Knowledge (XXG)

Chloride peroxidase

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1217: 298:-like activities in addition to catalyzing halogenation reactions. Despite functional similarities with other heme enzymes, the structure of CPO is unique, which folds into a tertiary structure dominated by eight helical segments. The catalytic acid base, required to cleave the peroxide O-O bond, is glutamic acid rather than histidine as in 174: 193: 454:
Hofrichter, M.; Ullrich, R.; Pecyna, Marek J.; Liers, Christiane; Lundell, Taina (2010). "New and classic families of secreted fungal heme peroxidases".
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Butler, Alison; Carter-Franklin, Jayme N. (2004). "The role of vanadium bromoperoxidase in the biosynthesis of halogenated marine natural products".
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Morris DR, Hager LP (1966). "Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein".
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Hager LP, Hollenberg PF, Rand-Meir T, Chiang R, Doubek D (1975). "Chemistry of peroxidase intermediates".
299: 198: 122: 1242: 1010: 929: 768: 753: 225: 1082: 695: 652: 586: 57: 150: 1046: 74: 52: 1237: 979: 838: 676: 610: 535:"The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid" 479: 311: 668: 643:
Theiler R, Cook JC, Hager LP, Siuda JF (1978). "Halohydrocarbon synthesis by homoperoxidase".
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In fact the source of "Cl" is hypochlorous acid (HOCl). Many organochlorine compounds are
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to produce the equivalent of Cl, which replaces a proton in hydrocarbon substrate:
664: 1188: 1123: 959: 786: 17: 1216: 843: 722: 467: 1162: 1136: 672: 518: 475: 267:, specifically those acting on a peroxide as acceptors (peroxidases). The 635: 606: 560: 758: 291: 229: 217: 98: 117: 1175: 945: 510: 228:
of organic compounds. This enzyme combines the inorganic substrates
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The heme-containing chloroperoxidase (CPO) exhibits peroxidase,
284: 105: 918: 691: 914: 1205: 1101: 1065: 1034: 1003: 952: 864: 734: 192: 180: 168: 163: 140: 128: 116: 104: 92: 80: 68: 63: 51: 39: 34: 29: 314:have been solved for this class of enzymes, with 533:Poulos TL, Sundaramoorthy M, Terner J (1995). 930: 703: 523:(this paper also discussed chloroperoxidases. 8: 937: 923: 915: 710: 696: 688: 160: 550: 273:chloride:hydrogen-peroxide oxidoreductase 1212: 446: 26: 263:This enzyme belongs to the family of 7: 599:10.1111/j.1749-6632.1975.tb41524.x 25: 1215: 1: 665:10.1126/science.202.4372.1094 552:10.1016/S0969-2126(01)00274-X 275:. This enzyme is also called 1264: 1248:Enzymes of known structure 1093:Michaelis–Menten kinetics 468:10.1007/s00253-010-2633-0 456:Appl Microbiol Biotechnol 159: 985:Diffusion-limited enzyme 849:Iodothyronine deiodinase 271:of this enzyme class is 854:Iodotyrosine deiodinase 764:Cytochrome c peroxidase 499:Natural Product Reports 824:Horseradish peroxidase 774:Glutathione peroxidase 300:horseradish peroxidase 248:+ H → R-Cl + 2 H 1078:Eadie–Hofstee diagram 1011:Allosteric regulation 769:Eosinophil peroxidase 754:Fatty-acid peroxidase 1088:Lineweaver–Burk plot 579:Ann. N. Y. Acad. Sci 310:As of late 2007, 30 283:which may be either 657:1978Sci...202.1094T 651:(4372): 1094–1096. 