Knowledge (XXG)

Aspartate-semialdehyde dehydrogenase

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which plays an essential role in bacterial cell wall formation. There is particular interest in ASADH as disabling this enzyme proves fatal to the organism giving rise to the possibility of a new class of antibiotics, fungicides, and herbicides aimed at inhibiting it.
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that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. This pathway also produces
802: 290: 934: 511: 194: 858: 213: 833: 564: 330: 315: 795: 1349: 708:"Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis" 788: 1378: 924: 880: 1011: 851: 829: 1373: 206: 954: 777:
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
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biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various
402: 275: 218: 1383: 1085: 1004: 344:, specifically those acting on the aldehyde or oxo group of a donor with NAD+ or NADP+ as acceptor. The 126: 1157: 515: 61: 1121: 319: 154: 56: 78: 1054: 587: 1368: 978: 766: 727: 591: 506: 263: 145: 1319: 1100: 1095: 1069: 997: 902: 756: 719: 498: 114: 1147: 1131: 1044: 578:. All proteins in this entry contain a dimerisation domain of semialdehyde dehydrogenase. 345: 251: 90: 780: 49: 1296: 1185: 1126: 812: 341: 337:. However, under physiological conditions the reaction runs in the opposite direction. 189: 761: 744: 169: 1362: 1090: 1049: 406: 164: 447: 1039: 575: 494: 334: 460: 472: 1263: 1198: 1034: 552: 173: 1291: 949: 872: 231: 1237: 1211: 916: 556: 391: 311: 259: 770: 731: 723: 707: 410: 547:-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in 745:"Aspartic beta-semialdehyde dehydrogenase and aspartic beta-semialdehyde" 572: 548: 467: 242: 102: 383: 121: 1315: 1312: 1250: 1020: 944: 939: 894: 560: 526: 395: 387: 246: 201: 97: 85: 73: 706:
Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R (1999).
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Aspartate semialdehyde dehydrogenase tetramer, Trichophyton rubrum
488: 454: 442: 353:-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating) 109: 993: 784: 28: 16:
Amino-acid-synthesizing enzyme in fungi, plants and prokaryota
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Branched-chain alpha-keto acid dehydrogenase complex
1176: 1140: 1109: 1078: 1027: 965: 911: 889: 867: 824: 525: 505: 487: 482: 466: 453: 441: 433: 428: 423: 212: 200: 188: 183: 163: 144: 132: 120: 108: 96: 84: 72: 67: 55: 43: 38: 21: 563:Arg5,6 protein, which is cleaved into the enzymes 284: 590:have been solved for this class of enzymes, with 368:-aspartate-beta-semialdehyde:NADP+ oxidoreductase 424:Semialdehyde dehydrogenase, dimerisation domain 859:Mycothiol-dependent formaldehyde dehydrogenase 1343: 1005: 796: 272:-aspartate 4-semialdehyde + phosphate + NADP 8: 401:Aspartate-semialdehyde dehydrogenase may be 565:N-acetyl-gamma-glutamyl-phosphate reductase 1350: 1336: 1012: 998: 990: 803: 789: 781: 479: 180: 760: 277: 376:aspartic beta-semialdehyde dehydrogenase 1287: 698: 420: 18: 340:This enzyme belongs to the family of 7: 1308: 1306: 357:aspartate semialdehyde dehydrogenase 355:. Other names in common use include 236:aspartate-semialdehyde dehydrogenase 22:aspartate-semialdehyde dehydrogenase 361:aspartic semialdehyde dehydrogenase 285:{\displaystyle \rightleftharpoons } 1322:. You can help Knowledge (XXG) by 925:Oxoglutarate dehydrogenase complex 881:Formate dehydrogenase (cytochrome) 14: 852:Long-chain-aldehyde dehydrogenase 559:. It also contains the yeast and 295:-4-aspartyl phosphate + NADPH + H 1290: 27: 382:. This enzyme participates in 1: 762:10.1016/S0021-9258(18)71042-9 571:. These are also involved in 483:Available protein structures: 743:BLACK S, WRIGHT NG (1955). 