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P450-containing systems

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1403: 679:). In this system, the N-terminal P450 domain is fused to the reductase domain that shows sequence similarity to phthalate dioxygenase reductase and consists, in its turn, of FMN-binding domain and C-terminal plant-type ferredoxin domain. Similar systems have been identified in the heavy-metal-tolerant bacterium 965:
McLean, K.J.; Sabri, M.; Marshall, K.R.; Lawson, R.J.; Lewis, D.G.; Clift, D.; Balding, P.R.; Dunford, A.J.; Warman, A.J.; McVey, J.P.; Quinn, A.-M.; Sutcliffe, M.J.; Scrutton, N.S.; Munro, A.W. (2005). "Biodiversity of cytochrome P450 redox systems".
869:) are examples of P450 enzymes that do not require a reductase or molecular oxygen for their catalytic activity. Substrates for all these enzymes are fatty acid derivatives containing partially reduced dioxygen (either hydroperoxy or epidioxy groups). 42:
chains, called P450-containing monooxygenase systems, although self-sufficient, non-monooxygenase P450s have been also described. All known P450-containing monooxygenase systems share common structural and functional
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transfer electrons between the flavin reductase (protein or domain) and P450. While P450-containing systems are found throughout all kingdoms of life, some organisms lack one or more of these redox domains.
417:, CPR is a C-terminal domain of CYP102, a single polypeptide self-sufficient soluble P450 system (P450 is an N-terminal domain). The general scheme of electron flow in the CPR/P450 system is: 1042:
McLean, K.J.; Warman, A.J.; Seward, H.E.; Marshall, K.R.; Girvan, H.M.; Cheesman, M.R.; Waterman, M.R.; Munro, A.W. (2006). "Biophysical characterization of the sterol demethylase P450 from
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and several membrane-bound P450s (CYP11A, CYP11B, CYP27). In bacteria, putidaredoxin, terpredoxin, and rhodocoxin serve as electron carriers between corresponding
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ferredoxins (Fd) that act as single electron carriers between FAD-containing ferredoxin reductase (FR) and P450. In mitochondrial monooxygenase systems,
1155: 77:. These ubiquitous redox domains, in various combinations, are widely distributed in biological systems. FMN domain, ferredoxin or cytochrome 1083:"A self-sufficient cytochrome P450 with a primary structural organisation that includes a flavin domain and a [2Fe-2S] redox center" 1003:"Redundancy or flexibility: molecular diversity of the electron transfer components for P450 monooxygenases in higher plants" 922: 1348: 1148: 1241: 1081:
Roberts, G.A.; Γ‡elik, A.; Hunter, D.J.B.; Ost, T.W.B.; White, J.H.; Chapman, S.K.; Turner, N.J.; Flitsch, S.L. (2003).
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Degtyarenko, K.N.; Kulikova, T.A. (2001). "Evolution of bioinorganic motifs in P450-containing systems".
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P450 enzymes and some bacterial P450s receive electrons from a FAD- and FMN-containing enzyme known as
