752:
496:
1674:
225:
817:
Valiña AL, Mazumder-Shivakumar D, Bruice TC (December 2004). "Probing the Ser-Ser-Lys catalytic triad mechanism of peptide amidase: computational studies of the ground state, transition state, and intermediate".
1082:
943:
Kwak JH, Shin K, Woo JS, Kim MK, Kim SI, Eom SH, Hong KW (December 2002). "Expression, purification, and crystallization of glutamyl-tRNA(Gln) specific amidotransferase from
Bacillus stearothermophilus".
610:
specificity and function. Nonetheless, these enzymes maintain a core alpha/beta/alpha structure, where the topologies of the N- and C-terminal halves are similar. AS enzymes characteristically have a
1075:
381:
179:
1068:
325:
313:
198:
1745:
542:
1311:
293:
1774:
896:"Structure of malonamidase E2 reveals a novelSer-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in nature"
1393:
1020:"The fate of certain organic acids and amides in the rabbit. 11 Further observations on the hydrolysis of amides by tissue extracts"
191:
790:
1286:
118:
1549:
401:
142:
558:
1738:
733:
enzyme that catalyses the formation of Gln-tRNA(Gln) by the transamidation of misacylated Glu-tRNA(Gln) via amidolysis of
686:
1664:
231:
1248:
1534:
1764:
1650:
1637:
1624:
1611:
1598:
1585:
1572:
1346:
1323:
1258:
1225:
1192:
1104:
1544:
554:
1731:
1498:
1441:
1095:
675:
546:
465:
422:
136:
29:
389:
1446:
1165:
611:
123:
562:
1779:
1467:
1386:
643:
550:
203:
1539:
385:
111:
505:, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The
1296:
306:
46:
1503:
1276:
1175:
1060:
723:
481:
337:
41:
139:
1436:
1301:
783:
631:
577:
569:
63:
1769:
1271:
1049:
961:
925:
876:
835:
376:
130:
1715:
1482:
1477:
1451:
1379:
1039:
1031:
1004:
996:
953:
915:
907:
866:
827:
607:
985:"The fate of certain organic acids and amides in the rabbit. 7. An amidase of rabbit liver"
368:
1529:
1513:
1426:
1153:
794:
690:
683:
635:
506:
495:
99:
855:"A second fatty acid amide hydrolase with variable distribution among placental mammals"
765:
Please help update this article to reflect recent events or newly available information.
75:
1678:
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34:
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318:
154:
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704:
the hydrolysis of malonamate into malonate and ammonia, and which is involved in the
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149:
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1619:
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682:
and sleep-inducing oleamide), thereby controlling the level and duration of
671:
657:
639:
627:
623:
502:
457:
1053:
965:
929:
880:
871:
854:
839:
894:
Shin S, Lee TH, Ha NC, Koo HM, Kim SY, Lee HS, Kim YS, Oh BH (June 2002).
853:
Wei BQ, Mikkelsen TS, McKinney MK, Lander ES, Cravatt BF (December 2006).
302:
224:
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709:
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269:
236:
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87:
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453:
396:
186:
82:
70:
58:
1606:
1306:
713:
694:
600:
473:
469:
606:(CO-NH2), although the family has diverged widely with regard to
1686:
1170:
1142:
358:
257:
94:
1375:
1064:
786:
have been solved for this family, which can be accessed at the
745:
1371:
983:
Bray HG, James SP, Raffan IM, Ryman BE, Thorpe WV (1949).
1719:
1685:
This article incorporates text from the public domain
626:
residues, therefore they differ from classical serine
1662:
649:
Examples of AS signature-containing enzymes include:
1558:
1522:
1491:
1460:
1409:
1345:
1322:
1257:
1224:
1191:
1103:
395:
375:
357:
352:
336:
324:
312:
292:
280:
268:
256:
248:
243:
217:
197:
185:
173:
168:
148:
129:
117:
105:
93:
81:
69:
57:
52:
40:
28:
23:
18:
1018:Bray HG, James SP, Thorpe WV, Wasdell MR (1950).
729:Subunit A of Glu-tRNA(Gln) amidotransferase, a
660:the hydrolysis of the C-terminal amide bond of
229:X-ray structure of native peptide amidase from
812:
810:
1739:
1387:
1076:
8:
580:. They are widespread, being found in both
1746:
1732:
1394:
1380:
1372:
1083:
1069:
1061:
349:
223:
165:
1043:
1008:
919:
870:
630:. These enzymes possess a unique, highly
543:urea cycle and metabolism of amino groups
638:used for amide hydrolysis, although the
1669:
806:
646:formation can differ between enzymes.
