29:
424:
517:
332:
2120:
431:
bovine lens LAP and PepA have been elucidated (Ref 1 and 2), however, the exact mechanism of tomato LAP-A is unknown at this time. A search of current literature does not indicate that new research is underway to determine the exact mechanism of LAP-A. Based on the biochemical similarities of the
500:
whose expression changes over time. The early genes amplify the wounding signal and can be detected 30 minutes to 2 hours after damage (Ryan 2000). Late gene expression can be seen 4–24 hours after wounding. Products of late-response genes act as deterrents to chewing-insect feeding, often by
563:
in wounded LapA-SI plants, and the LapA-SI plants were also more susceptible to tobacco hornworm feeding, relative to wildtype (WT) plants. In comparison, the wounded LapA-OX leaves exhibited heightened levels of late gene RNA accumulation, an increased resistance to herbivory, and extended
577:
LAP proteins are expressed in a variety of marine organisms as a method of coping with the osmotic threat high salinity poses to the cell. During bouts of high salinity, LAP begins the catalysis of proteins in order to release amino acids into the cell in an attempt to balance the high ion
1244:
1107:
854:
601:
903:
Sträter N, Lipscomb WN (November 1995). "Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography".
484:, which are specific to the stressor and the amount of tissue damage inflicted. Similar to mechanical wounding, chewing insects, such as the tobacco hornworm (Manduca sexta, one of the major pests of tomato), cause extensive
564:
expression of late wound-response genes. These data suggest that LAP-A functions in regulating both the intensity and the persistence of the late wound response. However, unwounded LapA-OX did not accumulate late gene
419:
have been much more well-studied and understood by researchers (Ref #6 Lipscomb 1990). Work within the past two decades has provided vital knowledge regarding the mechanisms of aminopeptidases. The mechanism of
568:
transcripts, suggesting that presence of LAP-A alone is not sufficient to induce late gene expression. LAP-A is the first plant aminopeptidase shown to have a regulatory role in signal transduction pathway.
398:
come together to form the 353kDa bioactive LAP-A hexamer. Structures of the bovine lens LAP protomer and the biologically active hexamer have been constructed can be found through
Protein Data Bank (2J9A).
347:
in PepA and in bovine lens LAP have been found to be similar. Shown in the picture below is the proposed model for the active site of LAP-A in tomato based on the work of
Strater
64:
1158:"Hydrogen peroxide acts as a second messenger for the induction of defense genes in tomato plants in response to wounding, systemin, and methyl jasmonate"
513:
by herbivores (Johnson et al. 1989; Ryan 2000; Orozco-Cardenas 2001). Please see the
Picture 3 for a summary of the wound response in tomato.
2140:
28:
1765:
1395:
88:
496:, which is responsible for the synthesis of JA and several other potent signaling molecules, and ends in the regulation of two sets of
427:
In this mechanism, the bicarbonate ion acts as a general base. For LAP-A, R1 could be the R group of leucine, methionine, or arginine.
1839:
1240:"Expression of proteinase inhibitors I and II in transgenic tobacco plants: effects on natural defense against Manduca sexta larvae"
1750:
978:
941:
705:
662:
76:
559:(WT), (LapA-SI) plants that were silenced for LAP-A, and LapA-OX that constitutively expressed LAP-A. Late-gene expression was
69:
423:
385:
optima. At pH 8, the highest enzymatic activity is seen at 60 °C. PepA, bovine lens LAP and LAP-A are also known to form
1995:
377:
for their enzymatic activity
Enzymes are active in the presence of Mn, Mg and Zn. These enzymes are also known to have high
501:
decreasing the nutritional value of the food ingested or interfering with insect gut function (Walling 2000). For example,
1681:
1596:
395:
2110:
1614:
1064:
2145:
516:
974:"Overexpression, purification and biochemical characterization of the wound-induced leucine aminopeptidase of tomato"
701:"Overexpression, purification and biochemical characterization of the wound-induced leucine aminopeptidase of tomato"
1980:
2096:
2083:
2070:
2057:
2044:
2031:
2018:
1797:
1713:
1636:
1606:
1588:
1541:
1506:
1434:
1421:
1990:
937:"Identification of residues critical for activity of the wound-induced leucine aminopeptidase (LAP-A) of tomato"
658:"Identification of residues critical for activity of the wound-induced leucine aminopeptidase (LAP-A) of tomato"
339:
residues. Two Zn+2 cations are also shown, along with a water and a bicarbonate ion that acts as a general base.
