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Results 1 - 10 of 12 > >>
EC Number Cofactor Commentary Reference
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme - 439739, 439747, 439751, 439752, 439754, 671338, 672519, 674928, 688396, 695576, 695687, 696298, 696482, 696500, 696779, 697530, 698044, 698048, 698420, 698897, 698919, 699011, 699269, 700707, 701107, 710744, 711160, 711361, 711550, 712224, 712226, 712714, 713470, 713517, 724110, 724400, 724412, 725055, 725088, 725143, 725507, 726432
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme 1.3 mol heme per molecule, protoheme 439741
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme contains 2 mol of heme per mol of the enzyme. Iron of heme is in Fe-III state 676949
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme enzyme contains a high-spin heme. The FeIII/FeII reduction potential is -266 mV vs normal hydrogen electrode. The gamma-heme edge shows a substrate binding site 742917
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme holo-form binds two c-type hemes covalently bound to the polypeptide chain, a high-potential E heme and a low-potential P heme, with redox potentials of (+310 mV) and (-190 mV/-300 mV), respectively in the presence of calcium ions, at pH 7.5. A calcium dependent reductive activation mechanism is present, in which P heme is bis-His coordinated low-spin in the fully oxidized state of the enzyme, and becomes penta-coordinated high-spin upon reduction of E heme in the presence of calcium ions. The rate-limiting step in the catalytic cycle is the electron transfer between the two hemes 743044
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme iron protoporphyrin-containing heme peroxidase 695785
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme isozyme VPO1 has a heme content of 1.64 nmol/mg protein 698048
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme loss of a structural restraint in the proximal heme pocket of mutant enzyme T171S allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein 673533
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme protoheme IX 439741, 439762
Show all pathways known for 1.11.1.7Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.7heme spectra are typical of high valent heme iron intermediate states generated in the catalytic cycle of a peroxidase 742340
Results 1 - 10 of 12 > >>