214:
15:
1312:Activation-induced cytidine deaminase
559:benzoate degradation via coa ligation
501:This enzyme belongs to the family of
7:
1704:
1702:
618:and glycine residues, but devoid of
513:. Other names in common use include
464:of an amide. In this way, the two
1718:. You can help Knowledge (XXG) by
450:N-acetylaminohydrolase (ambiguous)
14:
537:. This enzyme participates in 6
1672:
750:
494:
1094:: carbon-nitrogen non-peptide (
1287:Inosine monophosphate synthase
1:
958:10.1016/S1016-8478(23)15118-1
572:stretch of approximately 130
353:Available protein structures:
232:Stenotrophomonas maltophilia
1796:
1775:Enzymes of known structure
1701:
1684:
1249:Protein-arginine deiminase
1171:Fatty acid amide hydrolase
614:C-terminal region rich in
555:cyanoamino acid metabolism
438:amidohydrolase (ambiguous)
1550:Michaelis–Menten kinetics
759:This section needs to be
348:
222:
164:
1442:Diffusion-limited enzyme
912:10.1093/emboj/21.11.2509
670:amide hydrolases, which
547:phenylalanine metabolism
511:acylamide amidohydrolase
509:of this enzyme class is
484:are monocarboxylate and
1166:Aspartylglucosaminidase
700:Malonamidase E2, which
1714:-related article is a
872:10.1074/jbc.M606646200
535:N-acetylaminohydrolase
468:of this enzyme are an
1535:Eadie–Hofstee diagram
1468:Allosteric regulation
782:As of late 2018, 162
656:amidase (Pam), which
551:tryptophan metabolism
442:deaminase (ambiguous)
1545:Lineweaver–Burk plot
1297:GTP cyclohydrolase I
434:acylase (misleading)
1277:Adenosine deaminase
1176:Histone deacetylase
724:nitrogen metabolism
712:from bacteroids to
640:catalytic mechanism
568:Amidases contain a
563:styrene degradation
1504:Enzyme superfamily
1437:Enzyme promiscuity
1302:Cytidine deaminase
1261:: Cyclic amidines/
1228:: Linear amidines/
793:2021-09-18 at the
742:Structural studies
678:(e.g. cannabinoid
539:metabolic pathways
480:, whereas its two
1727:
1726:
1660:
1659:
1369:
1368:
1272:Guanine deaminase
1107:: Linear amides /
1036:10.1042/bj0470294
1001:10.1042/bj0440618
832:10.1021/bi049025r
780:
779:
531:fatty acylamidase
446:fatty acylamidase
411:
410:
407:
406:
402:structure summary
213:
212:
209:
208:
112:metabolic pathway
1787:
1765:Protein families
1748:
1741:
1734:
1703:
1677:
1676:
1668:
1540:Hanes–Woolf plot
1483:Enzyme activator
1478:Enzyme inhibitor
1452:Enzyme catalysis
1396:
1389:
1382:
1373:
1195:: Cyclic amides/
1085:
1078:
1071:
1062:
1057:
1047:
1014:
1012:
970:
969:
940:
934:
933:
923:
891:
885:
884:
874:
865:(48): 36569–78.
850:
844:
843:
826:(50): 15657–72.
814:
775:
772:
766:
754:
753:
746:
689:by this diverse
674:fatty acid amid
642:for acyl-enzyme
612:highly conserved
576:known as the AS
498:
350:
227:
215:
166:
16:
1795:
1794:
1790:
1789:
1788:
1786:
1785:
1784:
1755:
1754:
1753:
1752:
1699:
1697:
1683:
1671:
1663:
1661:
1656:
1568:Oxidoreductases
1554:
1530:Enzyme kinetics
1518:
1514:List of enzymes
1487:
1456:
1427:Catalytic triad
1405:
1400:
1370:
1365:
1341:
1329:Aminohydrolases
1327:
1318:
1264:Aminohydrolases
1262:
1253:
1229:
1220:
1198:Amidohydrolases
1196:
1187:
1110:Amidohydrolases
1108:
1099:
1089:
1017:
982:
979:
977:Further reading
974:
973:
942:
941:
937:
906:(11): 2509–16.
