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Quercetin 2,3-dioxygenase

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26: 1014: 278: 191: 210: 1071: 558: 1105: 652: 322:
as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O
435:"Anaerobic enzymeâ‹…substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase" 733: 203: 154: 1064: 130: 889: 1115: 642: 618: 604: 551: 657: 613: 599: 391: 387: 383: 379: 375: 371: 1004: 874: 148: 1057: 990: 977: 964: 951: 938: 925: 912: 691: 672: 627: 584: 884: 838: 781: 575: 285: 236: 135: 41: 1100: 786: 544: 343: 215: 123: 263: 1095: 807: 726: 879: 647: 637: 499: 446: 151: 58: 75: 1090: 843: 300: 53: 25: 1110: 776: 700: 662: 525: 517: 474: 421: 367: 363: 251: 142: 111: 30:
Crystal structure of quercetin 2,3-dioxygenase from pdb entry 1H1I with quercetin and copper.
822: 817: 791: 719: 536: 507: 464: 454: 413: 87: 869: 853: 766: 327: 304: 46: 503: 450: 1041: 1018: 907: 848: 567: 315: 186: 512: 487: 469: 434: 417: 166: 1084: 812: 771: 161: 529: 761: 594: 308: 985: 920: 756: 170: 1013: 681: 228: 959: 933: 571: 289: 247: 521: 488:"Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase" 478: 459: 404:
Oka T, Simpson FJ (1971). "Quercetinase, a dioxygenase containing copper".
425: 239: 99: 1034: 118: 1037: 972: 742: 622: 608: 351: 293: 243: 198: 94: 82: 70: 946: 347: 106: 715: 540: 711: 280:
2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H
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are 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate,
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Bowater L, Fairhurst SA, Just VJ, Bornemann S (2004).
1002: 266: 898: 862: 831: 800: 749: 690: 671: 583: 318:, specifically those acting on single donors with O 209: 197: 185: 180: 160: 141: 129: 117: 105: 93: 81: 69: 64: 52: 40: 35: 18: 272: 366:have been solved for this class of enzymes, with 334:(decyclizing). Other names in common use include 1065: 727: 552: 8: 1072: 1058: 734: 720: 712: 559: 545: 537: 177: 24: 511: 468: 458: 433:Steiner RA, Kalk KH, Dijkstra BW (2002). 265: 1009: 15: 314:This enzyme belongs to the family of 7: 1030: 1028: 332:quercetin:oxygen 2,3-oxidoreductase 653:4-Hydroxyphenylpyruvate dioxygenase 273:{\displaystyle \rightleftharpoons } 14: 1012: 1: 643:Homogentisate 1,2-dioxygenase 513:10.1016/S0014-5793(03)01439-X 418:10.1016/S0006-291X(71)80076-1 406:Biochem. Biophys. Res. Commun 1044:. You can help Knowledge by 619:Arachidonate 15-lipoxygenase 605:Arachidonate 12-lipoxygenase 439:Proc. Natl. Acad. Sci. U.S.A 658:Indoleamine 2,3-dioxygenase 614:Arachidonate 8-lipoxygenase 600:Arachidonate 5-lipoxygenase 1132: 1106:Enzymes of known structure 1027: 890:Michaelis–Menten kinetics 628:Linoleate 11-lipoxygenase 233:quercetin 2,3-dioxygenase 176: 23: 19:quercetin 2,3-dioxygenase 782:Diffusion-limited enzyme 330:of this enzyme class is 1040:-related article is a 460:10.1073/pnas.262506299 340:flavonol 2,4-oxygenase 274: 875:Eadie–Hofstee diagram 808:Allosteric regulation 587:: two atoms of oxygen 362:As of late 2007, six 275: 1116:Oxidoreductase stubs 