Knowledge (XXG)

Tryptophanase

Source đź“ť

1123: 539: 301: 29: 284: 424:
Cowell JL, Maser K, DeMoss, RD (1973). "Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties".
571: 194: 213: 1180: 666: 690: 564: 1204: 773: 1214: 671: 621: 695: 557: 842: 656: 686: 611: 206: 661: 718: 157: 133: 998: 1173: 426: 1113: 740: 521: 509: 493: 1209: 651: 606: 983: 1099: 1086: 1073: 1060: 1047: 1034: 1021: 783: 755: 705: 641: 594: 993: 151: 1166: 947: 890: 807: 585: 543: 238: 44: 138: 895: 646: 631: 626: 345: 676: 616: 269: 218: 1219: 916: 835: 337: 126: 988: 636: 61: 952: 349: 341: 154: 56: 78: 1199: 885: 745: 365: 497: 476: 406: 369: 249: 145: 1150: 931: 926: 900: 828: 768: 466: 435: 398: 114: 978: 962: 875: 312: 90: 241: 49: 1127: 1016: 957: 598: 189: 471: 454: 169: 1193: 921: 880: 439: 402: 164: 870: 389:
BURNS RO, DEMOSS RD (1962). "Properties of tryptophanase from Escherichia coli".
1094: 1029: 865: 549: 173: 1122: 797: 733: 728: 723: 259: 1068: 1042: 802: 353: 245: 480: 410: 538: 709: 290: 102: 759: 681: 121: 311:, specifically in the "catch-all" class of carbon-carbon lyases. The 1146: 1143: 1081: 851: 286: 231: 201: 97: 85: 73: 1055: 581: 308: 300: 109: 824: 553: 28: 299: 820: 320:-tryptophan indole-lyase (deaminating; pyruvate-forming) 273: 1154: 1111: 272: 1007: 971: 940: 909: 858: 782: 754: 704: 593: 212: 200: 188: 183: 163: 144: 132: 120: 108: 96: 84: 72: 67: 55: 43: 38: 21: 278: 368:have been solved for this class of enzymes, with 1174: 836: 565: 8: 16:Enzyme that converts tryptophan into indole 1181: 1167: 843: 829: 821: 572: 558: 550: 180: 470: 455:"Properties of Crystalline Tryptophanase" 271: 667:Phosphoribosylaminoimidazole carboxylase 1118: 381: 524:Retrieved from Protein Data Bank (PDB) 512:Retrieved from Protein Data Bank (PDB) 453:NEWTON WA, MORINO Y, SNELL EE (1965). 372:accession codes 1AX4, 2C44, and 2OQX. 334:-tryptophan indole-lyase (deaminating) 18: 307:This enzyme belongs to the family of 7: 1139: 1137: 774:3-hydroxy-3-methylglutaryl-CoA lyase 691:Orotidine 5'-phosphate decarboxylase 322:. Other names in common use include 672:Pyrophosphomevalonate decarboxylase 622:Aromatic L-amino acid decarboxylase 279:{\displaystyle \rightleftharpoons } 1153:. You can help Knowledge (XXG) by 696:Uroporphyrinogen III decarboxylase 14: 657:Phosphoenolpyruvate carboxykinase 1121: 687:Uridine monophosphate synthetase 612:Adenosylmethionine decarboxylase 537: 27: 662:Phosphoenolpyruvate carboxylase 336:. This enzyme participates in 719:Fructose-bisphosphate aldolase 33:Tryptophanase tetramer, E.Coli 1: 472:10.1016/S0021-9258(18)97562-9 427:Biochimica et Biophysica Acta 741:2-hydroxyphytanoyl-CoA lyase 440:10.1016/0005-2744(73)90276-3 403:10.1016/0006-3002(62)91042-9 1205:Pyridoxal phosphate enzymes 1236: 1215:Enzymes of known structure 1136: 652:Oxaloacetate decarboxylase 607:Acetoacetate decarboxylase 999:Michaelis–Menten kinetics 642:Malonyl-CoA decarboxylase 179: 26: 891:Diffusion-limited enzyme 808:Spore photoproduct lyase 315:of this enzyme class is 647:Ornithine decarboxylase 632:Histidine decarboxylase 627:Glutamate decarboxylase 1149:-related article is a 677:Pyruvate decarboxylase 617:Arginine decarboxylase 391:Biochim. Biophys. Acta 304: 280: 984:Eadie–Hofstee diagram 917:Allosteric regulation 338:tryptophan