1944:
1887:
1576:
1412:
1367:
196:
129:
1755:
850:"A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase"
597:"A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase"
1892:
1745:
1571:
1472:
1462:
1388:
2150:
1559:
1447:
1209:
Ryan CA (March 2000). "The systemin signaling pathway: differential activation of plant defensive genes".
906:
81:
1913:
1832:
1566:
1985:
551:
to have a regulatory role in the late wound response of tomato. Experiments were conducted using three
1157:
1740:
1549:
1253:
1116:
1024:
863:
757:
610:
493:
146:
1295:"Leucine aminopeptidase regulates defense and wound signaling in tomato downstream of jasmonic acid"
547:(LAP-A), a product of the octadecanoid pathway in some solanaceous plants, has been shown by Fowler
1949:
1699:
1661:
1645:
481:
2155:
1882:
1735:
1676:
1666:
1656:
1381:
1363:
1179:
1103:"Leucine aminopeptidase: bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis"
1089:
1050:
818:
783:
506:
408:
33:
Crystal structure of bovine leucyl aminopeptidase with co-ordinated zinc ions. Rendered from PDB
1730:
1623:
1326:
1281:
1226:
1197:
1144:
1081:
1042:
997:
960:
923:
891:
826:
775:
724:
681:
638:
441:
356:
34:
1928:
1923:
1897:
1825:
1780:
1775:
1651:
1316:
1308:
1271:
1261:
1218:
1187:
1171:
1134:
1124:
1073:
1032:
987:
950:
915:
881:
871:
810:
765:
714:
671:
628:
618:
485:
461:
445:
412:
359:
is very similar. PepA, bovine lens LAP, and LAP-A preferentially cleave N-terminal leucine,
331:
290:
150:
141:
1357:
1353:
1349:
134:
1975:
1959:
1872:
1785:
1770:
1725:
432:
LAPs between kingdoms, the mechanism of LAP-A may be similar to bovine lens LAP and PepA.
170:
1293:
Fowler JH, Narváez-Vásquez J, Aromdee DN, Pautot V, Holzer FM, Walling LL (April 2009).
1257:
1120:
1028:
867:
761:
614:
2124:
2013:
1954:
1806:
1442:
1321:
1299:
1294:
1162:
536:
1276:
1239:
1222:
1192:
505:
proteinase inhibitors (Pins) interfere with digestive proteases in the insect gut and
289:. Other N-terminal residues can also be cleaved, however. LAPs have been found across
2134:
1918:
1877:
1717:
1519:
1139:
1102:
992:
973:
955:
936:
886:
849:
719:
700:
676:
657:
633:
596:
528:
492:(JA)-mediated response (Walling 2000). This JA-mediated response revolves around the
489:
416:
1093:
801:
Hilbish TJ (1985). "The
Physiological Basis of Natural Selection at the Lap Locus".
