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Ammonia monooxygenase

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1405: 266:. AMO is the first enzyme in ammonia oxidation. Aerobic oxidation of ammonia to hydroxylamine via AMO is an endergonic reaction. So, all aerobic ammonia oxidizing organisms conserve energy by further oxidizing hydroxylamine. It was believed that aerobic ammonia-oxidizing bacteria oxidize hydroxylamine to nitrite using octahaem 244: 151: 170: 882: 775: 336:
Bergmann DJ, Hooper AB (October 1994). "Sequence of the gene, amoB, for the 43-kDa polypeptide of ammonia monoxygenase of Nitrosomonas europaea".
270:(HAO). Recently, it was shown that the product of HAO is not nitrite but nitric oxide, which is further oxidized to nitrite by an unknown enzyme. 950: 689: 535:
Arp DJ, Sayavedra-Soto LA, Hommes NG (October 2002). "Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea".
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Gilch S, Meyer O, Schmidt I (September 2009). "A soluble form of ammonia monooxygenase in Nitrosomonas europaea".
124: 1381: 1368: 1355: 1342: 1329: 1316: 1303: 1086: 1047: 1037: 1023: 1019: 1009: 997: 977: 960: 928: 892: 792: 719: 1275: 1229: 1172: 710: 661: 191: 111: 29: 932: 1177: 723: 496:"Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea" 175: 1071: 987: 736: 99: 373:"Evidence that particulate methane monooxygenase and ammonia monooxygenase may be evolutionarily related" 229: 1198: 1117: 867: 840: 675: 607:"Oxidation of monohalogenated ethanes and n-chlorinated alkanes by whole cells of Nitrosomonas europaea" 1270: 982: 945: 706: 127: 51: 1425: 1234: 968: 289:"Oxidation of methyl fluoride and dimethyl ether by ammonia monooxygenase in Nitrosomonas europaea" 1167: 731: 657: 877: 765: 636: 587: 552: 517: 476: 435: 394: 353: 318: 210: 118: 87: 1213: 1208: 1182: 1110: 626: 618: 579: 544: 507: 466: 425: 384: 345: 308: 300: 63: 1260: 1244: 1157: 855: 34: 1409: 1298: 1239: 1081: 1061: 1056: 698: 389: 372: 146: 631: 606: 512: 495: 430: 413: 313: 288: 1419: 1203: 1162: 471: 454: 414:"Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea" 622: 304: 1152: 900: 896: 1376: 1311: 1147: 1404: 1032: 548: 1350: 1324: 1001: 964: 908: 702: 206: 591: 556: 521: 349: 640: 480: 439: 398: 357: 322: 194: 75: 780: 455:"The purification of ammonia monooxygenase from Paracoccus denitrificans" 583: 1076: 216: 94: 1363: 1133: 918: 913: 872: 259: 202: 158: 70: 58: 46: 1337: 1065: 800: 758: 751: 746: 741: 845: 833: 828: 818: 813: 796: 770: 263: 82: 1106: 671: 371:
Holmes AJ, Costello A, Lidstrom ME, Murrell JC (October 1995).
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Zahn JA, Arciero DM, Hooper AB, DiSpirito AA (November 1996).
494:
Whittaker M, Bergmann D, Arciero D, Hooper AB (August 2000).
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Moir JW, Crossman LC, Spiro S, Richardson DJ (May 1996).
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Rasche ME, Hicks RE, Hyman MR, Arp DJ (September 1990).
