371:
298:
29:
2215:
289:(350 kDa). This is cleaved into functional units by the three proteases: P1 protease (1 cleavage site), helper-component protease (1 cleavage site) and TEV protease (7 cleavage sites). The native TEV protease also contains an internal self-cleavage site. This site is slowly cleaved to inactivate the enzyme (the physiological reason for this is unknown).
362:, split between the two barrels (Asp on β1 and His and Cys on β2). The substrate is held as a β-sheet, forming an antiparallel interaction with the cleft between the barrels and a parallel interaction with the C-terminal tail. The enzyme therefore forms a binding tunnel around the substrate and side chain interactions control specificity.
413:). The highest cleavage is of sequences closest to the consensus EXLYΦQ\φ where X is any residue, Φ is any large or medium hydrophobe and φ is any small hydrophobic or polar residue. Although this sequence is the optimal, sequences with disfavoured residues at some positions can still be cleaved if the rest of the sequence is optimal.
459:
However, TEV protease does have limitations as a biochemical tool. It is prone to deactivation by self-cleavage (autolysis), though this can be abolished through a single S219V mutation in the internal cleavage site. The protease expressed alone is also poorly soluble, however several attempts have
471:
TEV protease has been reported to show a 10-fold loss of activity at 4 °C. TEV protease shows loss of activity at temperatures above 34 °C. The original TEV protease required the presence of reducing agent for high activity, which could interfere with the function of proteins containing
428:
In particular, peptide side chain P6-Glu contacts a network of three hydrogen bonds; P5-Asn points into the solvent, making no specific interactions (hence the absence of substrate consensus at this position); P4-Leu is buried in a hydrophobic pocket; P3-Tyr is held in a hydrophobic pocket with a
424:
with only one or two pockets that bind the substrate side chains. Conversely, viral proteases such as TEV protease have a long C-terminal tail which completely covers the substrate to create a binding tunnel. This tunnel contains a set of tight binding pockets such that each side chain of the
408:
Studies have subsequently used sequencing of cleaved substrates from a pool of randomised sequences to determine preference patterns. Although ENLYFQ\S is the optimal sequence, the protease is active to a greater or lesser extent on a range of substrates (i.e. shows some
445:. The reason for the use of TEV protease as a biochemical tool is its high sequence specificity. This specificity allows for the controlled cleavage of proteins when the preference sequence is inserted into flexible loops. It also makes TEV protease relatively non-toxic
405:. Residues of the substrate are labelled P6 to P1 before the cut site and P1’ after the cut site. Early works also measured cleavage of an array of similar substrates to characterise how specific the protease was for the native sequence.
400:
The preferred, native cleavage sequence was first identified by examining the cut sites in the native polyprotein substrate for recurring sequence. The consensus for these native cut sites is ENLYFQ\S where ‘\’ denotes the
429:
short hydrogen bond at the end; P2-Phe is also surrounded by hydrophobes including the face of the triad histidine; P1-Gln forms four hydrogen bonds; and P1’-Ser is only partly enclosed in a shallow hydrophobic groove.
1412:
Correnti CE, Gewe MM, Mehlin C, Bandaranayake AD, Johnsen WA, Rupert PB, Brusniak MY, Clarke M, Burke SE, De Van Der
Schueren W, Pilat K, Turnbaugh SM, May D, Watson A, Chan MK, Bahl CD, Olson JM, Strong RK (2018).
1320:
Nallamsetty S, Kapust RB, Tözsér J, Cherry S, Tropea JE, Copeland TD, Waugh DS (November 2004). "Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease
1034:
Parks TD, Leuther KK, Howard ED, Johnston SA, Dougherty WG (February 1994). "Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase".
188:
768:
Dougherty WG, Parks TD, Cary SM, Bazan JF, Fletterick RJ (September 1989). "Characterization of the catalytic residues of the tobacco etch virus 49-kDa proteinase".
207:
472:
disulfide bonds. After incorporation of various mutations, later "superTEV protease" versions are highly active in the presence or absence of reducing agent.
1567:
929:
Boulware KT, Jabaiah A, Daugherty PS (June 2010). "Evolutionary optimization of peptide substrates for proteases that exhibit rapid hydrolysis kinetics".
1187:
Verhoeven KD, Altstadt OC, Savinov SN (March 2012). "Intracellular detection and evolution of site-specific proteases using a genetic selection system".
876:
Kapust, Rachel B.; Tözsér, József; Copeland, Terry D.; Waugh, David S. (2002-06-28). "The P1' specificity of tobacco etch virus protease".