1400: 1379:Enzymes of known structure 1305: 847:Acetaldehyde dehydrogenase 543:This domain contains both 1168:Michaelis–Menten kinetics 478: 308:-aspartate 4-semialdehyde 179: 26: 1060:Diffusion-limited enzyme 348:of this enzyme class is 1374:NADPH-dependent enzymes 1318:-related article is a 930:Pyruvate dehydrogenase 842:Aldehyde dehydrogenase 724:10.1006/jmbi.1999.2828 569:acetylglutamate kinase 286: 1153:Eadie–Hofstee diagram 1086:Allosteric regulation 327:-4-aspartyl phosphate 287: 1163:Lineweaver–Burk plot 586:As of late 2007, 24 276: 971:iron–sulfur protein 413:of some Asd genes. 396:lysine biosynthesis 303:of this enzyme are 1122:Enzyme superfamily 1055:Enzyme promiscuity 582:Structural studies 282: 1331: 1330: 1278: 1277: 987: 986: 979:Pyruvate synthase 541: 540: 537: 536: 532:structure summary 380:ASA dehydrogenase 372:(phosphorylating) 367: 352: 326: 307: 294: 271: 264:chemical reaction 228: 227: 224: 223: 127:metabolic pathway 1391: 1352: 1345: 1338: 1307: 1295: 1294: 1286: 1158:Hanes–Woolf plot 1101:Enzyme activator 1096:Enzyme inhibitor 1070:Enzyme catalysis 1014: 1007: 1000: 991: 903:Aldehyde oxidase 805: 798: 791: 782: 774: 764: 736: 735: 703: 594:accession codes 480: 421: 417:Protein families 365: 350: 324: 318:, whereas its 3 305: 292: 291: 289: 288: 283: 269: 181: 31: 19: 1399: 1398: 1394: 1393: 1392: 1390: 1389: 1388: 1359: 1358: 1357: 1356: 1303: 1301: 1289: 1281: 1279: 1274: 1186:Oxidoreductases 1172: 1148:Enzyme kinetics 1136: 1132:List of enzymes 1105: 1074: 1045:Catalytic triad 1023: 1018: 988: 983: 961: 907: 885: 863: 820: 813:oxidoreductases 809: 742: 739: 718:(4): 991–1002. 705: 704: 700: 696: 584: 437:Semialdhyde_dhC 419: 394:metabolism and 346:systematic name 342:oxidoreductases 274: 273: 262:the reversible 252:diaminopimelate 34: 17: 12: 11: 5: 1397: 1395: 1387: 1386: 1381: 1376: 1371: 1361: 1360: 1355: 1354: 1347: 1340: 1332: 1329: 1328: 1300: 1299: 1276: 1275: 1273: 1272: 1259: 1246: 1233: 1220: 1207: 1194: 1180: 1178: 1174: 1173: 1171: 1170: 1165: 1160: 1155: 1150: 1144: 1142: 1138: 1137: 1135: 1134: 1129: 1124: 1119: 1113: 1111: 1110:Classification 1107: 1106: 1104: 1103: 1098: 1093: 1088: 1082: 1080: 1076: 1075: 1073: 1072: 1067: 1062: 1057: 1052: 1047: 1042: 1037: 1031: 1029: 1025: 1024: 1019: 1017: 1016: 1009: 1002: 994: 985: 984: 982: 981: 975: 973: 963: 962: 960: 959: 958: 957: 952: 947: 942: 932: 927: 921: 919: 909: 908: 906: 905: 899: 897: 887: 886: 884: 883: 877: 875: 865: 864: 862: 861: 856: 855: 854: 849: 838: 836: 822: 821: 810: 808: 807: 800: 793: 785: 779: 778: 775: 738: 737: 697: 695: 692: 583: 580: 539: 538: 535: 534: 529: 523: 522: 509: 503: 502: 492: 485: 484: 476: 475: 470: 464: 463: 458: 451: 450: 445: 439: 438: 435: 431: 430: 426: 425: 418: 415: 297: 296: 281: 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: 1396: 1385: 1382: 1380: 1377: 1375: 1372: 1370: 1367: 1366: 1364: 1353: 1348: 1346: 1341: 1339: 1334: 1333: 1327: 1325: 1321: 1317: 1314: 1309: 1304: 1298: 1293: 1288: 1284: 1270: 1266: 1265: 1260: 1257: 1253: 1252: 1247: 1244: 1240: 1239: 1234: 1231: 1227: 1226: 1221: 1218: 1214: 1213: 1208: 1205: 1201: 1200: 1195: 1192: 1188: 1187: 1182: 1181: 1179: 1175: 1169: 1166: 1164: 1161: 1159: 1156: 1154: 1151: 1149: 1146: 1145: 1143: 1139: 1133: 1130: 1128: 1127:Enzyme family 1125: 1123: 1120: 1118: 1115: 1114: 1112: 1108: 1102: 1099: 1097: 1094: 1092: 1091:Cooperativity 1089: 1087: 1084: 1083: 1081: 1077: 1071: 1068: 1066: 1063: 1061: 1058: 1056: 1053: 1051: 1050:Oxyanion hole 1048: 1046: 1043: 1041: 1038: 1036: 1033: 1032: 1030: 1026: 1022: 1015: 1010: 1008: 1003: 1001: 996: 995: 992: 980: 977: 976: 974: 972: 968: 964: 956: 953: 951: 948: 946: 943: 941: 938: 937: 936: 933: 931: 928: 926: 923: 922: 920: 918: 914: 910: 904: 901: 900: 898: 896: 892: 888: 