Knowledge (XXG)

Haloperoxidase

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1059: 418:
Vaillancourt, Frédéric H.; Yeh, Ellen; Vosburg, David A.; Garneau-Tsodikova, Sylvie; Walsh, Christopher T. (2006). "Nature's Inventory of Halogenation Catalysts: Oxidative Strategies Predominate".
69:) is generally favorable process. It is practiced industrially on a large scale for example. In nature, however, free halogens do not exist in appreciable amounts. The combination of 92:. The oxidation of these anions by hydrogen peroxide is slow in the absence of enzymes. These enzymes are called haloperoxidases. The reaction that they catalyze is: 551: 401:
S.L. Neidleman, J. Geigert (1986) Biohalogenation - principles, basic roles and applications; Ellis Horwood Ltd Publishers; Chichester;
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Eosinophils preferentially use bromide to generate halogenating agents - Mayeno et al. 264 (10): 5660 - Journal of Biological Chemistry
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The table shows the classification of haloperoxidases according to the halides whose oxidation they are able to catalyze.
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dye. The enzyme is very specific to bromide and physically stable, but has not been characterized as to its active site.
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is also capable of oxidizing these substrates, but its heme is not covalently bound and becomes damaged during turnover.
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The classification of these enzymes by substrate-usability does not necessarily indicate enzyme substrate
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perspective under natural conditions, i.e., a temperature range of about 0–30 °C and a
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in marine organisms (fungi, bacteria, microalgae, perhaps other eukaryotes) uses
1030: 965: 801: 628: 352: 192: 23: 1058: 685: 564: 320: 276: 266: 208: 1004: 978: 500: 204: 200: 143: 27: 519: 484:"Exploring the chemistry and biology of vanadium-dependent haloperoxidases" 439: 600: 223: 147: 119: 362: 123: 31: 431: 1017: 787: 306: 127: 991: 745: 740: 735: 730: 334: 310: 229: 139: 38:. Both halides and hydrogen peroxide are widely available in the 658: 653: 648: 643: 638: 633: 623: 302: 196: 760: 533: 73:, which is widely produced by aerobic life, and halide anions 472:
Role of Heme-Protein Covalent Bonds in Mammalian Peroxidases
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and hydrogen peroxide to brominate electrophilic organics.
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prosthetic group covalently bound by two ester linkages to
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to oxidize chloride, it preferentially oxidizes bromide.
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side-chains. MPO has a third covalent link through a
150:(E°= 2.87 V) cannot be oxidized by hydrogen peroxide. 1047: 50:
Halogenations of organic compounds by free halogens (