1934:
1531:
200:
1560:
838:
Dougherty WG, Cary SM, Parks TD (August 1989). "Molecular genetic analysis of a plant virus polyprotein cleavage site: a model".
1232:"Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency"
711:"Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications"
604:"A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing"
328:
167:
143:
2090:
1718:
1713:
1553:
254:-like proteases. Due to its high sequence specificity, TEV protease is frequently used for the controlled cleavage of
2205:
803:
Tyndall JD, Nall T, Fairlie DP (March 2005). "Proteases universally recognize beta strands in their active sites".
442:
2075:
2191:
2178:
2165:
2152:
2139:
2126:
2113:
1587:
161:
2085:
2039:
1982:
1584:
228:
54:
148:
668:
Phan J, Zdanov A, Evdokimov AG, Tropea JE, Peters HK, Kapust RB, Li M, Wlodawer A, Waugh DS (December 2002).
1987:
1778:
1071:"Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial libraries"
465:
564:
Kapust RB, Waugh DS (July 2000). "Controlled intracellular processing of fusion proteins by TEV protease".
475:
The molecular weight of this enzyme varies between 25 and 27 kDa depending on the specific construct used.
885:
212:
977:"Substrate profiling of tobacco etch virus protease using a novel fluorescence-assisted whole-cell assay"
136:
2008:
1927:
410:
386:
tunnel (left). A cutaway (right) shows the complementary shape of the binding tunnel to the substrate. (
375:
316:
269:. The consensus sequence recognized by TEV protease is Glu-Asn-Leu-Tyr-Phe-Gln-|-Ser, where "|" denotes
2080:
71:
1462:
Keeble AH, Turkki P, Stokes S, Khairil Anuar IN, Rahikainen R, Hytönen VP, Howarth M (December 2019).
33:
TEV protease (white) complexed with peptide substrate (black) with active site triad residues (red). (
1475:
1141:
1082:
988:
722:
615:
355:
etc.), TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases).
301:
Structure of TEV protease. The double β-barrels that define the superfamily are highlighted in red. (
890:
164:
2044:
1871:
324:
88:
66:
2240:
2235:
1977:
1212:
954:
461:
453:
416:
Specificity is endowed by the large contact area between enzyme and substrate. Proteases such as
282:
243:
1415:"Screening, large-scale production and structure-based classification of cystine-dense peptides"
370:
1580:
1503:
1444:
1394:
1345:
1302:
1253:
1204:
1169:
1110:
1051:
1016:
946:
911:
903:
855:
820:
785:
750:
691:
643:
581:
543:
464:
and computational design. It has also been shown that expression can be improved by fusion to
388:
303:
239:
155:
35:
2023:
2018:
1992:
1920:
1891:
1783:
1773:
1768:
1763:
1758:
1545:
1493:
1483:
1434:
1426:
1384:
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1337:
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1284:
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681:
633:
623:
573:
533:
525:
340:
124:
1738:
1230:
Kapust RB, Tözsér J, Fox JD, Anderson DE, Cherry S, Copeland TD, Waugh DS (December 2001).
297:
2070:
2054:
1967:
1535:
379:
359:
255:
100:
59:
1479:
1145:
1086:
992:
726:
619:
456:
has been used to change the preferred residue either before or after the cleavage site.
2219:
2108:
2049:
1528:
1498:
1463:
1439:
1414:
1389:
1364:
1297:
1273:"Differential temperature dependence of tobacco etch virus and rhinovirus 3C proteases"
1272:
1164:
1129:
1105:
1070:
1011:
976:
538:
513:
421:
183:
1130:"A tobacco etch virus protease with increased substrate tolerance at the P1' position"
899:
745:
710:
638:
603:
2229:
2013:
1972:
958:
851:
781:
438:
1216:
420:
have specificity for one residue before and after the cleaved bond due to a shallow
28:
1962:
1830:
1826:
452:
Although rational design has had limited success in changing protease specificity,
251:
1464:"Approaching infinite affinity through engineering of peptide-protein interaction"
1540:
1154:
1001:
2186:
2121:
1957:
1901:
1896:
1866:
1850:
1845:
1840:
1835:
1821:
1816:
1811:
1806:
1801:
1248:
1231:
402:
383:
320:
286:
270:
2214:
1468:
Proceedings of the
National Academy of Sciences of the United States of America
1365:"Enhancing the stability and solubility of TEV protease using in silico design"
670:"Structural basis for the substrate specificity of tobacco etch virus protease"
1881:
1695:
1664:
1659:
1654:
1649:
1430:
1341:
1200:
514:"MEROPS: the database of proteolytic enzymes, their substrates and inhibitors"
1363:
Cabrita LD, Gilis D, Robertson AL, Dehouck Y, Rooman M, Bottomley SP (2007).