893:
892:
888:
852:
851:
847:
816:
815:
808:
803:
795:Wayback Machine
776:
770:
767:
764:
755:
751:
744:
636:catalytic triad
507:systematic name
489:
477:
314:OPM superfamily
239:
12:
11:
5:
1793:
1791:
1783:
1782:
1777:
1772:
1767:
1757:
1756:
1751:
1750:
1743:
1736:
1728:
1725:
1724:
1682:
1681:
1658:
1657:
1655:
1654:
1641:
1628:
1615:
1602:
1589:
1576:
1562:
1560:
1556:
1555:
1553:
1552:
1547:
1542:
1537:
1532:
1526:
1524:
1520:
1519:
1517:
1516:
1511:
1506:
1501:
1495:
1493:
1492:Classification
1489:
1488:
1486:
1485:
1480:
1475:
1470:
1464:
1462:
1458:
1457:
1455:
1454:
1449:
1444:
1439:
1434:
1429:
1424:
1419:
1413:
1411:
1407:
1406:
1401:
1399:
1398:
1391:
1384:
1376:
1367:
1366:
1364:
1363:
1358:
1352:
1350:
1343:
1342:
1340:
1339:
1333:
1331:
1320:
1319:
1317:
1316:
1315:
1314:
1309:
1299:
1294:
1292:DCMP deaminase
1289:
1284:
1279:
1274:
1268:
1266:
1255:
1254:
1252:
1251:
1246:
1241:
1235:
1233:
1231:Ureohydrolases
1222:
1221:
1219:
1218:
1216:Dihydroorotase
1213:
1211:Beta-lactamase
1208:
1202:
1200:
1189:
1188:
1186:
1185:
1184:
1183:
1173:
1168:
1163:
1158:
1157:
1156:
1151:
1148:Aspartoacylase
1145:
1135:
1130:
1125:
1120:
1114:
1112:
1101:
1100:
1090:
1088:
1087:
1080:
1073:
1065:
1059:
1058:
1030:(3): 294–299.
1015:
995:(5): 618–625.
978:
975:
972:
971:
935:
886:
845:
805:
804:
802:
799:
778:
777:
758:
756:
749:
743:
740:
739:
738:
731:heterotrimeric
727:
698:
665:
523:amidohydrolase
487:
475:
409:
408:
405:
404:
399:
393:
392:
379:
373:
372:
362:
355:
354:
346:
345:
340:
334:
333:
328:
322:
321:
316:
310:
309:
296:
290:
289:
284:
278:
277:
272:
266:
265:
260:
254:
253:
250:
246:
245:
241:
240:
228:
220:
219:
211:
210:
207:
206:
201:
195:
194:
189:
183:
182:
177:
171:
170:
162:
161:
152:
146:
145:
134:
127:
126:
121:
115:
114:
109:
103:
102:
97:
91:
90:
85:
79:
78:
73:
67:
66:
61:
55:
54:
50:
49:
44:
38:
37:
32:
26:
25:
21:
20:
13:
10:
9:
6:
4:
3:
2:
1792:
1781:
1778:
1776:
1773:
1771:
1768:
1766:
1763:
1762:
1760:
1749:
1744:
1742:
1737:
1735:
1730:
1729:
1723:
1721:
1717:
1713:
1710:
1705:
1700:
1696:
1692:
1688:
1680:
1675:
1670:
1666:
1652:
1648:
1647:
1642:
1639:
1635:
1634:
1629:
1626:
1622:
1621:
1616:
1613:
1609:
1608:
1603:
1600:
1596:
1595:
1590:
1587:
1583:
1582:
1577:
1574:
1570:
1569:
1564:
1563:
1561:
1557:
1551:
1548:
1546:
1543:
1541:
1538:
1536:
1533:
1531:
1528:
1527:
1525:
1521:
1515:
1512:
1510:
1509:Enzyme family
1507:
1505:
1502:
1500:
1497:
1496:
1494:
1490:
1484:
1481:
1479:
1476:
1474:
1473:Cooperativity
1471:
1469:
1466:
1465:
1463:
1459:
1453:
1450:
1448:
1445:
1443:
1440:
1438:
1435:
1433:
1432:Oxyanion hole
1430:
1428:
1425:
1423:
1420:
1418:
1415:
1414:
1412:
1408:
1404:
1397:
1392:
1390:
1385:
1383:
1378:
1377:
1374:
1362:
1361:Thiaminase II
1359:
1357:
1356:Riboflavinase
1354:
1353:
1351:
1348:
1344:
1338:
1335:
1334:
1332:
1330:
1325:
1321:
1313:
1310:
1308:
1305:
1304:
1303:
1300:
1298:
1295:
1293:
1290:
1288:
1285:
1283:
1282:AMP deaminase
1280:
1278:
1275:
1273:
1270:
1269:
1267:
1265:
1260:
1256:
1250:
1247:
1245:
1242:
1240:
1237:
1236:
1234:
1232:
1227:
1223:
1217:
1214:
1212:
1209:
1207:
1204:
1203:
1201:
1199:
1194:
1190:
1182:
1179:
1178:
1177:
1174:
1172:
1169:
1167:
1164:
1162:
1159:
1155:
1152:
1149:
1146:
1144:
1141:
1140:
1139:
1136:
1134:
1131:
1129:
1126:
1124:
1121:
1119:
1116:
1115:
1113:
1111:
1106:
1102:
1097:
1093:
1086:
1081:
1079:
1074:
1072:
1067:
1066:
1063:
1055:
1051:
1046:
1041:
1037:
1033:
1029:
1025:
1021:
1016:
1011:
1006:
1002:
998:
994:
990:
986:
981:
980:
976:
967:
963:
959:
955:
952:(3): 374–81.