1867:
1425:
1054:
1015:
787:
748:
394:. The Gu et al. from 1999 demonstrated that six 55kDA enzymatically inactive LAP-A
352:
1037:
1010:
770:
743:
105:
2091:
2026:
1862:
1671:
1618:
1554:
1514:
1373:
1211:
Biochimica et
Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
532:
382:
344:
336:
312:
180:
2119:
1245:
Proceedings of the
National Academy of Sciences of the United States of America
1108:
Proceedings of the
National Academy of Sciences of the United States of America
855:
Proceedings of the
National Academy of Sciences of the United States of America
602:
Proceedings of the
National Academy of Sciences of the United States of America
364:
278:
274:
267:
112:
876:
623:
2065:
2039:
1404:
1266:
1129:
552:
525:
510:
477:
1330:
1312:
1230:
1201:
1085:
1046:
1001:
964:
895:
830:
779:
728:
685:
642:
1285:
1148:
1077:
1011:"Binding structure of the leucine aminopeptidase inhibitor microginin FR1"
927:
744:"Binding structure of the leucine aminopeptidase inhibitor microginin FR1"
1408:
556:
469:
368:
360:
286:
282:
263:
117:
919:
199:
1183:
822:
465:
390:
386:
307:
298:
271:
259:
2078:
1848:
1494:
1487:
1482:
1345:
560:
535:
pathways (Ref Walling 2000). This particular pathway is inhibited by
502:
473:
449:
316:
294:
100:
1175:
1062:
Walling LL (June 2000). "The Myriad Plant Responses to Herbivores".
814:
448:, studies have demonstrated that LAP-A has a regulatory role in the
2052:
1529:
1524:
1457:
1452:
497:
371:
1009:
Kraft M, Schleberger C, Weckesser J, Schulz GE (December 2006).
742:
Kraft M, Schleberger C, Weckesser J, Schulz GE (December 2006).
509:(PPO) act to decrease the nutritive value of plant leaves after
93:
1821:
1377:
1156:
Orozco-Cárdenas ML, Narváez-Vásquez J, Ryan CA (January 2001).
848:
Sträter N, Sun L, Kantrowitz ER, Lipscomb WN (September 1999).
595:
Sträter N, Sun L, Kantrowitz ER, Lipscomb WN (September 1999).
480:, and mechanical wounding. These stresses activate specialized
565:
524:
The plant response in this octadecanoid pathway is similar to
374:
1348:
online database for peptidases and their inhibitors: Animal:
460:
In order to survive, plants must be able to respond to many
367:
residues. These enzymes are all metallopeptidases requiring
378:
1817:
2108:
1238:
Johnson R, Narvaez J, An G, Ryan C (December 1989).
2004:
1968:
1937:
1906:
1855:
1796:
1712:
1692:
1635:
1605:
1587:
1540:
1505:
1433:
1420:
520:
The wounding response pathway as studied in tomato.
176:
166:
161:
140:
128:
123:
111:
99:
87:
75:
63:
55:
47:
42:
21:
1101:Burley SK, David PR, Lipscomb WN (August 1991).
327:Enzyme description, structure, and active site
1833:
1389:
8:
972:Gu YQ, Holzer FM, Walling LL (August 1999).
699:Gu YQ, Holzer FM, Walling LL (August 1999).
578:concentrations in the external environment.
311:) LAP (also known as PepA or XerB), and the
1840:
1826:
1818:
1430:
1396:
1382:
1374:
158:
27:
1366:at the U.S. National Library of Medicine
1320:
1275:
1265:
1191:
1138:
1128:
1036:
991:
954:
885:
875:
769:
718:
675:
632:
622:
515:
422:
330:
2115:
587:
18:
293:. Identified LAPs include human LAP,
7:
1766:Amyloid precursor protein secretase
456:Background on plant immune response
1065:Journal of Plant Growth Regulation
14:
2118:
1751:Proteasome endopeptidase complex
993:10.1046/j.1432-1327.1999.00548.x
979:European Journal of Biochemistry
956:10.1046/j.1432-1327.2002.02795.x
942:European Journal of Biochemistry
935:Gu YQ, Walling LL (March 2002).
720:10.1046/j.1432-1327.1999.00548.x
706:European Journal of Biochemistry
677:10.1046/j.1432-1327.2002.02795.x
663:European Journal of Biochemistry
656:Gu YQ, Walling LL (March 2002).