885:Lineweaver–Burk plot 675:: one atom of oxygen 648:Cysteine dioxygenase 638:Catechol dioxygenase 299:, whereas its three 264: 504:2004FEBSL.557...45B 451:2002PNAS...9916625S 288:of this enzyme are 844:Enzyme superfamily 777:Enzyme promiscuity 701:Inositol oxygenase 682:Firefly luciferase 663:Chlorite dismutase 635:other dioxygenase: 364:crystal structures 358:Structural studies 270: 1053: 1052: 1000: 999: 709: 708: 252:chemical reaction 225: 224: 221: 220: 124:metabolic pathway 1123: 1074: 1067: 1060: 1029: 1017: 1016: 1008: 880:Hanes–Woolf plot 823:Enzyme activator 818:Enzyme inhibitor 792:Enzyme catalysis 736: 729: 722: 713: 561: 554: 547: 538: 533: 515: 482: 472: 462: 445:(26): 16625–30. 429: 370:accession codes 279: 277: 276: 271: 178: 28: 16: 1131: 1130: 1126: 1125: 1124: 1122: 1121: 1120: 1081: 1080: 1079: 1078: 1025: 1023: 1011: 1003: 1001: 996: 908:Oxidoreductases 894: 870:Enzyme kinetics 858: 854:List of enzymes 827: 796: 767:Catalytic triad 745: 740: 710: 705: 686: 667: 579: 568:Oxidoreductases 565: 485: 432: 403: 400: 360: 328:systematic name 325: 321: 316:oxidoreductases 297: 262: 261: 260: 31: 12: 11: 5: 1129: 1127: 1119: 1118: 1113: 1108: 1103: 1101:Copper enzymes 1098: 1093: 1083: 1082: 1077: 1076: 1069: 1062: 1054: 1051: 1050: 1022: 1021: 998: 997: 995: 994: 981: 968: 955: 942: 929: 916: 902: 900: 896: 895: 893: 892: 887: 882: 877: 872: 866: 864: 860: 859: 857: 856: 851: 846: 841: 835: 833: 832:Classification 829: 828: 826: 825: 820: 815: 810: 804: 802: 798: 797: 795: 794: 789: 784: 779: 774: 769: 764: 759: 753: 751: 747: 746: 741: 739: 738: 731: 724: 716: 707: 706: 704: 703: 697: 695: 688: 687: 685: 684: 678: 676: 669: 668: 666: 665: 660: 655: 650: 645: 640: 631: 630: 625: 616: 611: 602: 590: 588: 581: 580: 572:monooxygenases 566: 564: 563: 556: 549: 541: 535: 534: 483: 430: 399: 396: 359: 356: 342:. It has two 323: 319: 295: 284:Thus, the two 282: 281: 269: 258: 223: 222: 219: 218: 213: 207: 206: 201: 195: 194: 189: 183: 182: 174: 173: 164: 158: 157: 146: 139: 138: 133: 127: 126: 121: 115: 114: 109: 103: 102: 97: 91: 90: 85: 79: 78: 73: 67: 66: 62: 61: 56: 50: 49: 44: 38: 37: 33: 32: 29: 21: 20: 13: 10: 9: 6: 4: 3: 2: 1128: 1117: 1114: 1112: 1109: 1107: 1104: 1102: 1099: 1097: 1094: 1092: 1089: 1088: 1086: 1075: 1070: 1068: 1063: 1061: 1056: 1055: 1049: 1047: 1043: 1039: 1036: 1031: 1026: 1020: 1015: 1010: 1006: 992: 988: 987: 982: 979: 975: 974: 969: 966: 962: 961: 956: 953: 949: 948: 943: 940: 936: 935: 930: 927: 923: 922: 917: 914: 910: 909: 904: 903: 901: 897: 891: 888: 886: 883: 881: 878: 876: 873: 871: 868: 867: 865: 861: 855: 852: 850: 849:Enzyme family 847: 845: 842: 840: 837: 836: 834: 830: 824: 821: 819: 816: 814: 813:Cooperativity 811: 809: 806: 805: 803: 799: 793: 790: 788: 785: 783: 780: 778: 775: 773: 772:Oxyanion hole 770: 768: 765: 763: 760: 758: 755: 754: 752: 748: 744: 737: 732: 730: 725: 723: 718: 717: 714: 702: 699: 698: 696: 693: 689: 683: 680: 679: 677: 674: 670: 664: 661: 659: 656: 654: 651: 649: 646: 644: 641: 639: 636: 633: 632: 629: 626: 624: 620: 617: 615: 612: 610: 606: 603: 601: 598: 596: 592: 591: 589: 586: 582: 577: 573: 569: 562: 557: 555: 550: 548: 543: 542: 539: 531: 527: 523: 519: 514: 509: 505: 501: 498:(1–3): 45–8. 