951:
947:
939:
936:
931:
927:
922:
917:
913:
909:
905:
901:
897:
890:
887:
882:
878:
873:
868:
864:
860:
859:J. Biol. Chem
856:
849:
846:
841:
837:
833:
829:
825:
821:
813:
811:
807:
800:
798:
796:
792:
789:
785:
774:
762:
757:
748:
747:
741:
736:
732:
728:
725:
722:
718:
715:
711:
707:
703:
699:
697:transmitters.
696:
692:
688:
685:
681:
677:
673:
669:
666:
663:
659:
655:
652:
651:
650:
647:
645:
641:
637:
633:
629:
625:
621:
620:aspartic acid
617:
613:
609:
605:
602:
598:
594:
591:
587:
583:
579:
575:
571:
566:
564:
560:
556:
552:
548:
544:
540:
536:
532:
528:
524:
520:
516:
512:
508:
504:
499:
497:
492:
490:
483:
479:
471:
467:
463:
459:
455:
451:
447:
443:
439:
435:
431:
427:
424:
420:
416:
403:
400:
398:
394:
391:
387:
383:
380:
378:
374:
370:
366:
363:
360:
356:
351:
347:
344:
341:
339:
335:
332:
329:
327:
323:
320:
317:
315:
311:
308:
304:
300:
297:
295:
291:
288:
285:
283:
279:
276:
273:
271:
267:
264:
261:
259:
255:
251:
247:
242:
238:
234:
233:
226:
221:
216:
205:
202:
200:
196:
193:
190:
188:
184:
181:
178:
176:
172:
167:
163:
160:
156:
153:
151:
150:Gene Ontology
147:
144:
141:
138:
135:
132:
128:
125:
122:
120:
116:
113:
110:
108:
104:
101:
98:
96:
92:
89:
88:NiceZyme view
86:
84:
80:
77:
74:
72:
68:
65:
62:
60:
56:
51:
48:
45:
43:
39:
36:
33:
31:
27:
22:
17:
1780:EC 3.5 stubs
1720:expanding it
1706:
1698:
1646:Translocases
1643:
1630:
1617:
1604:
1591:
1581:Transferases
1578:
1565:
1422:Binding site
1138:Aminoacylase
1118:Asparaginase
1027:
1023:
992:
988:
949:
945:
938:
903:
899:
889:
862:
858:
848:
823:
820:Biochemistry
819:
781:
768:
760:
648:
644:intermediate
634:Ser-Ser-Lys
567:
534:
530:
526:
522:
518:
514:
510:
500:
493:
449:
445:
441:
437:
433:
429:
418:
412:
230:
76:BRENDA entry
1417:Active site
1326:: Nitriles/
1206:Barbiturase
1133:Biotinidase
1123:Glutaminase
582:prokaryotes
574:amino acids
515:acylamidase
430:acylamidase
326:OPM protein
244:Identifiers
64:IntEnz view
24:Identifiers
1759:Categories
1620:Isomerases
1594:Hydrolases
1461:Regulation
1244:Agmatinase
1161:Ceramidase
1092:Hydrolases
1024:Biochem. J
989:Biochem. J
946:Mol. Cells
801:References
784:structures
684:signalling
680:anandamide
676:substrates
668:Fatty acid
628:hydrolases
597:hydrolysis
586:eukaryotes
503:hydrolases
466:substrates
462:hydrolysis
415:enzymology
365:structures
338:Membranome
133:structures
100:KEGG entry
47:9012-56-0
1695:IPR000120
1499:EC number
1337:Nitrilase
735:glutamine
721:symbiotic
708:of fixed
706:transport
702:catalyses
672:hydrolyse
658:catalyses
632:conserved