1288:
907:
2160:
2134:
1886:
1793:
1748:
1743:
1733:
1723:
1690:
1644:
1639:
1634:
1629:
1624:
1619:
1614:
1609:
1604:
1488:
1095:
735:
628:
425:
substrate peptide (P6 to P1’) is bound in a complementary site (S6 to S1’).
1507:
1448:
1398:
1349:
1306:
1257:
1208:
1173:
1114:
1047:
1020:
950:
915:
824:
695:
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669:
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577:
547:
1055:
859:
789:
754:
647:
1876:
1576:
1523:
1380:
529:
495:
352:
348:
259:
231:
112:
1271:
Raran-Kurussi S, Tözsér J, Cherry S, Tropea JE, Waugh DS (15 May 2013).
1705:
1596:
417:
344:
332:
265:
247:
131:
1069:
Yi L, Gebhard MC, Li Q, Taft JM, Georgiou G, Iverson BL (April 2013).
942:
816:
392:
307:
39:
2173:
1943:
1753:
1685:
1680:
336:
195:
107:
95:
83:
2147:
1728:
296:
119:
1916:
1549:
1912:
449:
as the recognized sequence scarcely occurs in proteins.
2203:
437:
One of the main uses of this protein is for removing
358:
Covalent catalysis is performed with an Asp-His-Cys
236:
Tobacco Etch Virus nuclear-inclusion-a endopeptidase
2099:
2063:
2032:
2001:
1950:
1859:
1792:
1704:
1673:
1595:
878:
512:Rawlings ND, Barrett AJ, Bateman A (January 2012).
206:
194:
182:
177:
154:
142:
130:
118:
106:
94:
82:
77:
65:
53:
48:
21:
468:(MBP) which acts a solubility-enhancing partner.
339:classification). Although homologous to cellular
315:The structure of TEV protease has been solved by
970:
968:
663:
661:
659:
657:
559:
557:
507:
505:
285:encodes its entire genome as a single massive
1928:
1561:
975:Kostallas G, Löfdahl PÅ, Samuelson P (2011).
597:
595:
8:
460:been made to improve its solubility through
323:and a flexible C-terminal tail and displays
1935:
1921:
1913:
1568:
1554:
1546:
174:
1497:
1487:
1438:
1388:
1296:
1247:
1163:
1153:
1128:Renicke C, Spadaccini R, Taxis C (2013).
1104:
1094:
1010:
1000:
889:
744:
734:
709:Bazan JF, Fletterick RJ (November 1988).
685:
637:
627:
537:
602:Carrington JC, Dougherty WG (May 1988).
374:Surface model of TEV bound to uncleaved
369:
2210:
483:
18:
871:
869:
382:(red). The substrate binds inside an
7:
489:
487:
14:
1541:National Cancer Institute TEV FAQ
433:Application as a biochemical tool
22:nuclear-inclusion-a endopeptidase
2213:
238:) is a highly sequence-specific
27:
1:
900:10.1016/S0006-291X(02)00574-0
246:(TEV). It is a member of the
1155:10.1371/journal.pone.0067915
1075:Proc. Natl. Acad. Sci. U.S.A
1002:10.1371/journal.pone.0016136
852:10.1016/0042-6822(89)90603-X
782:10.1016/0042-6822(89)90132-3
715:Proc. Natl. Acad. Sci. U.S.A
608:Proc. Natl. Acad. Sci. U.S.A
524:(Database issue): D343–50.