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Biochimica et Biophysica Acta (BBA) - Bioenergetics
338:
Biochemical and Biophysical Research Communications
169: 157: 145: 140: 117: 105: 93: 81: 69: 57: 45: 40: 28: 23: 18: 238: 1118: 683: 8: 1125: 1111: 1103: 690: 676: 668: 137: 660:at the U.S. National Library of Medicine 630: 511: 470: 429: 388: 312: 287:Hyman MR, Page CL, Arp DJ (August 1994). 231: 1400: 279: 293:Applied and Environmental Microbiology 15: 7: 883:24-hydroxycholesterol 7α-hydroxylase 239:{\displaystyle \rightleftharpoons } 390:10.1111/j.1574-6968.1995.tb07834.x 14: 1403: 863:Cholesterol 7 alpha-hydroxylase 809:Flavin-containing monooxygenase 623:10.1128/jb.172.9.5368-5373.1990 305:10.1128/AEM.60.8.3033-3035.1994 258:Ammonia monooxygenase contains 1: 513:10.1016/s0005-2728(00)00171-7 431:10.1016/s0014-5793(96)01116-7 472:10.1016/0014-5793(96)00463-2 268:hydroxylamine oxidoreductase 1092:Deoxyhypusine monooxygenase 1442: 1281:Michaelis–Menten kinetics 1087:Ecdysone 20-monooxygenase 1038:Stearoyl-CoA desaturase-1 1010:Dopamine beta-hydroxylase 978:Phenylalanine hydroxylase 549:10.1007/s00203-002-0452-0 377:FEMS Microbiology Letters 136: 1173:Diffusion-limited enzyme 662:Medical Subject Headings 537:Archives of Microbiology 611:Journal of Bacteriology 1072:Squalene monooxygenase 988:Tryptophan hydroxylase 737:HIF prolyl-hydroxylase 350:10.1006/bbrc.1994.2524 240: 1266:Eadie–Hofstee diagram 1199:Allosteric regulation 868:Methane monooxygenase 841:Nitric oxide synthase 658:Ammonia+monooxygenase 262:and possibly nonheme 241: 188:Ammonia monooxygenase 19:Ammonia monooxygenase 1276:Lineweaver–Burk plot 983:Tyrosine hydroxylase 707:steroid hydroxylases 572:Biological Chemistry 230: 933:iron–sulfur protein 584:10.1515/BC.2009.085 1235:Enzyme superfamily 1168:Enzyme promiscuity 732:Prolyl hydroxylase 236: 1391: 1390: 1100: 1099: 766:Lysyl hydroxylase 211:chemical reaction 185: 184: 181: 180: 100:metabolic pathway 1433: 1408: 1407: 1399: 1271:Hanes–Woolf plot 1214:Enzyme activator 1209:Enzyme inhibitor 1183:Enzyme catalysis 1127: 1120: 1113: 1104: 692: 685: 678: 669: 645: 644: 634: 602: 596: 595: 567: 561: 560: 532: 526: 525: 515: 491: 485: 484: 474: 450: 444: 443: 433: 409: 403: 402: 392: 368: 362: 361: 333: 327: 326: 316: 284: 245: 243: 242: 237: 138: 16: 1441: 1440: 1436: 1435: 1434: 1432: 1431: 1430: 1416: 1415: 1414: 1402: 1394: 1392: 1387: 1299:Oxidoreductases 1285: 1261:Enzyme kinetics 1249: 1245:List of enzymes 1218: 1187: 1158:Catalytic triad 1136: 1131: 1101: 1096: 1050:- miscellaneous 1042: 1014: 992: 955: 923: 887: 878:14α-demethylase 787: 714: 699:Oxidoreductases 696: 654: 649: 648: 604: 603: 599: 569: 568: 564: 534: 533: 529: 506:(2–3): 346–55. 