315:-specific acidic LAP (LAP-A) in
1:
1615:Serine type carboxypeptidases
1597:Angiotensin-converting enzyme
1223:10.1016/S0167-4838(99)00269-1
1038:10.1016/j.febslet.2006.11.060
771:10.1016/j.febslet.2006.11.060
355:of the LAPs from these three
482:signal transduction pathways
351:. It is also known that the
2141:Genes on human chromosome 4
2172:
236:leucinamide aminopeptidase
1996:Michaelis–Menten kinetics
472:attack, piercing/sucking
157:
26:
1888:Diffusion-limited enzyme
1577:Tripeptidyl peptidase II
1368:Medical Subject Headings
877:10.1073/pnas.96.20.11151
624:10.1073/pnas.96.20.11151
228:L-leucine aminopeptidase
1746:Threonine endopeptidase
1572:Tripeptidyl peptidase I
1267:10.1073/pnas.86.24.9871
1130:10.1073/pnas.88.16.6916
1736:Aspartic acid protease
1560:Dipeptidyl peptidase-4
1313:10.1105/tpc.108.065029
521:
488:damage activating the
428:
340:
220:cytosol aminopeptidase
204:leucine aminopeptidase
193:Leucyl aminopeptidases
22:Leucine aminopeptidase
1981:Eadie–Hofstee diagram
1914:Allosteric regulation
1567:Tripeptidyl peptidase
1364:Leucyl+aminopeptidase
1078:10.1007/s003440000026
519:
440:Once thought of as a
426:
334:
1991:Lineweaver–Burk plot
1741:Metalloendopeptidase
1646:Metalloexopeptidases
1550:Dipeptidyl peptidase
543:Octadecanoid pathway
494:octadecanoid pathway
468:stresses, including
452:response in tomato.
321:Solanum lycopersicum
262:that preferentially
232:leucinaminopeptidase
1756:HslU—HslV peptidase
1700:Metalloexopeptidase
1258:1989PNAS...86.9871J
1121:1991PNAS...88.6916B
1029:2006FEBSL.580.6943K
920:10.1021/bi00045a021
868:1999PNAS...9611151S
762:2006FEBSL.580.6943K
615:1999PNAS...9611151S
507:polyphenol oxidases
444:necessary only for
436:Biological function
2146:Chemical pathology
1950:Enzyme superfamily
1883:Enzyme promiscuity
555:of tomato plants:
522:
429:
407:Historically, the
341:
252:aminopeptidase III
2106:
2105:
1815:
1814:
1764:Other/ungrouped:
1731:Cysteine protease
1708:
1707:
1626:
914:(45): 14792–800.
442:housekeeping gene
413:carboxypeptidases
248:aminopeptidase II
190:
189:
186:
185:
2163:
2123:
2122:
2114:
1986:Hanes–Woolf plot
1929:Enzyme activator
1924:Enzyme inhibitor
1898:Enzyme catalysis
1842:
1835:
1828:
1819:
1781:Beta-secretase 2
1776:Beta-secretase 1
1652:Carboxypeptidase
1648:
1624:
1431:
1398:
1391:
1384:
1375:
1334:
1324:
1289:
1279:
1269:
1234:
1205:
1195:
1152:
1142:
1132:
1097:
1058:
1040:
1005:
995:
968:
958:
931:
899:
889:
879:
835:
834:
809:(6): 1302–1317.