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The general scheme of electron flow in the P450 systems containing adrenodoxin-type ferredoxins is:
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can serve as an effector (activator or inhibitor) of P450s. It was hypothesized that cytochrome
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architecture. Apart from the cytochrome itself, these systems contain one or more fundamental
318: 232: 109: 60: 8: 1380: 1370: 1338: 117: 1375: 759: 941: 1107: 1063: 1024: 983: 945: 903: 834: 811: 44: 39: 409:). Microsomal CPR is membrane-bound protein that interacts with different P450s. In 1097: 1055: 1014: 975: 937: 895: 1041: 845:) as an oxidant. These enzymes do not require any reduction system for catalysis. 1168: 1133: 750: 28: 1407: 1316: 1199: 1176: 1080: 964: 1417: 1211: 1194: 768: 93: 68: 1111: 1102: 1067: 1028: 987: 907: 764: 56: 1189: 855:), fatty acid hydroperoxide lyase (CYP74B), prostacyclin synthase (CYP8; 763:. This enzyme does not have monooxygenase activity but is able to reduce 240: 105: 866: 859: 852: 1301: 1278: 979: 899: 779: 695: 622: 505: 498: 421: 406: 395: 343: 271: 124: 64: 1059: 833:) catalyse the hydroxylation reaction of long-chain fatty acids using 38:
P450 enzymes usually function as a terminal oxidase in multicomponent
691:. The general scheme of electron flow in this system appears to be: 1402: 830: 816: 754: 684: 676: 1019: 1002: 248: 1273: 1268: 1164: 885: 1358: 1353: 753:
in several fungal species. The best-characterized P450nor is
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An unusual one-component P450 system was originally found in
48: 1251: 1246: 923:"Electron transfer proteins of cytochrome P450 systems" 595:
system to support P450 catalysis has been demonstrated
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functions as a soluble electron carrier between NADPH:
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The ubiquitous electron-transport protein cytochrome
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Branched-chain alpha-keto acid dehydrogenase complex
1000: 116:-dependent ferredoxin reductases and soluble P450s ( 1366:
Phosphoenolpyruvate sugar phosphotransferase system
1046:, its cognate ferredoxin, and their interactions". 618:the first and second electrons are donated by CBR. 1163: 96:and some bacterial P450 systems employ soluble Fe 1415: 1185:Photosynthetic reaction center complex proteins 1149: 920: 775:O) directly using NAD(P)H as electron donor: 1156: 1142: 932:. Advances in Molecular and Cell Biology. 483:electron to P450, either from CPR or from 327:contains flavoprotein reductase A (FprA), 1101: 1018: 14: 1416: 666: 460: 1137: 88: 1129:Directory of P450-containing Systems 741: 1349:Mitochondrial trifunctional protein 819:) and fatty acid Ξ±-hydroxylase P450 479:is involved in the transfer of the 389: 24: 862:) and thromboxane synthase (CYP5; 710: 599:using purified CBR and cytochrome 588:The ability of the CBR/cytochrome 358: 286: 31:protein or domain can be called a 25: 1435: 1122: 788: 723: 648: 637: 442: 371: 299: 1401: 747:Nitric oxide reductase (P450nor) 27:Any enzyme system that includes 1307:Carbamoyl phosphate synthase II 1001:Ohta, D.; Mizutani, M. (2004). 