1733:
40:
582:
are histidine, glutamate, aspartate or lysine and at least one other residue is required for catalysis, which may play an electrophilic role. Of the known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site. The
335:
177:
1057:
291:
279:
121:
109:
645:
1399:
849:
563:
Metalloproteases are the most diverse of the four main protease types, with more than 50 families classified to date. In these enzymes, a
1086:
1050:
994:
772:
King, John V.; Liang, Wenguang G.; Scherpelz, Kathryn P.; Schilling, Alexander B.; Meredith, Stephen C.; Tang, Wei-Jen (2014-07-08).
1452:
658:
Metalloproteinase inhibitors are found in numerous marine organisms, including fish, cephalopods, mollusks, algae and bacteria.
1043:
513:
peptidase families are grouped by their catalytic type, the first character representing the catalytic type: A, aspartic; C,
1608:
355:
197:
1723:
1404:
587:
is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often
1298:
1293:
1593:
1763:
1709:
1696:
1683:
1670:
1657:
1644:
1631:
1077:
625:
1603:
1557:
1500:
1414:
1231:
1074:
1007:
682:
502:
484:
394:
which plays a significant role in the fusion of muscle cells during embryo development, in a process known as
343:
185:
1505:
552:
that characterises the clan or family may have lost its catalytic activity, yet retained its function in
1526:
1445:
1389:
629:
534:
1598:
339:
181:
1070:
886:
720:
494:
1562:
687:
649:
614:
603:
557:
480:
461:
133:
1768:
1758:
1753:
1495:
549:
1035:
965:
914:
855:
845:
811:
793:
754:
736:
330:
172:
1541:
1536:
1510:
1438:
1338:
1003:
955:
945:
904:
894:
837:
801:
785:
744:
728:
460:
that removes zinc, which is essential for activity. They are also inhibited by the chelator
991:
709:"Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism"
541:. In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated
322:
164:
1588:
1572:
1485:
1094:
998:
875:"Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp"
510:
449:
272:
102:
890:
774:"Molecular basis of substrate recognition and degradation by human presequence protease"
724:
1737:
1626:
1567:
960:
933:
909:
874:
806:
773:
749:
708:
641:
618:
457:
284:
114:
505:, and M16 metalloproteinases such as Insulin Degrading Enzyme and Presequence Protease
1747:
1531:
1490:
841:
707:
Shen, Yuequan; Joachimiak, Andrzej; Rosner, Marsha Rich; Tang, Wei-Jen (2006-10-19).
637:
584:
490:
1015:
235:
65:
1480:
498:
476:
318:
160:
296:
248:
138:
126:
78:
1031:
899:
260:
90:
1704:
1639:
1475:
1409:
1394:
1239:
670:
600:
592:
538:
530:
1732:
17:
1384:
1256:
832:
Rawlings ND, Barrett AJ (1995). "Evolutionary families of metallopeptidases".
789:
596:
575:
526:
395:
797:
740:
1678:
1652:
525:; and U, unknown. The serine, threonine and cysteine peptidases utilise the
522:
430:
426:
422:
383:
969:
918:
815:
758:
950:
859:
39:
1419:
1221:
1216:
1211:
1066:
1027:
662:
652:
564:
545:
514:
438:
376:
255:
85:
732:
1206:
1201:
1196:
1191:
1186:
1181:
1176:
665:
sterol-regulatory element binding protein (SREBP) site 2 protease and
607:
579:
553:
414:
934:"Metalloproteinase inhibitors: status and scope from marine organisms"
1691:
1461:
1343:
1171:
1166:
1161:
1156:
1151:
1146:
1141:
1136:
1114:
1109:
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97:
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1333:
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1313:
1308:
1303:
1288:
1283:
1131:
1126:
1121:
1099:
611:
542:
387:
610:
is never found in this site, possibly because it would break the
1278:
1273:
1266:
1261:
1249:
1244:
1023:
633:
453:
402:
312:
242:
230:
154:
72:
60:
1434:
1039:
571:
410:
1430:
836:. Methods in Enzymology. Vol. 248. pp. 183–228.