798:
792:
791:
773:
739:
733:
732:
722:
696:
690:
689:
679:
653:
647:
646:
636:
626:
592:
446:protein turnover
303:Escherichia coli
256:aminopeptidase I
244:proteinates FTBL
212:leucyl peptidase
159:
31:
19:
16:Class of enzymes
2171:
2170:
2166:
2165:
2164:
2162:
2161:
2160:
2131:
2130:
2129:
2117:
2109:
2107:
2102:
2014:Oxidoreductases
2000:
1976:Enzyme kinetics
1964:
1960:List of enzymes
1933:
1902:
1873:Catalytic triad
1851:
1846:
1816:
1811:
1792:
1786:Gamma secretase
1771:Alpha secretase
1726:Serine protease
1704:
1693:Other/ungrouped
1688:
1644:
1631:
1627:-Transpeptidase
1601:
1583:
1536:
1501:
1416:
1402:
1341:
1292:
1237:
1217:(1–2): 112–21.
1208:
1176:10.2307/3871162
1155:
1115:(16): 6916–20.
1100:
1061:
1008:
971:
934:
902:
862:(20): 11151–5.
847:
839:
838:
815:10.2307/2408787
800:
799:
795:
741:
740:
736:
698:
697:
693:
655:
654:
650:
609:(20): 11151–5.
594:
593:
589:
584:
575:
545:
458:
438:
405:
329:
38:
17:
12:
11:
5:
2169:
2167:
2159:
2158:
2153:
2148:
2143:
2133:
2132:
2128:
2127:
2104:
2103:
2101:
2100:
2087:
2074:
2061:
2048:
2035:
2022:
2008:
2006:
2002:
2001:
1999:
1998:
1993:
1988:
1983:
1978:
1972:
1970:
1966:
1965:
1963:
1962:
1957:
1952:
1947:
1941:
1939:
1938:Classification
1935:
1934:
1932:
1931:
1926:
1921:
1916:
1910:
1908:
1904:
1903:
1901:
1900:
1895:
1890:
1885:
1880:
1875:
1870:
1865:
1859:
1857:
1853:
1852:
1847:
1845:
1844:
1837:
1830:
1822:
1813:
1812:
1810:
1809:
1807:Staphylokinase
1803:
1801:
1794:
1793:
1791:
1790:
1789:
1788:
1783:
1778:
1773:
1761:
1760:
1759:
1758:
1753:
1743:
1738:
1733:
1728:
1722:
1720:
1710:
1709:
1706:
1705:
1703:
1702:
1696:
1694:
1690:
1689:
1687:
1686:
1685:
1684:
1679:
1674:
1669:
1664:
1659:
1649:
1641:
1639:
1633:
1632:
1630:
1629:
1621:
1611:
1609:
1603:
1602:
1600:
1599:
1593:
1591:
1585:
1584:
1582:
1581:
1580:
1579:
1574:
1564:
1563:
1562:
1557:
1546:
1544:
1538:
1537:
1535:
1534:
1533:
1532:
1527:
1522:
1511:
1509:
1503:
1502:
1500:
1499:
1498:
1497:
1492:
1491:
1490:
1485:
1475:
1470:
1465:
1460:
1455:
1450:
1443:Aminopeptidase
1439:
1437:
1428:
1418:
1417:
1403:
1401:
1400:
1393:
1386:
1378:
1372:
1371:
1361:
1340:
1339:External links
1337:
1336:
1335:
1307:(4): 1239–51.
1300:The Plant Cell
1290:
1252:(24): 9871–5.
1235:
1206:
1163:The Plant Cell
1153:
1098:
1072:(2): 195–216.
1059:
1023:(30): 6943–7.
1006:
969:
949:(6): 1630–40.
932:
900:
844:
843:
837:
836:
793:
756:(30): 6943–7.
734:
691:
670:(6): 1630–40.