848:Allene oxide synthase (CYP74A; 1312:Aspartate carbamoyltransferase 1220:Pyruvate dehydrogenase complex 1074: 1035: 994: 958: 914: 879: 704: 631: 436: 430: 352: 280: 13: 1: 1344:Glycine decarboxylase complex 1339:Fatty acid synthetase complex 942:10.1016/S1569-2558(08)60339-2 872: 804:Fatty acid Ξ²-hydroxylase P450 749:is a P450 enzyme involved in 687:) and in several species of 7: 782: 698: 625: 546: 508: 424: 346: 274: 225: 193: 161: 127: 10: 1440: 1376:Sucrase-isomaltase complex 1242:Oxoglutarate dehydrogenase 1044:Mycobacterium tuberculosis 324:Mycobacterium tuberculosis 1294: 1210: 1175: 400:cytochrome P450 reductase 1334:Electron transport chain 826:Pseudomonas paucimobilis 608:Saccharomyces cerevisiae 1324:P450-containing systems 681:Ralstonia metallidurans 339:and CYP51 hemoprotein. 135:putidaredoxin reductase 1329:Cytochrome b6f complex 1103:10.1074/jbc.M309630200 921:Hanukoglu, I. (1996). 610:and CYP51 enzyme from 168:terpredoxin reductase 33:P450-containing system 1169:multienzyme complexes 233:adrenodoxin reductase 200:rhodocoxin reductase 110:adrenodoxin reductase 1381:Tryptophan synthase 1371:Polyketide synthase 1096:(49): 48914–48920. 968:Biochem. Soc. Trans 930:Adv. Mol. Cell Biol 888:Biochem. Soc. Trans 667:FMN/Fd/P450 systems 461:CBR/b5/P450 systems 411:Bacillus megaterium 120:, CYP108, CYP116). 1013:(1–3): 1587–1597. 980:10.1042/BST0330796 900:10.1042/BST0290139 760:Fusarium oxysporum 614:. In this system, 319:sterol demethylase 89:FR/Fd/P450 systems 1389: 1388: 1060:10.1021/bi0601609 1054:(27): 8427–8443. 835:hydrogen peroxide 812:Bacillus subtilis 799: 798: 742:P450-only systems 737: 736: 662: 661: 584: 583: 456: 455: 415:Bacillus subtilis 385: 384: 329:bacterial-type Fe 313: 312: 263: 262: 40:electron-transfer 16:(Redirected from 1431: 1406: 1405: 1397: 1158: 1151: 1144: 1135: 1134: 1116: 1115: 1105: 1087: 1078: 1072: 1071: 1039: 1033: 1032: 1022: 998: 992: 991: 962: 956: 955: 927: 918: 912: 911: 883: 780: 696: 675:sp. NCIMB 9784 ( 623: 612:Candida albicans 506: 485:NADH:cytochrome 422: 390:CPR/P450 systems 344: 272: 125: 21: 1439: 1438: 1434: 1433: 1432: 1430: 1429: 1428: 1424:Cytochrome P450 1414: 1413: 1412: 1400: 1392: 1390: 1385: 1290: 1206: 1171: 1162: 1125: 1120: 1119: 1085: 1079: 1075: 1040: 1036: 999: 995: 963: 959: 952: 925: 919: 915: 884: 880: 875: 844: 840: 822: 807: 774: 751:denitrification 744: 733: 718: 714: 669: 658: 643: 605: 594: 580: 565: 542: 527: 491: 478: 471: 463: 452: 392: 381: 366: 362: 336: 332: 309: 294: 290: 259: 221: 189: 157: 103: 99: 91: 83: 75: 29:cytochrome P450 23: 22: 18:Microsomal P450 15: 12: 11: 5: 1437: 1427: 1426: 1411: 1410: 1387: 1386: 1384: 1383: 1378: 1373: 1368: 1363: 1362: 1361: 1356: 1346: 1341: 1336: 1331: 1326: 1321: 1320: 1319: 1317:Dihydroorotase 1314: 1309: 1298: 1296: 1292: 1291: 1289: 1288: 1287: 1286: 1281: 1276: 1271: 1261: 1260: 1259: 1254: 1249: 1239: 1238: 1237: 1232: 1227: 1216: 1214: 1208: 1207: 1205: 1204: 1203: 1202: 1197: 1187: 1181: 1179: 1177:Photosynthesis 1173: 1172: 1161: 1160: 1153: 1146: 1138: 1132: 1131: 1124: 1123:External links 1121: 1118: 1117: 1073: 1034: 993: 974:(4): 796–801. 