metabolism 303: 281: 994:Lineweaver–Burk plot 637:Lysine decarboxylase 546:at Wikimedia Commons 270: 364:As of late 2007, 3 350:pyridoxal phosphate 342:nitrogen metabolism 953:Enzyme superfamily 886:Enzyme promiscuity 746:Threonine aldolase 360:Structural studies 305: 276: 1210:Potassium enzymes 1162: 1161: 1109: 1108: 818: 817: 542:Media related to 498:Protein Data Bank 333: 326: 319: 257: 250:chemical reaction 228: 227: 224: 223: 127:metabolic pathway 1227: 1183: 1176: 1169: 1138: 1126: 1125: 1117: 989:Hanes–Woolf plot 932:Enzyme activator 927:Enzyme inhibitor 901:Enzyme catalysis 845: 838: 831: 822: 769:Isocitrate lyase 574: 567: 560: 551: 541: 525: 519: 513: 507: 501: 491: 485: 484: 474: 450: 444: 443: 421: 415: 414: 386: 331: 324: 317: 285: 283: 282: 277: 255: 181: 31: 19: 1235: 1234: 1230: 1229: 1228: 1226: 1225: 1224: 1190: 1189: 1188: 1187: 1134: 1132: 1120: 1112: 1110: 1105: 1017:Oxidoreductases 1003: 979:Enzyme kinetics 967: 963:List of enzymes 936: 905: 876:Catalytic triad 854: 849: 819: 814: 778: 750: 700: 589: 578: 534: 529: 528: 520: 516: 508: 504: 496:Retrieved from 492: 488: 452: 451: 447: 423: 422: 418: 388: 387: 383: 378: 362: 313:systematic name 296: 268: 267: 265: 34: 17: 12: 11: 5: 1233: 1231: 1223: 1222: 1217: 1212: 1207: 1202: 1192: 1191: 1186: 1185: 1178: 1171: 1163: 1160: 1159: 1131: 1130: 1107: 1106: 1104: 1103: 1090: 1077: 1064: 1051: 1038: 1025: 1011: 1009: 1005: 1004: 1002: 1001: 996: 991: 986: 981: 975: 973: 969: 968: 966: 965: 960: 955: 950: 944: 942: 941:Classification 938: 937: 935: 934: 929: 924: 919: 913: 911: 907: 906: 904: 903: 898: 893: 888: 883: 878: 873: 868: 862: 860: 856: 855: 850: 848: 847: 840: 833: 825: 816: 815: 813: 812: 811: 810: 805: 795: 789: 787: 780: 779: 777: 776: 771: 765: 763: 752: 751: 749: 748: 743: 738: 737: 736: 731: 726: 715: 713: 702: 701: 699: 698: 693: 684: 679: 674: 669: 664: 659: 654: 649: 644: 639: 634: 629: 624: 619: 614: 609: 603: 601: 599:Carboxy-lyases 591: 590: 580:Carbon–carbon 579: 577: 576: 569: 562: 554: 548: 547: 533: 532:External links 530: 527: 526: 514: 502: 486: 445: 416: 380: 379: 377: 374: 361: 358: 327:-tryptophanase 298: 297: 294: 275: 263: 226: 225: 222: 221: 216: 210: 209: 204: 198: 197: 192: 186: 185: 177: 176: 167: 161: 160: 149: 142: 141: 136: 130: 129: 124: 118: 117: 112: 106: 105: 100: 94: 93: 88: 82: 81: 76: 70: 69: 65: 64: 59: 53: 52: 47: 41: 40: 36: 35: 32: 24: 23: 15: 13: 10: 9: 6: 4: 3: 2: 1232: 1221: 1218: 1216: 1213: 1211: 1208: 1206: 1203: 1201: 1198: 1197: 1195: 1184: 1179: 1177: 1172: 1170: 1165: 1164: 1158: 1156: 1152: 1148: 1145: 1140: 1135: 1129: 1124: 1119: 1115: 1101: 1097: 1096: 1091: 1088: 1084: 1083: 1078: 1075: 1071: 1070: 1065: 1062: 1058: 1057: 1052: 1049: 1045: 1044: 1039: 1036: 1032: 1031: 1026: 1023: 1019: 1018: 1013: 1012: 1010: 1006: 1000: 997: 995: 992: 990: 987: 985: 982: 980: 977: 976: 974: 970: 964: 961: 959: 958:Enzyme family 956: 954: 951: 949: 946: 945: 943: 939: 933: 930: 928: 925: 923: 922:Cooperativity 920: 918: 915: 914: 912: 908: 902: 899: 897: 894: 892: 889: 887: 884: 882: 881:Oxyanion hole 879: 877: 874: 872: 869: 867: 864: 863: 861: 857: 853: 846: 841: 839: 834: 832: 827: 826: 823: 809: 806: 804: 801: 800: 799: 796: 794: 793:Tryptophanase 791: 790: 788: 785: 781: 775: 772: 