LO activity, the enzyme contains two Ca2+, full activation is reached at 0.004-0.01 mM Ca2+ 711100 1.13.11.34 Ca2+ Ca2+ stimulates enzyme activity 712666 1.13.11.34 Ca2+ half-maximal activation around 0.03 mM 439457 1.13.11.34 Ca2+ half-maximal activity at 0.02 mM 439466 1.13.11.34 Ca2+ half-maximal activity at 0.1 mM 439461 1.13.11.34 Ca2+ optimal concentration is 2 mM 439451 1.13.11.34 Ca2+ phosphocholine in combination with Ca2+ markedly stimulate the formation of leukotrienes by wild-type 5-LO and C159S/C300S/C416S/C418S mutant, whereas their effect on the 5-LO 3W mutant is small 741975 1.13.11.34 Ca2+ required 439449, 439456, 439458, 439459, 439461, 439466, 742210, 742444 1.13.11.34 Ca2+ stimulates 439441, 439442, 439443, 439448, 439453, 439479 1.13.11.34 Ca2+ stimulation with calcium ionophore 705037 1.13.11.34 Ca2+ the enzyme is activated by a Ca2+-mediated translocation to membranes 658043 1.13.11.34 Ca2+ upon stimulation with calcium ionophore, GFP-5-lipoxygenase translocates to the nuclear envelope allowing it to interact with 5-lipoxygenase activating protein (FLAP) and leukotriene C4 synthase 702043 1.13.11.34 Ca2+ whilst the catalytic domain of wild-type 5-LO is destabilized by calcium, addition of calcium has no influence on the catalytic domain of 5-LODELTA4 743614 1.13.11.34 Fe required for catalysis, oxidizes Fe2+ to Fe3+ 742078 1.13.11.34 Fe the iron acts as electron acceptor and donor, during hydrogen abstraction and peroxide formation 711100 1.13.11.34 Fe2+ - 704997 1.13.11.34 Fe2+ a non-heme iron dioxygenase 741918 1.13.11.34 Fe2+ a non-heme iron that is required for catalytic activity 743614 1.13.11.34 Fe2+ a non-heme iron-containing enzyme. LOX catalytic activity depends on the presence of iron in the active site. Iron removal is able to affect the membrane binding properties of the enzyme, molecular dynamics simulations, overview 742135 1.13.11.34 Fe2+ a nonheme Fe2+ ion coordinated by three polar histidines H372, H550, and H367, the carbonyl group of N554, the carboxylic group of the C-terminal I673, and a water moleculein the active site, overview. On interaction with the active site, the ligands replaces the H2O molecule 741871 1.13.11.34 Fe2+ Asn720 is present in the fifth coordination position of iron 704832 1.13.11.34 Fe2+ ferrous form of LO-1 706001 1.13.11.34 Fe2+ isoflavones reduce active state iron to ferrous state and prevent the activation of the resting enzyme 684672 1.13.11.34 Fe2+ requied for activity 741898 1.13.11.34 Fe2+ required 742210, 742444 1.13.11.34 Fe2+ required, iron reduction from Fe3+ to Fe2+ during catalyis 741862 1.13.11.34 Fe3+ because catalysis by 5-LO requires oxidation of Fe2+ to the active Fe3+ state by lipid hydroperoxides, the redox tone is an important parameter of cellular 5-LO activity 690170 1.13.11.34 Iron contains one iron atom per molecule, the native enzyme is in a pseudo-axial high-spin ferric state 439454 1.13.11.34 Iron wild-type enzyme contains 0.65 mol of iron per mol of enzyme, H372 and H550 constitute two of the iron ligands 439478 1.13.11.34 Mg2+ - 689841 1.13.11.34 Mg2+ 5 mM activates 5LO in vitro in the presence of PC 676811 1.13.11.34 Mg2+ activates 704997