570:, usually zinc, activates the water molecule. The metal
421:. The ligands coordinating the metal ion can vary with
1022:
This article incorporates text from the public domain
1721:
990:
online database for peptidases and their inhibitors:
834:
Proteolytic
Enzymes: Aspartic and Metallo Peptidases
661:
Members of the M50 metallopeptidase family include:
441:. The fourth coordination position is taken up by a
1617:
1581:
1550:
1519:
1468:
1377:
1230:
1085:
497:(3.4.24). Well known metalloendopeptidases include
349:
329:
311:
306:
290:
278:
266:
254:
241:
229:
221:
216:
211:
191:
171:
153:
148:
132:
120:
108:
96:
84:
71:
59:
51:
46:
32:
591:or threonine and forms part of the S1' subsite in
578:ligands, usually three in number. The known metal
644:1, which proteolytically removes the C-terminal
472:There are two subgroups of metalloproteinases:
1446:
1051:
827:
825:
8:
537:- these peptidases can also readily act as
1453:
1439:
1431:
1058:
1044:
1036:
456:leads to complete inactivation. EDTA is a
303:
145:
38:
1006:at the U.S. National Library of Medicine
959:
949:
908:
898:
873:Minde DP, Maurice MM, RĂĽdiger SG (2012).
805:
748:
599:, 'b' is an uncharged residue, and 'c' a
1728:
699:
624:Metallopeptidases from family M48 are
208:
29:
1400:Pregnancy-associated plasma protein A
7:
548:. In many instances, the structural
938:Biochemistry Research International
517:; G, glutamic acid; M, metallo; S,
25:
1731:
401:Most metalloproteases require
1:
307:Available protein structures:
149:Available protein structures:
1405:Bone morphogenetic protein 1
900:10.1371/journal.pone.0046147
842:10.1016/0076-6879(95)48015-3
1785:
1021:
932:Thomas NV, Kim SK (2010).
626:integral membrane proteins
1609:Michaelis–Menten kinetics
1232:Matrix metalloproteinases
790:10.1016/j.str.2014.05.003
503:matrix metalloproteinases
302:
144:
37:
1501:Diffusion-limited enzyme
1415:Insulin-degrading enzyme
1008:Medical Subject Headings
683:Matrix metalloproteinase
669:protease EcfE, stage IV
636:ion per subunit. These
632:and Golgi, binding one
413:is coordinated to the
1594:Eadie–Hofstee diagram
1527:Allosteric regulation
1390:Procollagen peptidase
1071:metalloendopeptidases
630:endoplasmic reticulum
621:in metalloproteases.
495:metalloendopeptidases
386:mechanism involves a
1604:Lineweaver–Burk plot
640:include CAAX prenyl
628:associated with the
574:is held in place by
481:metalloexopeptidases
951:10.1155/2010/845975
891:2012PLoSO...746147M
733:10.1038/nature05143
725:2006Natur.443..870S
688:The Proteolysis Map
462:orthophenanthroline
1563:Enzyme superfamily
1496:Enzyme promiscuity
997:2017-04-04 at the
992:Metallo Peptidases
1719:
1718:
1428:
1427:
851:978-0-12-182149-4
719:(7113): 870–874.
533:and form an acyl
390:. An example is
369:metalloproteinase
365:
364:
361:
360:
356:structure summary
207:
206:
203:
202:
198:structure summary
16:(Redirected from
1776:
1764:Protein families
1736:
1735:
1727:
1599:Hanes–Woolf plot
1542:Enzyme activator
1537:Enzyme inhibitor
1511:Enzyme catalysis
1455:
1448:
1441:
1432:
1095:Alpha secretases
1060:
1053:
1046:
1037:
1016:Metalloproteases
1004:Metalloproteases
974:
973:
963:
953:
929:
923:
922:
912:
902:
870:
864:
863:
829:
820:
819:
809:
769:
763:
762:
752:
704:
667:Escherichia coli
617:adopted by this
556:recognition and
450:chelating agents
445:water molecule.
304:
209:
146:
42:
30:
21:
1784:
1783:
1779:
1778:
1777:
1775:
1774:
1773:
1744:
1743:
1742:
1730:
1722:
1720:
1715:
1627:Oxidoreductases
1613:
1589:Enzyme kinetics
1577:
1573:List of enzymes
1546:
1515:
1486:Catalytic triad
1464:
1459:
1429:
1424:
1373:
1226:
1081:
1064:
1034:
999:Wayback Machine
983:
978:
977:
931:
930:
926:
872:
871:
867:
852:
831:
830:
823:
784:(7): 996–1007.