648:
586:
585:
583:
580:
574:
573:Osmoregulation
571:
544:
541:
537:salicylic acid
457:
454:
437:
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2151:Tumor markers
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1997:
1994:
1992:
1989:
1987:
1984:
1982:
1979:
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1974:
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1971:
1967:
1961:
1958:
1956:
1955:Enzyme family
1953:
1951:
1948:
1946:
1943:
1942:
1940:
1936:
1930:
1927:
1925:
1922:
1920:
1919:Cooperativity
1917:
1915:
1912:
1911:
1909:
1905:
1899:
1896:
1894:
1891:
1889:
1886:
1884:
1881:
1879:
1878:Oxyanion hole
1876:
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1861:
1860:
1858:
1854:
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1843:
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1802:
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1729:
1727:
1724:
1723:
1721:
1719:
1718:Endopeptidase
1715:
1711:
1701:
1698:
1697:
1695:
1691:
1683:
1680:
1678:
1675:
1673:
1670:
1668:
1665:
1663:
1660:
1658:
1655:
1654:
1653:
1650:
1647:
1643:
1642:
1640:
1638:
1634:
1628:
1622:
1620:
1616:
1613:
1612:
1610:
1608:
1604:
1598:
1595:
1594:
1592:
1590:
1586:
1578:
1575:
1573:
1570:
1569:
1568:
1565:
1561:
1558:
1556:
1553:
1552:
1551:
1548:
1547:
1545:
1543:
1539:
1531:
1528:
1526:
1523:
1521:
1518:
1517:
1516:
1513:
1512:
1510:
1508:
1504:
1496:
1493:
1489:
1486:
1484:
1481:
1480:
1479:
1476:
1474:
1471:
1469:
1466:
1464:
1461:
1459:
1456:
1454:
1451:
1449:
1446:
1445:
1444:
1441:
1440:
1438:
1436:
1432:
1429:
1427:
1423:
1419:
1414:
1410:
1406:
1399:
1394:
1392:
1387:
1385:
1380:
1379:
1376:
1369:
1365:
1362:
1359:
1355:
1351:
1347:
1343:
1342:
1338:
1332:
1328:
1323:
1318:
1314:
1310:
1306:
1302:
1301:
1296:
1291:
1287:
1283:
1278:
1273:
1268:
1263:
1259:
1255:
1251:
1247:
1246:
1241:
1236:
1232:
1228:
1224:
1220:
1216:
1212:
1207:
1203:
1199:
1194:
1189:
1185:
1181:
1177:
1173:
1170:(1): 179–91.
1169:
1165:
1164:
1159:
1154:
1150:
1146:
1141:
1136:
1131:
1126:
1122:
1118:
1114:
1110:
1109:
1104:
1099:
1095:
1091:
1087:
1083:
1079:
1075:
1071:
1067:
1066:
1060:
1056:
1052:
1048:
1044:
1039:
1034:
1030:
1026:
1022:
1018:
1017:
1012:
1007:
1003:
999:
994:
989:
986:(3): 726–35.
985:
981:
980:
975:
970:
966:
962:
957:
952:
948:
944:
943:
938:
933:
929:
925:
921:
917:
913:
909:
908:
901:
897:
893:
888:
883:
878:
873:
869:
865:
861:
857:
856:
851:
846:
845:
841:
840:
832:
828:
824:
820:
816:
812:
808:
804:
797:
794:
789:
785:
781:
777:
772:
767:
763:
759:
755:
751:
750:
745:
738:
735:
730:
726:
721:
716:
713:(3): 726–35.