443:recombinant fusion proteins
2257:
1524:TEV polyprotein on UniProt
493:UniProt: TEV polyprotein:
378:(black), also showing the
2091:Michaelis–Menten kinetics
1431:10.1038/s41594-018-0033-9
1342:10.1016/j.pep.2004.08.016
1249:10.1093/protein/14.12.993
1201:10.1007/s12010-011-9522-6
1189:Appl. Biochem. Biotechnol
173:
26:
1983:Diffusion-limited enzyme
1289:10.1016/j.ab.2013.01.031
319:. It is composed of two
16:Highly specific protease
1489:10.1073/pnas.1909653116
1277:Analytical Biochemistry
1096:10.1073/pnas.1215994110
736:10.1073/pnas.85.21.7872
629:10.1073/pnas.85.10.3391
466:maltose binding protein
1529:TEV protease on MEROPS
1048:10.1006/abio.1994.1060
687:10.1074/jbc.M207224200
578:10.1006/prep.2000.1251
397:
312:
293:Structure and function
2076:Eadie–Hofstee diagram
2009:Allosteric regulation
411:substrate promiscuity
373:
317:X-ray crystallography
300:
2086:Lineweaver–Burk plot
1381:10.1110/ps.072822507
403:cleaved peptide bond
327:to the chymotrypsin
271:cleaved peptide bond
1872:Cancer procoagulant
1480:2019PNAS..11626523K
1474:(52): 26523–26533.
1419:Nat Struct Mol Biol
1330:Protein Expr. Purif
1146:2013PLoSO...867915R
1087:2013PNAS..110.7229Y
993:2011PLoSO...616136K
727:1988PNAS...85.7872B
620:1988PNAS...85.3391C
566:Protein Expr. Purif
325:structural homology
2045:Enzyme superfamily
1978:Enzyme promiscuity
1581:cysteine proteases
1534:2016-03-03 at the
931:Biotechnol. Bioeng
530:10.1093/nar/gkr987
462:directed evolution
454:directed evolution
398:
313:
283:tobacco etch virus
244:Tobacco Etch Virus
2201:
2200:
1910:
1909:
943:10.1002/bit.22693
817:10.1021/cr040669e
518:Nucleic Acids Res
240:cysteine protease
222:
221:
218:
217:
137:metabolic pathway
2248:
2218:
2217:
2209:
2081:Hanes–Woolf plot
2024:Enzyme activator
2019:Enzyme inhibitor
1993:Enzyme catalysis
1937:
1930:
1923:
1914:
1892:3C-like protease
1570:
1563:
1556:
1547:
1512:
1511:
1501:
1491:
1459:
1453:
1452:
1442:
1409:
1403:
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1392:
1360:
1354:
1353:
1317:
1311:
1310:
1300:
1268:
1262:
1261:
1251:
1242:(12): 993–1000.
1227:
1221:
1220:
1184:
1178:
1177:
1167:
1157:
1125:
1119:
1118:
1108:
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1031:
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1004:
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828:
800:
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793:
765:
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758:
748:
738:
706:
700:
699:
689:
680:(52): 50564–72.
665:
652:
651:
641:
631:
599:
590:
589:
561:
552:
551:
541:
509:
500:
499:
491:
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341:serine proteases
310:
175:
42:
31:
19:
2256:
2255:
2251:
2250:
2249:
2247:
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2245:
2226:
2225:
2224:
2212:
2204:
2202:
2197:
2109:Oxidoreductases
2095:
2071:Enzyme kinetics
2059:
2055:List of enzymes
2028:
1997:
1968:Catalytic triad
1946:
1941:
1911:
1906:
1855:
1788:
1700:
1669:
1591:
1574:
1536:Wayback Machine
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1185:
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1126:
1122:
1081:(18): 7229–34.
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1028:
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891:10.1.1.375.4271
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380:catalytic triad
368:
335:, C4 family by
302:
295:
279:
256:fusion proteins
44:
34:
17:
12:
11:
5:
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2033:Classification
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2016:
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1518:External links
1516:
1514:
1513:
1454:
1425:(3): 270–278.
1404:
1375:(11): 2360–7.
1355:
1336:(1): 108–115.
1312:
1283:(2): 142–144.
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1222:
1195:(5): 1340–54.
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1120:
1061:
1026:
964:
921:
884:(5): 949–955.
865:
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795:
760:
721:(21): 7872–6.
701:
653:
614:(10): 3391–5.