771:
770:
766:
706:
705:
701:
696:
679:
511:MEROPS database
470:
448:Treatment with
405:, but some use
373:metalloprotease
280:OPM superfamily
110:OPM superfamily
28:
23:
22:
18:Metalloprotease
15:
12:
11:
5:
1782:
1780:
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1585:
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1554:
1552:
1551:Classification
1548:
1547:
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1539:
1534:
1529:
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1517:
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1234:
1228:
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1204:
1199:
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1179:
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1129:
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1119:
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981:External links
979:
976:
975:
924:
885:(10): e46147.
865:
850:
821:
764:
698:
697:
695:
692:
691:
690:
685:
678:
675:
646:three residues
638:endopeptidases
507:
506:
491:Endopeptidases
488:
469:
468:Classification
466:
458:metal chelator
363:
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353:
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27:Type of enzyme
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24:
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1597:
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1586:
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1580:
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1571:
1569:
1568:Enzyme family
1566:
1564:
1561:
1559:
1556:
1555:
1553:
1549:
1543:
1540:
1538:
1535:
1533:
1532:Cooperativity
1530:
1528:
1525:
1524:
1522:
1518:
1512:
1509:
1507:
1504:
1502:
1499:
1497:
1494:
1492:
1491:Oxyanion hole
1489:
1487:
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1482:
1479:
1477:
1474:
1473:
1471:
1467:
1463:
1456:
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1300:
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1190:
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1128:
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1120:
1116:
1113:
1111:
1108:
1106:
1103:
1101:
1098:
1097:
1096:
1093:
1092:
1090:
1088:
1087:ADAM proteins
1084:
1079:
1076:
1072:
1068:
1061:
1056:
1054:
1049:
1047:
1042:
1041:
1038:
1033:
1029:
1025:
1018:
1017:
1013:Proteopedia:
1012:
1009:
1005:
1002:
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989:
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751:
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551:
547:
544:
540:
536:
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528:
524:
520:
516:
512:
504:
500:
499:ADAM proteins
496:
492:
489:
486:
482:
478:
477:Exopeptidases
475:
474:
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467:
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459:
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225:Peptidase_M50
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212:Peptidase_M50
210:
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62:
58:
55:Peptidase_M48
54:
50:
45:
41:
36:
33:Peptidase_M48
31:
19:
1705:Translocases
1702:
1689:
1676:
1663:
1650:
1640:Transferases
1637:
1624:
1481:Binding site
1240:Collagenases
1014:
941:
937:
927:
882:
878:
868:
833:
781:
777:
767:
716:
712:
702:
673:protein FB.
666:
660:
657:
650:farnesylated
623:
562:
550:protein fold
539:transferases
535:intermediate
508:
471:
447:
409:. The metal
400:
372:
368:
366:
1476:Active site
1410:Lysostaphin
1395:Thermolysin
1257:Gelatinases
671:sporulation
601:hydrophobic
593:thermolysin
531:nucleophile
292:OPM protein
217:Identifiers
122:OPM protein
47:Identifiers
1748:Categories
1679:Isomerases
1653:Hydrolases
1520:Regulation
1385:Neprilysin
944:: 845975.
694:References
597:neprilysin
576:amino acid
527:amino acid
487:: 3.4.17).