624:histidine
608:substrate
570:conserved
527:deaminase
458:catalyzes
287:PDOC00494
275:IPR000120
53:Databases
1770:EC 3.5.1
1691:InterPro
1523:Kinetics
1447:Cofactor
1410:Activity
1239:Arginase
1054:14800883
966:12521300
930:12032064
881:17015445
840:15595822
791:Archived
771:May 2017
710:nitrogen
662:peptides
593:catalyse
578:sequence
482:products
452:) is an
382:RCSB PDB
270:InterPro
204:proteins
192:articles
180:articles
137:RCSB PDB
1679:Biology
1633:Ligases
1403:Enzymes
1349:: Other
1181:Sirtuin
1045:1275209
1010:1274617
761:updated
687:induced
654:Peptide
590:enzymes
519:acylase
426:3.5.1.4
419:amidase
282:PROSITE
263:PF01425
252:Amidase
235:at 1.4
218:Amidase
159:QuickGO
124:profile
107:MetaCyc
42:CAS no.
35:3.5.1.4
19:amidase
1712:enzyme
1709:EC 3.5
1665:Portal
1607:Lyases
1347:3.5.99
1150:(ACY2)
1128:Urease
1052:
1042:
1007:
964:
928:
921:126024
918:
900:EMBO J
879:
838:
616:serine
561:, and
533:, and
454:enzyme
397:PDBsum
371:
361:
307:SUPFAM
249:Symbol
187:PubMed
169:Search
155:AmiGO
143:PDBsum
83:ExPASy
71:BRENDA
59:IntEnz
30:EC no.
1707:This
1559:Types
1324:3.5.5
1307:AICDA
1259:3.5.4
1226:3.5.3
1193:3.5.2
1105:3.5.1
717:cells
714:plant
695:lipid
691:class
604:bonds
601:amide
588:. AS
470:amide
456:that
417:, an
303:SCOPe
294:SCOP2
119:PRIAM
1716:stub
1689:and
1687:Pfam
1651:list
1644:EC7
1638:list
1631:EC6
1625:list
1618:EC5
1612:list
1605:EC4
1599:list
1592:EC3
1586:list
1579:EC2
1573:list
1566:EC1
1154:ACY3
1143:ACY1
1098:3.5)
1050:PMID
962:PMID
926:PMID
877:PMID
836:PMID
788:Pfam
622:and
595:the
584:and
472:and
460:the
390:PDBj
386:PDBe
369:ECOD
359:Pfam
331:1mt5
299:1ocm
258:Pfam
199:NCBI
140:PDBe
95:KEGG
1040:PMC
1032:doi
1005:PMC
997:doi
954:doi
916:PMC
908:doi
867:doi
863:281
828:doi
719:in
693:of
599:of
413:In
377:PDB
343:325
175:PMC
131:PDB
1761::
1693::
1096:EC
1048:.
1038:.
1028:47
1026:.
1022:.
1003:.
993:44
991:.
987:.
960:.
950:14
948:.
924:.
914:.
904:21
902:.
898:.
875:.
861:.
857:.
834:.
824:43
822:.
809:^
797:.
565:.
557:,
553:,
549:,
545:,
541::
529:,
525:,
521:,
517:,
491:.
486:NH
448:,
444:,
440:,
436:,
432:,
428:,
423:EC
388:;
384:;
367:/
319:55
305:/
301:/
157:/
1747:e
1740:t
1733:v
1722:.
1667::
1653:)
1649:(
1640:)
1636:(
1627:)
1623:(
1614:)
1610:(
1601:)
1597:(
1588:)
1584:(
1575:)
1571:(
1395:e
1388:t
1381:v
1084:e
1077:t
1070:v
1056:.
1034::
1013:.
999::
968:.
956::
932:.
910::
883:.
869::
842:.
830::
773:)
769:(
763:.
737:.
726:.
664:.
488:3
478:O
476:2
474:H
421:(
237:Ă…
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