943: 907: 876: 845: 794: 706: 576: 242: 772: 545: 337:snail bromoperoxidase (does not use I or Cl) 8: 118:confirms that hydrogen peroxide can oxidize 114:From the perspective of thermodynamics, the 46:Mechanistic and thermodynamic considerations 779: 765: 757: 552: 538: 530: 509: 499: 188:(EPO) are also capable of oxidizing the 106: 102: 98: 88: 84: 80: 65: 61: 57: 53: 1054: 394: 7: 332:,(marine algae, other marine spp.?), 482:Winter, JM; Moore, BS (July 2009). 14: 1057: 176:The mammalian haloperoxidases 1: 26:that are able to mediate the 195:(SCN). They each contain a 105:+ H + R−H → X + 2 H 77:provides the equivalent of 1096: 935:Michaelis–Menten kinetics 283:, can use Cl, prefers Br) 827:Diffusion-limited enzyme 691:Iodothyronine deiodinase 383:Vanadium bromoperoxidase 330:vanadium bromoperoxidase 220:vanadium bromoperoxidase 142:soil layer) to about 8 ( 696:Iodotyrosine deiodinase 606:Cytochrome c peroxidase 501:10.1074/jbc.R109.001602 666:Horseradish peroxidase 616:Glutathione peroxidase 357:horseradish peroxidase 213:Horseradish peroxidase 165:For example, although 138:ranging from about 3 ( 920:Eadie–Hofstee diagram 853:Allosteric regulation 611:Eosinophil peroxidase 596:Fatty-acid peroxidase 281:eosinophil peroxidase 186:eosinophil peroxidase 167:eosinophil peroxidase 130:(E°= 0.536 V) from a 930:Lineweaver–Burk plot 286:Caldariomyces fumago 889:Enzyme superfamily 822:Enzyme promiscuity 681:Thyroid peroxidase 457:2009-05-26 at the 367:thyroid peroxidase 249:Oxidisable halide 126:(E°= 1.09 V), and 1045: 1044: 754: 753: 432:10.1021/cr050313i 374: 373: 71:hydrogen peroxide 64:, and sometimes I 36:hydrogen peroxide 1087: 1062: 1061: 1053: 925:Hanes–Woolf plot 868:Enzyme activator 863:Enzyme inhibitor 837:Enzyme catalysis 781: 774: 767: 758: 591:NADPH peroxidase 554: 547: 540: 531: 524: 523: 513: 503: 494:(28): 18577–81. 479: 473: 468: 462: 450: 444: 443: 426:(8): 3364–3378. 420:Chemical Reviews 415: 409: 399: 258:Chloroperoxidase 243: 236:used to produce 110: 91: 76: 68: 16:Class of enzymes 1095: 1094: 1090: 1089: 1088: 1086: 1085: 1084: 1070: 1069: 1068: 1056: 1048: 1046: 1041: 953:Oxidoreductases 939: 915:Enzyme kinetics 903: 899:List of enzymes 872: 841: 812:Catalytic triad 790: 785: 755: 750: 702: 676:Myeloperoxidase 671:Lactoperoxidase 586:NADH peroxidase 572: 561:Oxidoreductases 558: 528: 527: 481: 480: 476: 469: 465: 459:Wayback Machine 451: 447: 417: 416: 412: 400: 396: 391: 379: 360: 333: 328: 318: 315:lactoperoxidase 294:Bromoperoxidase 284: 274: 271:myeloperoxidase 246:Haloperoxidase 234:bromoperoxidase 182:lactoperoxidase 178:myeloperoxidase 156: 116:Nernst equation 108: 104: 100: 96: 90: 86: 82: 78: 74: 67: 63: 59: 55: 51: 48: 20:Haloperoxidases 17: 12: 11: 5: 1093: 1091: 1083: 1082: 1072: 1071: 1067: 1066: 1043: 1042: 1040: 1039: 1026: 1013: 1000: 987: 974: 961: 947: 945: 941: 940: 938: 937: 932: 927: 922: 917: 911: 909: 905: 904: 902: 901: 896: 891: 886: 880: 878: 877:Classification 874: 873: 871: 870: 865: 860: 855: 849: 847: 843: 842: 840: 839: 834: 829: 824: 819: 814: 809: 804: 798: 796: 792: 791: 786: 784: 783: 776: 769: 761: 752: 751: 749: 748: 743: 738: 733: 728: 723: 717: 715: 704: 703: 701: 700: 699: 698: 693: 683: 678: 673: 668: 663: 662: 661: 656: 651: 646: 641: 636: 631: 626: 613: 608: 603: 598: 593: 588: 582: 580: 574: 573: 559: 557: 556: 549: 542: 534: 526: 525: 474: 463: 445: 410: 393: 392: 390: 387: 386: 385: 378: 375: 372: 371: 350: 347: 344:Iodoperoxidase 340: 339: 300: 297: 290: 289: 264: 261: 254: 253: 252:Origin, Notes 250: 247: 232:snails have a 155: 154:Classification 152: 122:(E°= 1.36 V), 112: 111: 47: 44: 15: 13: 10: 9: 6: 4: 3: 2: 1092: 1081: 1078: 1077: 1075: 1065: 1060: 1055: 1051: 1037: 1033: 1032: 1027: 1024: 1020: 1019: 1014: 1011: 1007: 1006: 1001: 998: 994: 993: 988: 985: 981: 980: 975: 972: 968: 967: 962: 959: 955: 954: 949: 948: 946: 942: 936: 933: 931: 928: 926: 923: 921: 918: 916: 913: 912: 910: 906: 900: 897: 895: 894:Enzyme family 892: 890: 887: 885: 882: 881: 879: 875: 869: 866: 864: 861: 859: 858:Cooperativity 856: 854: 851: 850: 848: 844: 838: 835: 833: 