497: 493: 489: 484: 480: 476: 471: 466: 461: 456: 452: 448: 444: 440: 436: 431: 427: 423: 419: 415: 411: 407: 402: 401: 397: 395: 393: 389: 385: 381: 377: 373: 369: 365: 357: 355: 353: 349: 345: 341: 337: 333: 329: 317: 312: 310: 306: 302: 298: 291: 287: 257:quercetin + O 256: 255: 254: 253: 249: 245: 241: 238: 234: 230: 217: 214: 212: 208: 205: 202: 200: 196: 193: 190: 188: 184: 179: 175: 172: 168: 165: 163: 162:Gene Ontology 159: 156: 153: 150: 147: 144: 140: 137: 134: 132: 128: 125: 122: 120: 116: 113: 110: 108: 104: 101: 100:NiceZyme view 98: 96: 92: 89: 86: 84: 80: 77: 74: 72: 68: 63: 60: 57: 55: 51: 48: 45: 43: 39: 34: 27: 22: 17: 1096:Iron enzymes 1046:expanding it 1032: 1024: 986:Translocases 983: 970: 957: 944: 931: 921:Transferases 918: 905: 762:Binding site 634: 595:lipoxygenase 593: 495: 491: 442: 438: 409: 405: 361: 339: 336:quercetinase 335: 331: 313: 283: 232: 226: 88:BRENDA entry 757:Active site 76:IntEnz view 36:Identifiers 1091:EC 1.13.11 1085:Categories 960:Isomerases 934:Hydrolases 801:Regulation 412:(1): 1–5. 398:References 286:substrates 240:1.13.11.24 229:enzymology 145:structures 112:KEGG entry 59:9075-67-6 47:1.13.11.24 1111:Quercetin 839:EC number 492:FEBS Lett 344:cofactors 290:quercetin 268:⇌ 248:catalyzes 65:Databases 863:Kinetics 787:Cofactor 750:Activity 530:45729959 522:14741339 479:12486225 301:products 242:) is an 216:proteins 204:articles 192:articles 149:RCSB PDB 1035:EC 1.13 1019:Biology 973:Ligases 743:Enzymes 694:: other 692:1.13.99 673:1.13.12 585:1.13.11 500:Bibcode 447:Bibcode 426:5579942 326:. The 171:QuickGO 136:profile 119:MetaCyc 54:CAS no. 1038:enzyme 1005:Portal 947:Lyases 623:ALOX15 609:ALOX12 528:  520:  477:  470:139194 467:  424:  390:, and 352:copper 307:, and 244:enzyme 199:PubMed 181:Search 167:AmiGO 155:PDBsum 95:ExPASy 83:BRENDA 71:IntEnz 42:EC no. 1033:This 899:Types 578:1.13) 526:S2CID 246:that 131:PRIAM 1042:stub 991:list 984:EC7 978:list 971:EC6 965:list 958:EC5 952:list 945:EC4 939:list 932:EC3 926:list 919:EC2 913:list 906:EC1 518:PMID 475:PMID 422:PMID 392:2H0V 388:1JUH 384:1H1M 380:1H1I 376:1GQH 372:1GQG 350:and 348:iron 338:and 292:and 250:the 231:, a 211:NCBI 152:PDBe 107:KEGG 508:doi 496:557 465:PMC 455:doi 414:doi 368:PDB 227:In 187:PMC 143:PDB 1087:: 576:EC 570:: 524:. 516:. 506:. 494:. 490:. 473:. 463:. 453:. 443:99 441:. 437:. 420:. 410:43 408:. 394:. 386:, 382:, 378:, 374:, 354:. 346:: 311:. 305:CO 237:EC 169:/ 1073:e 1066:t 1059:v 1048:. 1007:: 993:) 989:( 980:) 976:( 967:) 963:( 954:) 950:( 941:) 937:( 928:) 924:( 915:) 911:( 735:e 728:t 721:v 621:/ 607:/ 597:: 574:( 560:e 553:t 546:v 532:. 510:: 502:: 481:. 457:: 449:: 428:. 416:: 324:2 320:2 309:H 296:2 294:O 259:2 235:(

Index


EC no.
1.13.11.24
CAS no.
9075-67-6
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
Gene Ontology
AmiGO
QuickGO
PMC
articles
PubMed
articles
NCBI
proteins

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