Knowledge (XXG)

Aldehyde dehydrogenase (FAD-independent)

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991: 376:
MJ, Moura JJ; Archer, M; Dias, JM; Bursakov, S; Huber, R; Moura, I; RomĂŁo, MJ; Moura, JJ (2000). "Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774".
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Andrade SL, Brondino CD, Feio MJ, Moura I, Moura JJ (2000). "Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal cluster to the Mo site".
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RomĂŁo MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R (1995). "Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas".
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Branched-chain alpha-keto acid dehydrogenase complex
323:
has been solved for this class of enzymes, with the
875: 839: 808: 777: 726: 664: 610: 588: 566: 523: 172: 160: 148: 143: 120: 108: 96: 84: 72: 60: 48: 43: 31: 26: 21: 293:aldehyde:acceptor oxidoreductase (FAD-independent) 236: 558:Mycothiol-dependent formaldehyde dehydrogenase 1042: 704: 495: 8: 1049: 1035: 711: 697: 689: 502: 488: 480: 140: 358: 341:Fujishiro K, Aisaka K, Uwajima T (2003). 229: 196:aldehyde dehydrogenase (FAD-independent) 22:Aldehyde dehydrogenase (FAD-independent) 986: 16:Enzyme in the family of oxidoreductases 18: 283:This enzyme belongs to the family of 7: 1007: 1005: 295:. Other names in common use include 237:{\displaystyle \rightleftharpoons } 1021:. You can help Knowledge (XXG) by 624:Oxoglutarate dehydrogenase complex 580:Formate dehydrogenase (cytochrome) 14: 551:Long-chain-aldehyde dehydrogenase 989: 420:10.1046/j.1432-1327.2000.01209.x 244:a carboxylate + reduced acceptor 1: 457:10.1126/science.270.5239.1170 379:Biochem. Biophys. Res. Commun 360:10.1016/S0378-1097(03)00781-X 1094: 1073:Enzymes of known structure 1004: 546:Acetaldehyde dehydrogenase 319:As of late 2007, only one 867:Michaelis–Menten kinetics 139: 759:Diffusion-limited enzyme 291:of this enzyme class is 301:aldehyde oxidoreductase 1017:-related article is a 629:Pyruvate dehydrogenase 541:Aldehyde dehydrogenase 391:10.1006/bbrc.2000.2135 238: 852:Eadie–Hofstee diagram 785:Allosteric regulation 239: 862:Lineweaver–Burk plot 347:FEMS Microbiol. Lett 228: 670:iron–sulfur protein 449:1995Sci...270.1170R 252:of this enzyme are 821:Enzyme superfamily 754:Enzyme promiscuity 315:Structural studies 268:, whereas its two 234: 1030: 1029: 977: 976: 686: 685: 678:Pyruvate synthase 215:chemical reaction 188: 187: 184: 183: 103:metabolic pathway 1085: 1051: 1044: 1037: 1006: 994: 993: 985: 857:Hanes–Woolf plot 800:Enzyme activator 795:Enzyme inhibitor 769:Enzyme catalysis 713: 706: 699: 690: 602:Aldehyde oxidase 504: 497: 490: 481: 476: 443:(5239): 1170–6. 431: 402: 372: 362: 297:aldehyde oxidase 278:reduced acceptor 243: 241: 240: 235: 141: 19: 1093: 1092: 1088: 1087: 1086: 1084: 1083: 1082: 1058: 1057: 1056: 1055: 1002: 1000: 988: 980: 978: 973: 885:Oxidoreductases 871: 847:Enzyme kinetics 835: 831:List of enzymes 804: 773: 744:Catalytic triad 722: 717: 687: 682: 660: 606: 584: 562: 519: 512:oxidoreductases 508: 434: 408:Eur. J. Biochem 405: 375: 340: 337: 327:accession code 317: 289:systematic name 285:oxidoreductases 261: 226: 225: 223: 220:an aldehyde + H 17: 12: 11: 5: 1091: 1089: 1081: 1080: 1075: 1070: 1060: 1059: 1054: 1053: 1046: 1039: 1031: 1028: 1027: 999: 998: 975: 974: 972: 971: 958: 945: 932: 919: 906: 893: 879: 877: 873: 872: 870: 869: 864: 859: 854: 849: 843: 841: 837: 836: 834: 833: 828: 823: 818: 812: 810: 809:Classification 806: 805: 803: 802: 797: 792: 787: 781: 779: 775: 774: 772: 771: 766: 761: 756: 751: 746: 741: 736: 730: 728: 724: 723: 718: 716: 715: 708: 701: 693: 684: 683: 681: 680: 674: 672: 662: 661: 659: 658: 657: 656: 651: 646: 641: 631: 626: 620: 618: 608: 607: 605: 604: 598: 596: 586: 585: 583: 582: 576: 574: 564: 563: 561: 560: 555: 554: 553: 548: 537: 535: 521: 520: 509: 507: 506: 499: 492: 484: 478: 477: 432: 414:(7): 2054–61. 