591:1975NYASA.244...80H 224:that catalyzes the 211:Chloride peroxidase 30:Chloride peroxidase 1047:Enzyme superfamily 980:Enzyme promiscuity 839:Thyroid peroxidase 306:Structural studies 279:. It employs one 1203: 1202: 912: 911: 545:(12): 1367–1377. 234:hydrogen peroxide 220:) is a family of 208: 207: 204: 203: 123:metabolic pathway 16:(Redirected from 1255: 1220: 1219: 1211: 1083:Hanes–Woolf plot 1026:Enzyme activator 1021:Enzyme inhibitor 995:Enzyme catalysis 939: 932: 925: 916: 749:NADPH peroxidase 712: 705: 698: 689: 684: 639: 618: 565: 564: 554: 530: 524: 522: 511:10.1039/b302337k 494: 488: 487: 451: 318:accession codes 277:chloroperoxidase 240:R-H + Cl + H 161: 27: 21: 18:Chloroperoxidase 1263: 1262: 1258: 1257: 1256: 1254: 1253: 1252: 1228: 1227: 1226: 1214: 1206: 1204: 1199: 1111:Oxidoreductases 1097: 1073:Enzyme kinetics 1061: 1057:List of enzymes 1030: 999: 970:Catalytic triad 948: 943: 913: 908: 860: 834:Myeloperoxidase 829:Lactoperoxidase 744:NADH peroxidase 730: 719:Oxidoreductases 716: 642: 621: 576: 573: 571:Further reading 568: 532: 531: 527: 496: 495: 491: 453: 452: 448: 444: 308: 296:cytochrome P450 269:systematic name 265:oxidoreductases 251: 247: 243: 23: 22: 15: 12: 11: 5: 1261: 1259: 1251: 1250: 1245: 1240: 1230: 1229: 1225: 1224: 1201: 1200: 1198: 1197: 1184: 1171: 1158: 1145: 1132: 1119: 1105: 1103: 1099: 1098: 1096: 1095: 1090: 1085: 1080: 1075: 1069: 1067: 1063: 1062: 1060: 1059: 1054: 1049: 1044: 1038: 1036: 1035:Classification 1032: 1031: 1029: 1028: 1023: 1018: 1013: 1007: 1005: 1001: 1000: 998: 997: 992: 987: 982: 977: 972: 967: 962: 956: 954: 950: 949: 944: 942: 941: 934: 927: 919: 910: 909: 907: 906: 901: 896: 891: 886: 881: 875: 873: 862: 861: 859: 858: 857: 856: 851: 841: 836: 831: 826: 821: 820: 819: 814: 809: 804: 799: 794: 789: 784: 771: 766: 761: 756: 751: 746: 740: 738: 732: 731: 717: 715: 714: 707: 700: 692: 686: 685: 640: 619: 572: 569: 567: 566: 525: 489: 462:(3): 871–897. 445: 443: 440: 307: 304: 258:biosynthesized 254: 253: 249: 245: 241: 206: 205: 202: 201: 196: 190: 189: 184: 178: 177: 172: 166: 165: 157: 156: 145: 138: 137: 132: 126: 125: 120: 114: 113: 108: 102: 101: 96: 90: 89: 84: 78: 77: 72: 66: 65: 61: 60: 55: 49: 48: 43: 37: 36: 32: 31: 24: 14: 13: 10: 9: 6: 4: 3: 2: 1260: 1249: 1246: 1244: 1241: 1239: 1236: 1235: 1233: 1223: 1218: 1213: 1209: 1195: 1191: 1190: 1185: 1182: 1178: 1177: 1172: 1169: 1165: 1164: 1159: 1156: 1152: 1151: 1146: 1143: 1139: 1138: 1133: 1130: 1126: 1125: 1120: 1117: 1113: 1112: 1107: 1106: 1104: 1100: 1094: 1091: 1089: 1086: 1084: 1081: 1079: 1076: 1074: 1071: 1070: 1068: 1064: 1058: 1055: 1053: 1052:Enzyme family 1050: 1048: 1045: 1043: 1040: 1039: 1037: 1033: 1027: 1024: 1022: 1019: 1017: 1016:Cooperativity 1014: 1012: 1009: 1008: 1006: 1002: 996: 993: 991: 988: 986: 983: 981: 978: 976: 975:Oxyanion hole 973: 971: 968: 966: 963: 961: 958: 957: 955: 951: 947: 940: 935: 933: 928: 926: 921: 920: 917: 905: 902: 900: 897: 895: 892: 890: 887: 885: 882: 880: 877: 876: 874: 871: 870:peroxiredoxin 867: 863: 855: 852: 850: 847: 846: 845: 842: 840: 837: 835: 832: 830: 827: 825: 822: 818: 815: 813: 810: 808: 805: 803: 800: 798: 795: 793: 790: 788: 785: 783: 780: 777: 776: 775: 772: 770: 767: 765: 762: 760: 757: 755: 752: 750: 747: 745: 742: 741: 739: 737: 733: 728: 724: 720: 713: 708: 706: 701: 699: 694: 693: 690: 682: 678: 674: 670: 666: 662: 658: 654: 650: 646: 641: 637: 633: 630:(8): 1763–8. 