591:
553:
501:
482:
480:
477:
441:from purified
434:
431:
367:
364:
331:of proteases (
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2050:Enzyme family
2048:
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2041:
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2017:
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2014:Cooperativity
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1973:Oxyanion hole
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1956:
1955:
1953:
1949:
1945:
1938:
1933:
1931:
1926:
1924:
1919:
1918:
1915:
1903:
1900:
1898:
1895:
1893:
1890:
1888:
1885:
1883:
1880:
1878:
1875:
1873:
1870:
1868:
1865:
1864:
1862:
1858:
1852:
1849:
1847:
1844:
1842:
1839:
1837:
1834:
1832:
1828:
1825:
1823:
1820:
1818:
1815:
1813:
1810:
1808:
1805:
1803:
1800:
1799:
1797:
1795:
1791:
1785:
1782:
1780:
1777:
1775:
1772:
1770:
1767:
1765:
1762:
1760:
1757:
1755:
1752:
1750:
1747:
1745:
1742:
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1737:
1735:
1732:
1730:
1727:
1725:
1722:
1720:
1717:
1715:
1712:
1711:
1709:
1707:
1703:
1697:
1694:
1692:
1689:
1687:
1684:
1682:
1679:
1678:
1676:
1674:Fruit-derived
1672:
1666:
1663:
1661:
1658:
1656:
1653:
1651:
1648:
1646:
1643:
1641:
1638:
1636:
1633:
1631:
1628:
1626:
1623:
1621:
1618:
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1613:
1611:
1608:
1606:
1603:
1602:
1600:
1598:
1594:
1589:
1586:
1582:
1578:
1571:
1566:
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1557:
1552:
1551:
1548:
1542:
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1537:
1533:
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1527:
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1522:
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1517:
1509:
1505:
1500:
1495:
1490:
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1481:
1477:
1473:
1469:
1465:
1458:
1455:
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1446:
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1436:
1432:
1428:
1424:
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1416:
1408:
1405:
1400:
1396:
1391:
1386:
1382:
1378:
1374:
1370:
1366:
1359:
1356:
1351:
1347:
1343:
1339:
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1331:
1327:
1323:
1316:
1313:
1308:
1304:
1299:
1294:
1290:
1286:
1282:
1278:
1274:
1267:
1264:
1259:
1255:
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1245:
1241:
1237:
1233:
1226:
1223:
1218:
1214:
1210:
1206:
1202:
1198:
1194:
1190:
1183:
1180:
1175:
1171:
1166:
1161:
1156:
1151:
1147:
1143:
1140:(6): e67915.
1139:
1135:
1131:
1124:
1121:
1116:
1112:
1107:
1102:
1097:
1092:
1088:
1084:
1080:
1076:
1072:
1065:
1062:
1057:
1053:
1049:
1045:
1041:
1037:
1036:Anal. Biochem
1030:
1027:
1022:
1018:
1013:
1008:
1003:
998:
994:
990:
987:(1): e16136.
986:
982:
978:
971:
969:
965:
960:
956:
952:
948:
944:
940:
937:(3): 339–46.
936:
932:
925:
922:
917:
913:
909:
905:
901:
897:
892:
887:
883:
879:
872:
870:
866:
861:
857:
853:
849:
846:(2): 356–64.
845:
841:
834:
831:
826:
822:
818:
814:
811:(3): 973–99.
810:
806:
799:
796:
791:
787:
783:
779:
776:(1): 302–10.
775:
771:
764:
761:
756:
752:
747:
742:
737:
732:
728:
724:
720:
716:
712:
705:
702:
697:
693:
688:
683:
679:
675:
674:J. Biol. Chem
671:
664:
662:
660:
658:
654:
649:
645:
640:
635:
630:
625:
621:
617:
613:
609:
605:
598:
596:
592:
587:
583:
579:
575:
571:
567:
560:
558:
554:
549:
545:
540:
535:
531:
527:
523:
519:
515:
508:
506:
502:
497:
490:
488:
484:
478:
476:
473:
469:
467:
463:
457:
455:
450:
448:
444:
440:
439:affinity tags
432:
430:
426:
423:
422:binding cleft
419:
414:
412:
406:
404:
394:
390:
385:
381:
377:
372:
365:
363:
361:
356:
354:
350:
346:
342:
338:
334:
330:
326:
322:
318:
309:
305:
299:
292:
290:
288:
284:
276:
274:
272:
268:
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262:
261:
257:
253:
249:
245:
241:
237:
233:
230:
226:
214:
211:
209:
205:
202:
199:
197:
193:
190:
187:
185:
181:
176:
172:
169:
166:
163:
160:
157:
153:
150:
147:
145:
141:
138:
135:
133:
129:
126:
123:
121:
117:
114:
113:NiceZyme view
111:
109:
105:
102:
99:
97:
93:
90:
87:
85:
81:
76:
73:
70:
68:
64:
61:
58:
56:
52:
47:
41:
37:
30:
25:
20:
2187:Translocases
2184:
2171:
2158:
2145:
2132:
2122:Transferases
2119:
2106:
1963:Binding site
1471:
1467:
1457:
1422:
1418:
1407:
1372:
1368:
1358:
1333:
1329:
1325:
1321:
1315:
1280:
1276:
1266:
1239:
1235:
1225:
1192:
1188:
1182:
1137:
1133:
1123:
1078:
1074:
1064:
1042:(2): 413–7.