712:
708:
707:
702:
695:
692:
687:
683:
678:
673:
669:
665:
664:
659:
652:
649:
644:
640:
635:
630:
625:
620:
616:
612:
608:
604:
603:
598:
591:
588:
581:
579:
572:
570:
567:
562:
558:
554:
550:
542:
540:
538:
534:
530:
529:prostaglandin
527:
518:
514:
512:
508:
504:
499:
495:
491:
490:jasmonic acid
487:
483:
479:
475:
471:
467:
463:
455:
453:
451:
447:
443:
435:
433:
425:
421:
418:
414:
410:
402:
400:
397:
393:
392:
388:
384:
380:
376:
373:
370:
366:
362:
358:
354:
350:
346:
338:
333:
326:
324:
322:
318:
314:
310:
309:
304:
300:
296:
292:
291:superkingdoms
288:
284:
280:
276:
273:
269:
265:
261:
257:
253:
249:
245:
241:
240:FTBL proteins
237:
233:
229:
225:
224:cathepsin III
221:
217:
213:
209:
205:
201:
198:
194:
182:
179:
175:
172:
169:
165:
160:
156:
153:
152:
148:
145:
143:
139:
136:
133:
131:
127:
122:
119:
116:
114:
110:
107:
104:
102:
98:
95:
92:
90:
86:
83:
80:
78:
74:
71:
68:
66:
62:
58:
54:
50:
46:
41:
36:
30:
25:
20:
2092:Translocases
2089:
2076:
2063:
2050:
2037:
2027:Transferases
2024:
2011:
1868:Binding site
1682:Glutamate II
1477:
1467:
1426:Exopeptidase
1304:
1298:
1249:
1243:
1214:
1210:
1167:
1161:
1112:
1106:
1069:
1063:
1020:
1016:FEBS Letters
1014:
983:
977:
946:
940:
911:
907:Biochemistry
905:
859:
853:
806:
802:
796:
753:
749:FEBS Letters
747:
737:
710:
704:
694:
667:
661:
651:
606:
600:
590:
576:
548:
546:
523:
459:
439:
430:
417:endoprotease
406:
403:Mechanism(s)
389:
353:biochemistry
348:
345:active sites
342:
320:
306:
302:
255:
251:
247:
243:
239:
235:
231:
227:
223:
219:
215:
211:
207:
203:
192:
191:
149:
56:Alt. symbols
1863:Active site
1619:Cathepsin A
1555:Cathepsin C
1515:Dipeptidase
1352:, Bacteria:
533:leukotriene
383:temperature
381:(pH 8) and
337:active site
313:solanaceous
216:peptidase S
171:Swiss-model
43:Identifiers
2135:Categories
2066:Isomerases
2040:Hydrolases
1907:Regulation
582:References
409:mechanisms
365:methionine
297:lens LAP,
279:N-terminus
268:hydrolysis
167:Structures
162:Search for
124:Other data
2156:EC 3.4.11
1945:EC number
1800:: Unknown
1478:Methionyl
1409:proteases
1405:Hydrolase
1356:, Plant::
803:Evolution
561:inhibited
553:genotypes
526:mammalian
511:ingestion
478:herbivory
396:protomers
130:EC number
106:NM_015907
65:NCBI gene
1969:Kinetics
1893:Cofactor
1856:Activity
1473:Glutamyl
1463:Cystinyl
1458:Aspartyl
1331:19376935
1231:10708853
1202:11158538
1094:11842328
1086:11038228
1047:17157838
1002:10469136
965:11895433
896:10500145
831:28564261
780:17157838
729:10469136
686:11895433
643:10500145
557:wildtype
470:pathogen
387:hexamers
369:divalent
361:arginine
357:kingdoms
287:proteins
283:peptides
275:residues
264:catalyze
200:3.4.11.1
181:InterPro
135:3.4.11.1
2125:Biology
2079:Ligases
1849:Enzymes
1453:Arginyl
1448:Alanine
1358:M17.002
1354:M17.003
1350:M17.001
1322:2685619
1286:2602379
1254:Bibcode
1184:3871162
1149:1871107
1117:Bibcode
1055:6425967
1025:Bibcode
928:7578088
864:Bibcode
842:Sources
823:2408787
788:6425967
758:Bibcode
611:Bibcode
474:insects
466:abiotic
391:in vivo
375:cations
308:E. coli
299:porcine
277:at the
272:leucine
260:enzymes
177:Domains
113:UniProt
2111:Portal
2053:Lyases
1798:3.4.99
1714:3.4.21
1637:3.4.17
1607:3.4.16
1589:3.4.15
1542:3.4.14
1507:3.4.13
1468:Leucyl
1435:3.4.11
1422:3.4.11
1370:(MeSH)
1346:MEROPS
1329:
1319:
1284:
1277:298604
1274:
1229:
1200:
1193:102208
1190:
1182:
1147:
1137:
1092:
1084:
1053:
1045:
1000:
963:
926:
894:
884:
829:
821:
786:
778:
727:
684:
641:
631:
549:et al.