882: 879: 878: 876: 874: 870: 866: 860: 857: 853: 850: 848: 845: 844: 843: 840: 839: 837: 835: 831: 827: 823: 818: 814: 811:Aldehyde/oxo 806: 801: 799: 794: 792: 787: 786: 783: 776: 772: 768: 763: 758: 754: 750: 749:J. Biol. Chem 746: 741: 740: 733: 729: 725: 721: 717: 713: 709: 702: 699: 693: 691: 689: 685: 681: 677: 673: 669: 665: 661: 657: 653: 649: 645: 641: 637: 633: 629: 625: 621: 617: 613: 609: 605: 601: 597: 593: 589: 581: 579: 577: 574: 570: 566: 562: 558: 554: 550: 546: 533: 530: 528: 524: 521: 517: 513: 510: 508: 504: 500: 496: 493: 490: 486: 481: 477: 474: 471: 469: 465: 462: 459: 456: 452: 449: 446: 444: 440: 436: 432: 427: 422: 416: 414: 412: 409:found in the 408: 407:Asd RNA motif 404: 403:cis-regulated 399: 397: 393: 389: 385: 381: 377: 373: 369: 362: 358: 354: 347: 343: 338: 336: 332: 328: 321: 317: 313: 309: 302: 268: 267: 266: 265: 261: 256: 253: 248: 244: 241: 237: 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: 20: 1384:EC 1.2 stubs 1324:expanding it 1310: 1302: 1264:Translocases 1261: 1248: 1235: 1222: 1209: 1199:Transferases 1196: 1183: 1040:Binding site 755:(1): 39–50. 752: 748: 715: 711: 701: 585: 576:biosynthesis 544: 542: 400: 379: 375: 371: 364: 360: 356: 349: 339: 298: 257: 235: 229: 91:BRENDA entry 1035:Active site 553:amino acids 429:Identifiers 258:The enzyme 79:IntEnz view 39:Identifiers 1363:Categories 1238:Isomerases 1212:Hydrolases 1079:Regulation 873:cytochrome 712:J Mol Biol 694:References 588:structures 495:structures 301:substrates 232:enzymology 148:structures 115:KEGG entry 62:9000-98-0 1117:EC number 917:disulfide 557:aspartate 473:IPR012280 392:threonine 312:phosphate 280:⇌ 260:catalyzes 68:Databases 1369:EC 1.2.1 1141:Kinetics 1065:Cofactor 1028:Activity 771:14353904 732:10369777 573:arginine 549:arginine 512:RCSB PDB 468:InterPro 320:products 245:) is an 243:1.2.1.11 219:proteins 207:articles 195:articles 152:RCSB PDB 50:1.2.1.11 1297:Biology 1251:Ligases 1021:Enzymes 448:PF02774 384:glycine 174:QuickGO 139:profile 122:MetaCyc 57:CAS no. 1316:enzyme 1313:EC 1.2 1283:Portal 1225:Lyases 945:BCKDHB 940:BCKDHA 895:oxygen 769:  730:  686:, and 561:fungal 527:PDBsum 501:  491:  461:CL0139 434:Symbol 411:5' UTR 405:by an 388:serine 378:, and 333:, and 314:, and 299:The 3 247:enzyme 202:PubMed 184:Search 170:AmiGO 158:PDBsum 98:ExPASy 86:BRENDA 74:IntEnz 45:EC no. 1311:This 1177:Types 967:1.2.7 913:1.2.4 891:1.2.3 869:1.2.2 826:1.2.1 555:from 331:NADPH 234:, an 134:PRIAM 1320:stub 1269:list 1262:EC7 1256:list 1249:EC6 1243:list 1236:EC5 1230:list 1223:EC4 1217:list 1210:EC3 1204:list 1197:EC2 1191:list 1184:EC1 834:NADP 819:1.2) 767:PMID 728:PMID 688:2GZ3 684:2GZ2 680:2GZ1 676:2GYY 672:2EP5 668:1YS4 664:1TB4 660:1TA4 656:1T4D 652:1T4B 648:1Q2X 644:1PU2 640:1PS8 636:1PR3 632:1PQU 628:1PQP 624:1OZA 620:1NX6 616:1NWH 612:1NWC 608:1MC4 604:1MB4 600:1GL3 596:1BRM 567:and 520:PDBj 516:PDBe 499:ECOD 489:Pfam 457:clan 455:Pfam 443:Pfam 390:and 322:are 316:NADP 214:NCBI 155:PDBe 110:KEGG 955:DLD 950:DBT 832:or 830:NAD 757:doi 753:213 720:doi 716:289 592:PDB 507:PDB 230:In 190:PMC 146:PDB 1365:: 969:: 915:: 893:: 871:: 828:: 817:EC 765:. 751:. 747:. 726:. 714:. 710:. 690:. 682:, 678:, 674:, 670:, 666:, 662:, 658:, 654:, 650:, 646:, 642:, 638:, 634:, 630:, 626:, 622:, 618:, 614:, 610:, 606:, 602:, 598:, 518:; 514:; 497:/ 398:. 386:, 374:, 370:, 363:, 359:, 329:, 310:, 240:EC 172:/ 1351:e 1344:t 1337:v 1326:. 1285:: 1271:) 1267:( 1258:) 1254:( 1245:) 1241:( 1232:) 1228:( 1219:) 1215:( 1206:) 1202:( 1193:) 1189:( 1013:e 1006:t 999:v 815:( 804:e 797:t 790:v 773:. 759:: 734:. 722:: 545:N 366:L 351:L 335:H 325:L 306:L 293:L 270:L 238:(

Index


EC no.
1.2.1.11
CAS no.
9000-98-0
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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