957: 950: 913: 894:(2): 139–147. 877: 876: 874: 871: 842: 838: 820: 805: 801: 800: 797: 796: 793: 790: 787: 784: 772: 743: 740: 739: 738: 735: 734: 731: 728: 725: 722: 719: 716: 712: 709: 706: 703: 700: 668: 665: 664: 663: 660: 659: 656: 653: 650: 647: 644: 641: 636: 633: 630: 627: 603: 592: 586: 585: 582: 581: 578: 575: 572: 569: 566: 563: 557: 554: 551: 548: 544: 543: 540: 537: 534: 531: 528: 525: 519: 516: 513: 510: 489: 476: 469: 462: 459: 458: 457: 454: 453: 450: 447: 444: 441: 438: 435: 432: 429: 426: 391: 388: 387: 386: 383: 382: 379: 376: 373: 370: 367: 364: 360: 357: 354: 351: 348: 334: 330: 315: 314: 311: 310: 307: 304: 301: 298: 295: 292: 288: 285: 282: 279: 276: 265: 264: 261: 260: 257: 254: 251: 246: 243: 238: 235: 230: 227: 223: 222: 219: 216: 213: 210: 207: 204: 201: 198: 195: 191: 190: 187: 184: 181: 178: 175: 172: 169: 166: 163: 159: 158: 155: 152: 149: 146: 143: 142:putidaredoxin 140: 137: 132: 129: 101: 97: 90: 87: 81: 73: 9: 6: 4: 3: 2: 1436: 1425: 1422: 1421: 1419: 1409: 1404: 1399: 1398: 1395: 1382: 1379: 1377: 1374: 1372: 1369: 1367: 1364: 1360: 1357: 1355: 1352: 1351: 1350: 1347: 1345: 1342: 1340: 1337: 1335: 1332: 1330: 1327: 1325: 1322: 1318: 1315: 1313: 1310: 1308: 1305: 1304: 1303: 1300: 1299: 1297: 1293: 1285: 1282: 1280: 1277: 1275: 1272: 1270: 1267: 1266: 1265: 1262: 1258: 1255: 1253: 1250: 1248: 1245: 1244: 1243: 1240: 1236: 1233: 1231: 1228: 1226: 1223: 1222: 1221: 1218: 1217: 1215: 1213: 1212:Dehydrogenase 1209: 1201: 1198: 1196: 1193: 1192: 1191: 1188: 1186: 1183: 1182: 1180: 1178: 1174: 1170: 1166: 1159: 1154: 1152: 1147: 1145: 1140: 1139: 1136: 1130: 1127: 1126: 1113: 1109: 1104: 1099: 1095: 1091: 1090:J. Biol. Chem 1084: 1077: 1069: 1065: 1061: 1057: 1053: 1049: 1045: 1038: 1030: 1026: 1021: 1016: 1012: 1008: 1007:Front. Biosci 1004: 997: 989: 985: 981: 977: 973: 969: 961: 953: 951:9780762301133 947: 943: 939: 935: 931: 924: 917: 909: 905: 901: 897: 893: 889: 882: 878: 870: 868: 865: 861: 858: 854: 851: 846: 836: 832: 828: 827: 818: 814: 813: 808: 794: 791: 785: 781: 778: 777: 776: 770: 769:nitrous oxide 767:(NO) to form 766: 762: 761: 756: 752: 748: 729: 726: 720: 707: 701: 697: 694: 693: 692: 690: 686: 682: 678: 674: 654: 651: 645: 640: 634: 628: 624: 621: 620: 619: 617: 613: 609: 602: 598: 591: 576: 573: 570: 567: 562: 558: 555: 552: 549: 545: 538: 535: 532: 529: 524: 520: 517: 514: 511: 507: 504: 503: 502: 500: 497: 493: 488: 482: 475: 468: 448: 445: 439: 433: 427: 423: 420: 419: 418: 416: 412: 408: 405: 401: 397: 377: 374: 368: 355: 349: 345: 342: 341: 340: 338: 326: 325: 320: 305: 302: 296: 283: 277: 273: 270: 269: 268: 255: 252: 250: 247: 244: 242: 239: 236: 234: 231: 228: 224: 217: 214: 211: 208: 205: 202: 199: 196: 192: 185: 182: 179: 176: 173: 170: 167: 164: 160: 153: 150: 147: 144: 141: 138: 136: 133: 130: 126: 123: 122: 121: 119: 115: 111: 107: 95: 94:Mitochondrial 86: 80: 76: 72: 66: 62: 58: 54: 50: 46: 41: 36: 34: 30: 19: 1323: 1093: 1089: 1076: 1051: 1048:Biochemistry 1047: 1043: 1037: 1020:10.2741/1356 1010: 1006: 996: 971: 967: 960: 933: 929: 916: 891: 887: 