403: 373: 336: 333: 316: 313: 259: 246: 245: 233: 221: 186: 185: 182: 181: 176: 170: 169: 164: 158: 157: 152: 146: 145: 137: 136: 125: 118: 117: 112: 106: 105: 100: 94: 93: 88: 82: 81: 76: 70: 69: 64: 58: 57: 52: 46: 45: 41: 40: 35: 29: 28: 24: 23: 15: 13: 10: 9: 6: 4: 3: 2: 1090: 1079: 1076: 1074: 1071: 1069: 1066: 1065: 1063: 1052: 1047: 1045: 1040: 1038: 1033: 1032: 1026: 1024: 1020: 1016: 1013: 1008: 1003: 997: 992: 987: 983: 969: 965: 964: 959: 956: 952: 951: 946: 943: 939: 938: 933: 930: 926: 925: 920: 917: 913: 912: 907: 904: 900: 899: 894: 891: 887: 886: 881: 880: 878: 874: 868: 865: 863: 860: 858: 855: 853: 850: 848: 845: 844: 842: 838: 832: 829: 827: 826:Enzyme family 824: 822: 819: 817: 814: 813: 811: 807: 801: 798: 796: 793: 791: 790:Cooperativity 788: 786: 783: 782: 780: 776: 770: 767: 765: 762: 760: 757: 755: 752: 750: 749:Oxyanion hole 747: 745: 742: 740: 737: 735: 732: 731: 729: 725: 721: 714: 709: 707: 702: 700: 695: 694: 691: 679: 676: 675: 673: 671: 667: 663: 655: 652: 650: 647: 645: 642: 640: 637: 636: 635: 632: 630: 627: 625: 622: 621: 619: 617: 613: 609: 603: 600: 599: 597: 595: 591: 587: 581: 578: 577: 575: 573: 569: 565: 559: 556: 552: 549: 547: 544: 543: 542: 539: 538: 536: 534: 530: 526: 522: 517: 513: 510:Aldehyde/oxo 505: 500: 498: 493: 491: 486: 485: 482: 474: 470: 466: 462: 458: 454: 450: 446: 442: 438: 433: 429: 425: 421: 417: 413: 409: 404: 400: 396: 392: 388: 384: 380: 374: 370: 366: 361: 356: 352: 348: 344: 339: 338: 334: 332: 330: 326: 322: 314: 312: 310: 306: 302: 298: 294: 290: 286: 281: 279: 275: 271: 267: 263: 255: 251: 224:O + acceptor 219: 218: 217: 216: 212: 208: 204: 201: 197: 193: 180: 177: 175: 171: 168: 165: 163: 159: 156: 153: 151: 147: 142: 138: 135: 132: 129: 126: 123: 119: 116: 113: 111: 107: 104: 101: 99: 95: 92: 89: 87: 83: 80: 79:NiceZyme view 77: 75: 71: 68: 65: 63: 59: 56: 53: 51: 47: 42: 39: 36: 34: 30: 25: 20: 1078:EC 1.2 stubs 1023:expanding it 1009: 1001: 963:Translocases 960: 947: 934: 921: 908: 898:Transferases 895: 882: 739:Binding site 440: 436: 411: 407: 385:(3): 745–9. 382: 378: 350: 346: 318: 308: 304: 300: 296: 292: 282: 247: 195: 189: 67:BRENDA entry 734:Active site 353:(1): 31–6. 274:carboxylate 55:IntEnz view 27:Identifiers 1062:Categories 937:Isomerases 911:Hydrolases 778:Regulation 572:cytochrome 335:References 250:substrates 192:enzymology 124:structures 91:KEGG entry 1068:EC 1.2.99 816:EC number 616:disulfide 321:structure 232:⇌ 211:catalyzes 44:Databases 840:Kinetics 764:Cofactor 727:Activity 473:34922450 428:10727945 399:10679276 369:14659539 270:products 266:acceptor 254:aldehyde 205:) is an 203:1.2.99.7 179:proteins 167:articles 155:articles 128:RCSB PDB 38:1.2.99.7 996:Biology 950:Ligases 720:Enzymes 465:7502041 445:Bibcode 437:Science 115:profile 98:MetaCyc 1015:enzyme 1012:EC 1.2 982:Portal 924:Lyases 644:BCKDHB 639:BCKDHA 594:oxygen 471:  463:  426:  397:  367:  307:, and 264:, and 248:The 3 207:enzyme 162:PubMed 144:Search 134:PDBsum 74:ExPASy 62:BRENDA 50:IntEnz 33:EC no. 1010:This 876:Types 666:1.2.7 612:1.2.4 590:1.2.3 568:1.2.2 525:1.2.1 469:S2CID 309:AORDd 209:that 194:, an 110:PRIAM 1019:stub 968:list 961:EC7 955:list 948:EC6 942:list 935:EC5 929:list 922:EC4 916:list 909:EC3 903:list 896:EC2 890:list 883:EC1 533:NADP 518:1.2) 461:PMID 424:PMID 395:PMID 365:PMID 329:1ZCS 276:and 272:are 213:the 174:NCBI 131:PDBe 86:KEGG 654:DLD 649:DBT 531:or 529:NAD 453:doi 441:270 416:doi 412:267 387:doi 383:268 355:doi 351:229 325:PDB 305:Mop 190:In 150:PMC 122:PDB 1064:: 668:: 614:: 592:: 570:: 527:: 516:EC 467:. 459:. 451:. 439:. 422:. 410:. 393:. 381:. 363:. 349:. 345:. 331:. 311:. 303:, 299:, 280:. 256:, 200:EC 1050:e 1043:t 1036:v 1025:. 984:: 970:) 966:( 957:) 953:( 944:) 940:( 931:) 927:( 918:) 914:( 905:) 901:( 892:) 888:( 712:e 705:t 698:v 514:( 503:e 496:t 489:v 475:. 455:: 447:: 430:. 418:: 401:. 389:: 371:. 357:: 262:O 260:2 258:H 222:2 198:(

Index

EC no.
1.2.99.7
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
enzymology
EC
1.2.99.7
enzyme
catalyzes
chemical reaction

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