629: 625: 624:J. Biol. Chem 620: 616: 612: 608: 604: 600: 596: 592: 588: 584: 580: 575: 574: 570: 562: 558: 553: 548: 544: 540: 536: 529: 526: 520: 516: 512: 508: 504: 500: 493: 490: 485: 481: 477: 473: 469: 465: 461: 457: 450: 447: 441: 439: 437: 433: 429: 425: 421: 417: 413: 409: 405: 401: 397: 393: 389: 385: 381: 377: 373: 369: 365: 361: 357: 353: 349: 345: 341: 337: 333: 329: 325: 321: 317: 313: 305: 303: 301: 297: 293: 288: 287:or vanadium. 286: 282: 278: 274: 270: 266: 261: 260:in this way. 259: 239: 238: 237: 235: 231: 227: 223: 219: 216: 212: 200: 197: 195: 191: 188: 185: 183: 179: 176: 173: 171: 167: 162: 158: 155: 152: 149: 146: 143: 139: 136: 133: 131: 127: 124: 121: 119: 115: 112: 109: 107: 103: 100: 99:NiceZyme view 97: 95: 91: 88: 85: 83: 79: 76: 73: 71: 67: 62: 59: 56: 54: 50: 47: 44: 42: 38: 33: 28: 19: 1243:Heme enzymes 1189:Translocases 1186: 1173: 1160: 1147: 1134: 1124:Transferases 1121: 1108: 965:Binding site 778: 648: 644: 627: 623: 585:(1): 80–93. 582: 578: 542: 538: 528: 505:(1): 180–8. 502: 498: 492: 459: 455: 449: 309: 289: 276: 272: 262: 255: 226:chlorination 210: 209: 87:BRENDA entry 960:Active site 736:1.11.1.1-14 723:peroxidases 75:IntEnz view 35:Identifiers 1232:Categories 1163:Isomerases 1137:Hydrolases 1004:Regulation 844:Deiodinase 442:References 312:structures 144:structures 111:KEGG entry 58:9055-20-3 1238:EC 1.11.1 1042:EC number 866:1.11.1.15 539:Structure 218:1.11.1.10 64:Databases 46:1.11.1.10 1066:Kinetics 990:Cofactor 953:Activity 759:Catalase 681:21448823 673:17777960 615:27336177 519:15039842 484:24417282 476:20495915 292:catalase 281:cofactor 230:chloride 199:proteins 187:articles 175:articles 148:RCSB PDB 1222:Biology 1176:Ligases 946:Enzymes 653:Bibcode 645:Science 636:5949836 607:1056179 587:Bibcode 561:8747463 222:enzymes 135:profile 118:MetaCyc 53:CAS no. 1208:Portal 1150:Lyases 679:  671:  634:  613:  605:  559:  517:  482:  474:  434:, and 182:PubMed 164:Search 154:PDBsum 94:ExPASy 82:BRENDA 70:IntEnz 41:EC no. 1102:Types 729:1.11) 677:S2CID 611:S2CID 480:S2CID 130:PRIAM 1194:list 1187:EC7 1181:list 1174:EC6 1168:list 1161:EC5 1155:list 1148:EC4 1142:list 1135:EC3 1129:list 1122:EC2 1116:list 1109:EC1 669:PMID 632:PMID 603:PMID 557:PMID 515:PMID 472:PMID 436:2J5M 432:2J19 428:2J18 424:2CPO 420:2CJ2 416:2CJ1 412:2CJ0 408:2CIZ 404:2CIY 400:2CIX 396:2CIW 392:2CIV 388:1VNS 384:1VNI 380:1VNH 376:1VNG 372:1VNF 368:1VNE 364:1VNC 360:1QI9 356:1QHB 352:1IDU 348:1IDQ 344:1CPO 340:1BRT 336:1A8U 332:1A8S 328:1A8Q 324:1A88 320:1A7U 294:and 285:heme 232:and 194:NCBI 151:PDBe 106:KEGG 779:GPX 661:doi 649:202 628:241 595:doi 583:244 547:doi 507:doi 464:doi 316:PDB 170:PMC 142:PDB 1234:: 727:EC 721:: 675:. 667:. 659:. 647:. 626:. 609:. 601:. 593:. 581:. 555:. 541:. 537:. 513:. 503:21 501:. 478:. 470:. 460:87 458:. 438:. 430:, 426:, 422:, 418:, 414:, 410:, 406:, 402:, 398:, 394:, 390:, 386:, 382:, 378:, 374:, 370:, 366:, 362:, 358:, 354:, 350:, 346:, 342:, 338:, 334:, 330:, 326:, 322:, 302:. 215:EC 1210:: 1196:) 1192:( 1183:) 1179:( 1170:) 1166:( 1157:) 1153:( 1144:) 1140:( 1131:) 1127:( 1118:) 1114:( 938:e 931:t 924:v 904:6 899:5 894:4 889:3 884:2 879:1 872:) 868:( 817:8 812:7 807:6 802:5 797:4 792:3 787:2 782:1 725:( 711:e 704:t 697:v 683:. 663:: 655:: 638:. 617:. 597:: 589:: 563:. 549:: 543:3 521:. 509:: 486:. 466:: 252:O 250:2 246:2 244:O 242:2 213:( 20:)

Index

Chloroperoxidase
EC no.
1.11.1.10
CAS no.
9055-20-3
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
PMC
articles
PubMed
articles
NCBI
proteins
EC
1.11.1.10
enzymes

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