493: 492: 488: 452: 451: 447: 411: 410: 406: 370: 369: 365: 335: 334: 330: 286: 285: 281: 276: 253: 249: 228: 227: 226: 222: 12: 11: 5: 1439: 1437: 1429: 1428: 1418: 1417: 1413: 1412: 1389: 1388: 1386: 1385: 1372: 1359: 1346: 1333: 1320: 1307: 1293: 1291: 1287: 1286: 1284: 1283: 1278: 1273: 1268: 1263: 1257: 1255: 1251: 1250: 1248: 1247: 1242: 1237: 1232: 1226: 1224: 1223:Classification 1220: 1219: 1217: 1216: 1211: 1206: 1201: 1195: 1193: 1189: 1188: 1186: 1185: 1180: 1175: 1170: 1165: 1160: 1155: 1150: 1144: 1142: 1138: 1137: 1132: 1130: 1129: 1122: 1115: 1107: 1098: 1097: 1095: 1094: 1089: 1084: 1079: 1074: 1069: 1062:Heme oxygenase 1059: 1057:Cyclooxygenase 1053: 1051: 1044: 1043: 1041: 1040: 1035: 1029: 1027: 1016: 1015: 1013: 1012: 1006: 1004: 994: 993: 991: 990: 985: 980: 974: 972: 957: 956: 954: 953: 948: 943: 937: 935: 925: 924: 922: 921: 916: 911: 905: 903: 889: 888: 886: 885: 880: 875: 870: 865: 860: 859: 858: 853: 848: 838: 837: 836: 831: 826: 821: 816: 805: 803: 789: 788: 786: 785: 784: 783: 778: 768: 763: 762: 761: 756: 755: 754: 749: 744: 728: 726: 724:2-oxoglutarate 716: 715: 697: 695: 694: 687: 680: 672: 666: 665: 653: 652:External links 650: 647: 646: 617:(9): 5368–73. 597: 562: 527: 486: 445: 404: 363: 328: 278: 277: 275: 272: 256: 255: 251: 247: 235: 224: 220: 209:the following 183: 182: 179: 178: 173: 167: 166: 161: 155: 154: 149: 143: 142: 134: 133: 122: 115: 114: 109: 103: 102: 97: 91: 90: 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981: 979: 976: 975: 973: 970: 969:BH4 dependent 966: 962: 958: 952: 949: 947: 944: 942: 939: 938: 936: 934: 930: 926: 920: 917: 915: 912: 910: 907: 906: 904: 902: 898: 894: 890: 884: 881: 879: 876: 874: 871: 869: 866: 864: 861: 857: 854: 852: 849: 847: 844: 843: 842: 839: 835: 832: 830: 827: 825: 822: 820: 817: 815: 812: 811: 810: 807: 806: 804: 802: 798: 794: 790: 782: 779: 777: 774: 773: 772: 769: 767: 764: 760: 757: 753: 750: 748: 745: 743: 740: 739: 738: 735: 734: 733: 730: 729: 727: 725: 721: 717: 712: 708: 704: 700: 693: 688: 686: 681: 679: 674: 673: 670: 663: 659: 656: 655: 651: 642: 638: 633: 628: 624: 620: 616: 612: 608: 601: 598: 593: 589: 585: 581: 578:(9): 863–73. 577: 573: 566: 563: 558: 554: 550: 546: 542: 538: 531: 528: 523: 519: 514: 509: 505: 501: 497: 490: 487: 482: 478: 473: 468: 464: 460: 456: 449: 446: 441: 437: 432: 427: 423: 419: 415: 408: 405: 400: 396: 391: 386: 382: 378: 374: 367: 364: 359: 355: 351: 347: 344:(2): 759–62. 343: 339: 332: 329: 324: 320: 315: 310: 306: 302: 299:(8): 3033–5. 298: 294: 290: 283: 280: 273: 271: 269: 265: 261: 218: 215: 214: 213: 212: 208: 204: 200: 196: 193: 189: 177: 174: 172: 168: 165: 162: 160: 156: 153: 150: 148: 144: 139: 135: 132: 129: 126: 123: 120: 116: 113: 110: 108: 104: 101: 98: 96: 92: 89: 86: 84: 80: 77: 76:NiceZyme view 74: 72: 68: 65: 62: 60: 56: 53: 50: 48: 44: 39: 36: 33: 31: 27: 22: 17: 1377:Translocases 1374: 1361: 1348: 1335: 1322: 1312:Transferases 1309: 1296: 1153:Binding site 901:flavoprotein 705:, including 703:dioxygenases 614: 610: 600: 575: 571: 565: 543:(4): 250–5. 