417:via three
396:myogenesis
319:structures
161:structures
134:Membranome
1769:Proteases
1759:EC 3.4.17
1754:EC 3.4.24
1558:EC number
1067:Proteases
1032:IPR008915
798:1878-4186
778:Structure
741:1476-4687
663:mammalian
615:structure
523:threonine
485:EC number
431:aspartate
427:glutamate
423:histidine
384:catalytic
375:, is any
261:IPR008915
91:IPR001915
1582:Kinetics
1506:Cofactor
1469:Activity
1420:ZMPSTE24
1222:ADAMTS13
1217:ADAMTS12
1212:ADAMTS10
1028:InterPro
995:Archived
970:21197102
919:23056252
879:PLOS ONE
816:24931469
759:17051221
677:See also
653:proteins
642:protease
565:divalent
546:molecule
515:cysteine
452:such as
439:arginine
377:protease
336:RCSB PDB
256:InterPro
178:RCSB PDB
86:InterPro
1738:Biology
1692:Ligases
1462:Enzymes
1207:ADAMTS9
1202:ADAMTS8
1197:ADAMTS5
1192:ADAMTS4
1187:ADAMTS3
1182:ADAMTS2
1177:ADAMTS1
961:3004377
910:3463568
887:Bibcode
860:7674922
807:4128088
750:3366509
721:Bibcode
612:helical
608:Proline
604:residue
580:ligands
558:binding
554:protein
509:In the
419:ligands
415:protein
236:PF02163
66:PF01435
1724:Portal
1666:Lyases
1344:MMP23B
1339:MMP23A
1172:ADAM33
1167:ADAM28
1162:ADAM23
1157:ADAM22
1152:ADAM18
1147:ADAM15
1142:ADAM12
1137:ADAM11
1115:ADAM19
1110:ADAM17
1105:ADAM10
1078:3.4.24
1010:(MeSH)
988:MEROPS
968:
958:
917:
907:
858:
848:
814:
804:
796:
757:
747:
739:
713:Nature
589:valine
583:HEXXH
568:cation
519:serine
443:labile
437:, and
435:lysine
407:cobalt
392:ADAM12
382:whose
380:enzyme
351:PDBsum
325:
315:
268:MEROPS
249:CL0126
222:Symbol
193:PDBsum
167:
157:
98:MEROPS
79:CL0126
52:Symbol
1618:Types
1378:Other
1369:MMP28
1364:MMP27
1359:MMP26
1354:MMP25
1349:MMP24
1334:MMP21
1329:MMP20
1324:MMP19
1319:MMP17
1314:MMP16
1309:MMP15
1304:MMP14
1299:MMP13
1294:MMP12
1289:MMP11
1284:MMP10
1132:ADAM8
1127:ADAM7
1122:ADAM2
1100:ADAM9
619:motif
585:motif
543:water
529:as a
521:; T,
388:metal
371:, or
1710:list
1703:EC7
1697:list
1690:EC6
1684:list
1677:EC5
1671:list
1664:EC4
1658:list
1651:EC3
1645:list
1638:EC2
1632:list
1625:EC1
1279:MMP7
1274:MMP3
1267:MMP9
1262:MMP2
1250:MMP8
1245:MMP1
1026:and
1024:Pfam
986:The
966:PMID
942:2010
915:PMID
856:PMID
846:ISBN
812:PMID
794:ISSN
755:PMID
737:ISSN
634:zinc
595:and
501:and
454:EDTA
403:zinc
344:PDBj
340:PDBe
323:ECOD
313:Pfam
297:3b4r
245:clan
243:Pfam
231:Pfam
186:PDBj
182:PDBe
165:ECOD
155:Pfam
127:4aw6
75:clan
73:Pfam
61:Pfam
956:PMC
946:doi
905:PMC
895:doi
838:doi
802:PMC
786:doi
745:PMC
729:doi
717:443
648:of
572:ion
411:ion
331:PDB
285:184
273:M50
173:PDB
139:317
115:394
103:M48
1750::
1075:EC
1069::
1030::
964:.
954:.
940:.
936:.
913:.
903:.
893:.
881:.
877:.
854:.
844:.
824:^
810:.
800:.
792:.
782:22
780:.
776:.
753:.
743:.
735:.
727:.
715:.
711:.
655:.
606:.
560:.
493:,
479:,
464:.
433:,
429:,
425:,
398:.
367:A
342:;
338:;
321:/
184:;
180:;
163:/
1726::
1712:)
1708:(
1699:)
1695:(
1686:)
1682:(
1673:)
1669:(
1660:)
1656:(
1647:)
1643:(
1634:)
1630:(
1454:e
1447:t
1440:v
1080:)
1073:(
1059:e
1052:t
1045:v
972:.
948::
921:.
897::
889::
883:7
862:.
840::
818:.
788::
761:.
731::
723::
483:(
20:)
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