830: 828: 825: 823: 820: 818: 817:Oxyanion hole 815: 813: 810: 808: 805: 803: 800: 799: 797: 793: 789: 782: 777: 775: 770: 768: 763: 762: 759: 747: 744: 742: 739: 737: 734: 732: 729: 727: 724: 722: 719: 718: 716: 713: 712:peroxiredoxin 709: 705: 697: 694: 692: 689: 688: 687: 684: 682: 679: 677: 674: 672: 669: 667: 664: 660: 657: 655: 652: 650: 647: 645: 642: 640: 637: 635: 632: 630: 627: 625: 622: 619: 618: 617: 614: 612: 609: 607: 604: 602: 599: 597: 594: 592: 589: 587: 584: 583: 581: 579: 575: 570: 566: 562: 555: 550: 548: 543: 541: 536: 535: 532: 521: 517: 512: 507: 502: 497: 493: 489: 488:J. Biol. Chem 485: 478: 475: 471: 467: 464: 460: 456: 453: 449: 446: 441: 437: 433: 429: 425: 421: 414: 411: 408: 407:0-85312-984-3 404: 398: 395: 388: 384: 381: 380: 376: 370: 368: 364: 358: 354: 351: 348: 345: 342: 341: 338: 336: 331: 326: 325:ovoperoxidase 322: 316: 312: 308: 304: 301: 298: 295: 292: 291: 288: 287: 282: 278: 272: 268: 265: 262: 259: 256: 255: 251: 248: 245: 244: 241: 239: 238:Tyrian purple 235: 231: 227: 225: 221: 216: 214: 210: 206: 202: 198: 194: 191: 187: 183: 179: 174: 172: 168: 164: 159: 153: 151: 149: 145: 141: 137: 133: 132:thermodynamic 129: 125: 121: 117: 95: 94: 93: 72: 45: 43: 41: 37: 33: 29: 25: 21: 1031:Translocases 1028: 1015: 1002: 989: 976: 966:Transferases 963: 950: 807:Binding site 620: 491: 487: 477: 466: 448: 423: 419: 413: 397: 361: 319: 285: 275: 228: 217: 190:pseudohalide 175: 170: 162: 160: 157: 113: 49: 19: 18: 802:Active site 578:1.11.1.1-14 565:peroxidases 353:horseradish 277:eosinophils 267:neutrophils 218:A specific 193:thiocyanate 163:preference. 40:environment 24:peroxidases 1005:Isomerases 979:Hydrolases 846:Regulation 686:Deiodinase 389:References 321:sea urchin 263:Cl, Br, I 211:residue. 209:methionine 184:(LPO) and 1080:EC 1.11.1 884:EC number 708:1.11.1.15 205:glutamate 201:aspartate 144:sea water 109:O + R−X 75:Cl, Br, I 28:oxidation 1074:Category 908:Kinetics 832:Cofactor 795:Activity 601:Catalase 520:19363038 455:Archived 440:16895332 377:See also 224:vanadate 148:Fluoride 120:chloride 1064:Biology 1018:Ligases 788:Enzymes 511:2707250 363:thyroid 203:and/or 180:(MPO), 124:bromide 97:X + H 32:halides 1050:Portal 992:Lyases 518:  508:  438:  405:  346:(IPO) 323:eggs ( 307:saliva 299:Br, I 296:(BPO) 260:(CPO) 128:iodide 944:Types 571:1.11) 335:Murex 311:tears 230:Murex 140:humic 1036:list 1029:EC7 1023:list 1016:EC6 1010:list 1003:EC5 997:list 990:EC4 984:list 977:EC3 971:list 964:EC2 958:list 951:EC1 516:PMID 436:PMID 403:ISBN 303:milk 197:heme 171:able 83:, Br 60:, Br 56:, Cl 22:are 621:GPX 506:PMC 496:doi 492:284 428:doi 424:106 169:is 146:). 87:, I 34:by 30:of 1076:: 569:EC 563:: 514:. 504:. 490:. 486:. 434:. 422:. 369:) 349:I 327:), 317:), 309:, 305:, 273:), 136:pH 79:Cl 42:. 1052:: 1038:) 1034:( 1025:) 1021:( 1012:) 1008:( 999:) 995:( 986:) 982:( 973:) 969:( 960:) 956:( 780:e 773:t 766:v 746:6 741:5 736:4 731:3 726:2 721:1 714:) 710:( 659:8 654:7 649:6 644:5 639:4 634:3 629:2 624:1 567:( 553:e 546:t 539:v 522:. 498:: 442:. 430:: 365:( 359:) 355:( 313:( 279:( 269:( 107:2 103:2 101:O 99:2 89:2 85:2 81:2 66:2 62:2 58:2 54:2 52:F

Index

peroxidases
oxidation
halides
hydrogen peroxide
environment
hydrogen peroxide
Nernst equation
chloride
bromide
iodide
thermodynamic
pH
humic
sea water
Fluoride
eosinophil peroxidase
myeloperoxidase
lactoperoxidase
eosinophil peroxidase
pseudohalide
thiocyanate
heme
aspartate
glutamate
methionine
Horseradish peroxidase
vanadium bromoperoxidase
vanadate
Murex
bromoperoxidase

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