540: 536: 530: 503: 499: 489: 462: 459:FEBS Letters 458: 448: 421: 418:FEBS Letters 417: 407: 383:(3): 203–8. 380: 376: 366: 341: 337: 331: 296: 292: 282: 257: 198: 187: 186: 64:BRENDA entry 1148:Active site 465:(1): 71–4. 424:(1): 35–8. 52:IntEnz view 24:Identifiers 1426:EC 1.14.99 1351:Isomerases 1325:Hydrolases 1192:Regulation 1033:Tyrosinase 1000:: reduced 963:: reduced 931:: reduced 895:: reduced 274:References 250:OH + A + H 195:1.14.99.39 121:structures 88:KEGG entry 35:1.14.99.39 1230:EC number 1002:ascorbate 965:pteridine 234:⇌ 207:catalyses 41:Databases 1420:Category 1254:Kinetics 1178:Cofactor 1141:Activity 592:19453274 557:12209257 522:11004450 205:, which 201:) is an 176:proteins 164:articles 152:articles 125:RCSB PDB 1410:Biology 1364:Ligases 1134:Enzymes 1048:1.14.99 1026:: other 1020:1.14.18 998:1.14.17 961:1.14.16 929:1.14.15 893:1.14.14 793:1.14.13 720:1.14.11 641:2394686 481:8654570 440:8941709 399:7590173 358:7980540 323:8085841 217:ammonia 112:profile 95:MetaCyc 1396:Portal 1338:Lyases 897:flavin 776:ALKBH1 664:(MeSH) 639:  632:213201 629:  590:  555:  520:  479:  438:  397:  356:  321:  314:201762 311:  260:copper 203:enzyme 159:PubMed 141:Search 131:PDBsum 71:ExPASy 59:BRENDA 47:IntEnz 30:EC no. 1290:Types 1066:HMOX1 801:NADPH 759:P4HTM 752:EGLN3 747:EGLN2 742:EGLN1 713:1.14) 107:PRIAM 1382:list 1375:EC7 1369:list 1362:EC6 1356:list 1349:EC5 1343:list 1336:EC4 1330:list 1323:EC3 1317:list 1310:EC2 1304:list 1297:EC1 1082:21A2 1077:17A1 951:11A1 946:11B2 941:11B1 909:19A1 856:NOS3 851:NOS2 846:NOS1 834:FMO5 829:FMO4 824:FMO3 819:FMO2 814:FMO1 797:NADH 771:AlkB 637:PMID 588:PMID 553:PMID 518:PMID 504:1459 477:PMID 436:PMID 395:PMID 354:PMID 319:PMID 264:iron 219:+ AH 171:NCBI 128:PDBe 83:KEGG 919:2E1 914:2D6 899:or 873:3A4 799:or 781:FTO 627:PMC 619:doi 615:172 580:doi 576:390 545:doi 541:178 508:doi 467:doi 463:387 426:doi 422:397 385:doi 381:132 346:doi 342:204 309:PMC 301:doi 223:+ O 199:AMO 147:PMC 119:PDB 1422:: 1024:19 795:: 722:: 711:EC 701:: 635:. 625:. 613:. 609:. 586:. 574:. 551:. 539:. 516:. 502:. 498:. 475:. 461:. 457:. 434:. 420:. 416:. 393:. 379:. 375:. 352:. 340:. 317:. 307:. 297:60 295:. 291:. 246:NH 197:, 192:EC 1398:: 1384:) 1380:( 1371:) 1367:( 1358:) 1354:( 1345:) 1341:( 1332:) 1328:( 1319:) 1315:( 1306:) 1302:( 1126:e 1119:t 1112:v 1068:) 1064:( 1022:- 971:) 967:( 709:( 691:e 684:t 677:v 643:. 621:: 594:. 582:: 559:. 547:: 524:. 510:: 483:. 469:: 442:. 428:: 401:. 387:: 360:. 348:: 325:. 303:: 254:O 252:2 248:2 225:2 221:2 190:(

Index

EC no.
1.14.99.39
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
1.14.99.39
enzyme
catalyses
chemical reaction
ammonia

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