503:serine
486:tissue
462:biotic
450:immune
363:, and
335:LAP-A
317:tomato
295:bovine
258:) are
151:p15.33
147:Chr. 4
118:P28838
101:RefSeq
94:170250
48:Symbol
2005:Types
1716:-25:
1424:-19:
1180:JSTOR
1140:52204
1090:S2CID
1051:S2CID
887:18002
819:JSTOR
784:S2CID
634:18002
498:genes
372:metal
349:et al
301:LAP,
142:Locus
82:18449
70:51056
2097:list
2090:EC7
2084:list
2077:EC6
2071:list
2064:EC5
2058:list
2051:EC4
2045:list
2038:EC3
2032:list
2025:EC2
2019:list
2012:EC1
1415:3.4)
1344:The
1327:PMID
1282:PMID
1227:PMID
1215:1477
1198:PMID
1145:PMID
1082:PMID
1043:PMID
998:PMID
961:PMID
924:PMID
892:PMID
827:PMID
776:PMID
725:PMID
682:PMID
639:PMID
531:and
464:and
415:and
343:The
285:and
266:the
208:LAPs
89:OMIM
77:HGNC
59:PEPS
35:1BLL
1317:PMC
1309:doi
1272:PMC
1262:doi
1219:doi
1188:PMC
1172:doi
1135:PMC
1125:doi
1074:doi
1033:doi
1021:580
988:doi
984:263
951:doi
947:269
916:doi
882:PMC
872:doi
811:doi
766:doi
754:580
715:doi
711:263
672:doi
668:269
629:PMC
619:doi
566:RNA
411:of
323:).
281:of
270:of
51:LAP
2137::
1662:A2
1625:DD
1617::
1413:EC
1407::
1325:.
1315:.
1305:21
1303:.
1297:.
1280:.
1270:.
1260:.
1250:86
1248:.
1242:.
1225:.
1213:.
1196:.
1186:.
1178:.
1168:13
1166:.
1160:.
1143:.
1133:.
1123:.
1113:88
1111:.
1105:.
1088:.
1080:.
1070:19
1068:.
1049:.
1041:.
1031:.
1019:.
1013:.
996:.
982:.
976:.
959:.
945:.
939:.
922:.
912:34
910:.
890:.
880:.
870:.
860:96
858:.
852:.
825:.
817:.
807:39
805:.
782:.
774:.
764:.
752:.
746:.
723:.
709:.
703:.
680:.
666:.
660:.
637:.
627:.
617:.
607:96
605:.
599:.
539:.
476:,
379:pH
254:,
250:,
246:,
242:,
238:,
234:,
230:,
226:,
222:,
218:,
214:,
210:,
206:,
202:,
197:EC
2113::
2099:)
2095:(
2086:)
2082:(
2073:)
2069:(
2060:)
2056:(
2047:)
2043:(
2034:)
2030:(
2021:)
2017:(
1841:e
1834:t
1827:v
1677:E
1672:C
1667:B
1657:A
1530:3
1525:2
1520:1
1495:O
1488:2
1483:1
1411:(
1397:e
1390:t
1383:v
1360:.
1333:.
1311::
1288:.
1264::
1256::
1233:.
1221::
1204:.
1174::
1151:.
1127::
1119::
1096:.
1076::
1057:.
1035::
1027::
1004:.
990::
967:.
953::
930:.
918::
898:.
874::
866::
833:.
813::
790:.
768::
760::
731:.
717::
688:.
674::
645:.
621::
613::
319:(
305:(
195:(
37:.
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