770: 767: 766: 764: 761: 757: 753: 747: 744: 742: 739: 735: 732: 730: 727: 725: 722: 721: 720: 717: 716: 714: 711: 707: 703: 697: 694: 692: 688: 685: 683: 680: 678: 675: 673: 670: 668: 665: 663: 660: 658: 655: 653: 650: 648: 645: 643: 640: 638: 635: 633: 630: 628: 625: 623: 620: 618: 615: 613: 610: 608: 605: 604: 602: 600: 596: 592: 587: 583: 575: 570: 568: 563: 561: 556: 555: 552: 545: 544:Tryptophanase 540: 536: 535: 531: 523: 518: 515: 511: 506: 503: 499: 495: 490: 487: 482: 478: 473: 468: 465:(3): 1211–8. 464: 460: 459:J. Biol. Chem 456: 449: 446: 441: 437: 433: 429: 428: 420: 417: 412: 408: 404: 400: 397:(2): 233–44. 396: 392: 385: 382: 375: 373: 371: 367: 359: 357: 355: 351: 347: 343: 339: 335: 328: 321: 314: 310: 302: 292: 288: 261: 254: 253: 252: 251: 247: 243: 240: 236: 235:tryptophanase 233: 220: 217: 215: 211: 208: 205: 203: 199: 196: 193: 191: 187: 182: 178: 175: 171: 168: 166: 165:Gene Ontology 162: 159: 156: 153: 150: 147: 143: 140: 137: 135: 131: 128: 125: 123: 119: 116: 113: 111: 107: 104: 103:NiceZyme view 101: 99: 95: 92: 89: 87: 83: 80: 77: 75: 71: 66: 63: 60: 58: 54: 51: 48: 46: 42: 37: 30: 25: 22:tryptophanase 20: 1220:EC 4.1 stubs 1155:expanding it 1141: 1133: 1095:Translocases 1092: 1079: 1066: 1053: 1040: 1030:Transferases 1027: 1014: 871:Binding site 792: 517: 505: 489: 462: 458: 448: 431: 425: 419: 394: 390: 384: 363: 344:. It has 2 330: 323: 316: 306: 234: 229: 91:BRENDA entry 866:Active site 434:: 449–463. 79:IntEnz view 39:Identifiers 1194:Categories 1069:Isomerases 1043:Hydrolases 910:Regulation 798:Photolyase 734:Aldolase C 729:Aldolase B 724:Aldolase A 376:References 366:structures 260:tryptophan 148:structures 115:KEGG entry 62:9024-00-4 1200:EC 4.1.99 948:EC number 803:CPD lyase 354:potassium 346:cofactors 274:⇌ 246:catalyzes 68:Databases 972:Kinetics 896:Cofactor 859:Activity 760:Oxo-acid 710:Aldehyde 481:14284727 411:14017164 291:pyruvate 242:4.1.99.1 219:proteins 207:articles 195:articles 152:RCSB PDB 50:4.1.99.1 1128:Biology 1082:Ligases 852:Enzymes 786:: Other 762:-lyases 712:-lyases 682:RuBisCO 352:, and 174:QuickGO 139:profile 122:MetaCyc 57:CAS no. 1147:enzyme 1144:EC 4.1 1114:Portal 1056:Lyases 784:4.1.99 582:lyases 479:  409:  329:, and 309:lyases 287:indole 232:enzyme 202:PubMed 184:Search 170:AmiGO 158:PDBsum 98:ExPASy 86:BRENDA 74:IntEnz 45:EC no. 1142:This 1008:Types 756:4.1.3 706:4.1.2 595:4.1.1 500:(PDB) 134:PRIAM 1151:stub 1100:list 1093:EC7 1087:list 1080:EC6 1074:list 1067:EC5 1061:list 1054:EC4 1048:list 1041:EC3 1035:list 1028:EC2 1022:list 1015:EC1 588:4.1) 522:2OQX 510:2C44 494:1AX4 477:PMID 407:PMID 340:and 293:+ NH 248:the 230:The 214:NCBI 155:PDBe 110:KEGG 467:doi 463:240 436:doi 432:315 399:doi 370:PDB 262:+ H 190:PMC 146:PDB 1196:: 758:: 708:: 597:: 586:EC 475:. 461:. 457:. 430:. 405:. 395:65 393:. 356:. 348:: 289:+ 266:O 244:) 239:EC 172:/ 1182:e 1175:t 1168:v 1157:. 1116:: 1102:) 1098:( 1089:) 1085:( 1076:) 1072:( 1063:) 1059:( 1050:) 1046:( 1037:) 1033:( 1024:) 1020:( 844:e 837:t 830:v 689:/ 584:( 573:e 566:t 559:v 483:. 469:: 442:. 438:: 413:. 401:: 332:L 325:L 318:L 295:3 264:2 258:- 256:L 237:(

Index


EC no.
4.1.99.1
CAS no.
9024-00-4
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

Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.

↑