881: 847: 824: 810: 802: 765:nitric oxide 758: 745: 688: 680: 672: 670: 638: 615: 611: 607: 600: 596: 589: 587: 560: 522: 486: 480: 473: 466: 464: 414: 410: 393: 322: 321:system from 316: 266: 174:terpredoxin 92: 78: 70: 57:flavoprotein 55:-containing 37: 32: 26: 1190:Photosystem 689:Burkolderia 673:Rhodococcus 394:Eukaryotic 241:adrenodoxin 206:rhodocoxin 106:adrenodoxin 69:cytochrome 59:or domain, 873:References 396:microsomal 337:ferredoxin 65:ferredoxin 936:: 29–56. 492:reductase 51:domains: 1418:Category 1112:14514666 1068:16819841 1029:14977570 988:16042601 908:11356142 867:5.3.99.5 860:5.3.99.4 853:4.2.1.92 831:CYP152B1 817:CYP152A1 685:CYP116A1 677:CYP116B2 626:NAD(P)H 597:in vitro 63:domain, 1408:Biology 1165:Enzymes 783:NAD(P)H 755:CYP55A1 499:1.6.2.2 407:1.6.2.4 347:NAD(P)H 275:NAD(P)H 249:CYP11A1 212:CYP116 180:CYP108 148:CYP101 1394:Portal 1274:BCKDHB 1269:BCKDHA 1110:  1066:  1027:  986:  948:  906:  494:(CBR; 481:second 402:(CPR; 118:CYP101 45:domain 1359:HADHB 1354:HADHA 1295:Other 1086:(PDF) 926:(PDF) 823:from 809:from 789:P450 757:from 724:P450 649:P450 606:from 571:P450 533:P450 509:NADPH 443:P450 425:NADPH 372:P450 300:P450 226:NADPH 49:redox 1252:DLST 1247:OGDH 1108:PMID 1064:PMID 1025:PMID 984:PMID 946:ISBN 904:PMID 705:FMN 699:NADH 632:FAD 616:both 559:cyt 547:NADH 521:cyt 437:FMN 431:FAD 413:and 353:FAD 317:The 281:FAD 194:NADH 162:NADH 128:NADH 114:NADH 67:and 1302:CAD 1284:DLD 1279:DBT 1257:DLD 1098:doi 1094:278 1056:doi 1015:doi 976:doi 938:doi 896:doi 821:SPΞ± 806:BSΞ² 795:NO 553:CBR 515:CPR 501:): 61:FMN 53:FAD 1420:: 1235:E3 1230:E2 1225:E1 1200:II 1167:: 1106:. 1092:. 1088:. 1062:. 1052:45 1050:. 1023:. 1009:. 1005:. 982:. 972:33 970:. 944:. 934:14 928:. 902:. 892:29 890:. 864:EC 857:EC 850:EC 837:(H 786:β†’ 771:(N 721:β†’ 711:Fe 708:β†’ 702:β†’ 652:β†’ 646:β†’ 635:β†’ 629:β†’ 556:β†’ 550:β†’ 518:β†’ 512:β†’ 496:EC 440:β†’ 434:β†’ 428:β†’ 404:EC 369:β†’ 359:Fe 356:β†’ 350:β†’ 297:β†’ 287:Fe 284:β†’ 278:β†’ 245:β†’ 237:β†’ 229:β†’ 209:β†’ 203:β†’ 197:β†’ 177:β†’ 171:β†’ 165:β†’ 145:β†’ 139:β†’ 131:β†’ 35:. 1396:: 1195:I 1157:e 1150:t 1143:v 1114:. 1100:: 1070:. 1058:: 1031:. 1017:: 1011:9 990:. 978:: 954:. 940:: 910:. 898:: 843:2 841:O 839:2 829:( 815:( 792:β†’ 773:2 732:2 730:O 727:β†’ 717:2 715:S 713:2 683:( 657:2 655:O 642:5 639:b 604:5 601:b 593:5 590:b 579:2 577:O 574:β†’ 568:β†’ 564:5 561:b 541:2 539:O 536:β†’ 530:β†’ 526:5 523:b 490:5 487:b 477:5 474:b 470:5 467:b 451:2 449:O 446:β†’ 380:2 378:O 375:β†’ 365:4 363:S 361:3 335:4 333:S 331:3 308:2 306:O 303:β†’ 293:2 291:S 289:2 258:2 256:O 253:β†’ 220:2 218:O 215:β†’ 188:2 186:O 183:β†’ 156:2 154:O 151:β†’ 102:2 100:S 98:2 82:5 79:b 74:5 71:b 20:)

Index

Microsomal P450
cytochrome P450
electron-transfer
domain
redox
FAD
flavoprotein
FMN
ferredoxin
cytochrome b5
Mitochondrial
adrenodoxin
adrenodoxin reductase
NADH
CYP101
putidaredoxin reductase
adrenodoxin reductase
adrenodoxin
CYP11A1
sterol demethylase
Mycobacterium tuberculosis
bacterial-type Fe3S4 ferredoxin
microsomal
cytochrome P450 reductase
EC
1.6.2.4
NADH:cytochrome b5 reductase
EC
1.6.2.2
CYP116B2

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