1039:
1035:
1029:
984:
980:
934:
930:
924:
881:
877:
843:
839:
833:
808:
804:
798:
773:
769:
763:
718:
714:
704:
677:
673:
611:
607:
572:(2): 312–8.
569:
565:
521:
517:
474:
470:
458:
451:
446:
436:
427:
415:
407:
399:
357:
314:
280:
264:
258:
252:chymotrypsin
235:
225:TEV protease
224:
223:
101:BRENDA entry
72:139946-51-3
1958:Active site
1902:Gingipain K
1897:Gingipain R
1867:Clostripain
1369:Protein Sci
1236:Protein Eng
384:active site
366:Specificity
329:superfamily
287:polyprotein
89:IntEnz view
49:Identifiers
2230:Categories
2161:Isomerases
2135:Hydrolases
2002:Regulation
1882:Autophagin
1696:Actinidain
1665:Caspase 14
1660:Caspase 13
1655:Caspase 12
1650:Caspase 10
479:References
158:structures
125:KEGG entry
2241:Proteases
2236:EC 3.4.22
2040:EC number
1887:Cruzipain
1794:Cathepsin
1691:Bromelain
1645:Caspase 9
1640:Caspase 8
1635:Caspase 7
1630:Caspase 6
1625:Caspase 5
1620:Caspase 4
1615:Caspase 3
1610:Caspase 2
1605:Caspase 1
1577:Proteases
959:205499859
908:0006-291X
886:CiteSeerX
805:Chem. Rev
376:substrate
343:(such as
321:β-barrels
232:3.4.22.44
78:Databases
60:3.4.22.44
2064:Kinetics
1988:Cofactor
1951:Activity
1877:Separase
1532:Archived
1508:31822621
1449:29483648
1399:17905838
1350:15477088
1326:in vitro
1307:23395976
1258:11809930
1217:36583382
1209:22270548
1174:23826349
1134:PLOS ONE
1115:23589865
1021:21267463
981:PLOS ONE
951:20148412
916:12074568
840:Virology
825:15755082
770:Virology
696:12377789
586:10873547
548:22086950
496:"P04517"
396:)
353:thrombin
349:elastase
311:)
260:in vitro
213:proteins
201:articles
189:articles
162:RCSB PDB
43:)
2220:Biology
2174:Ligases
1944:Enzymes
1706:Calpain
1597:Caspase
1499:6936558
1476:Bibcode
1440:5840021
1390:2211701
1322:in vivo
1298:4196241
1165:3691164
1142:Bibcode
1106:3645551
1083:Bibcode
1056:8179197
1012:3022733
989:Bibcode
860:2669323
790:2475971
755:3186696
723:Bibcode
648:3285343
616:Bibcode
539:3245014
447:in vivo
418:trypsin
345:trypsin
333:PA clan
266:in vivo
248:PA clan
149:profile
132:MetaCyc
67:CAS no.
2206:Portal
2148:Lyases
1784:CAPNS2
1779:CAPNS1
1774:CAPN14
1769:CAPN13
1764:CAPN12
1759:CAPN11
1754:CAPN10
1686:Ficain
1681:Papain
1588:3.4.22
1506:
1496:
1447:
1437:
1397:
1387:
1348:
1305:
1295:
1256:
1215:
1207:
1172:
1162:
1113:
1103:
1054:
1019:
1009:
957:
949:
914:
906:
888:
858:
823:
788:
753:
746:282299
743:
694:
646:
639:280215
636:
584:
546:
536:
337:MEROPS
277:Origin
196:PubMed
178:Search
168:PDBsum
108:ExPASy
96:BRENDA
84:IntEnz
55:EC no.
2100:Types
1860:Other
1749:CAPN9
1744:CAPN8
1739:CAPN7
1734:CAPN6
1729:CAPN5
1724:CAPN3
1719:CAPN2
1714:CAPN1
1213:S2CID
955:S2CID
360:triad
242:from
144:PRIAM
2192:list
2185:EC7
2179:list
2172:EC6
2166:list
2159:EC5
2153:list
2146:EC4
2140:list
2133:EC3
2127:list
2120:EC2
2114:list
2107:EC1
1504:PMID
1445:PMID
1395:PMID
1346:PMID
1324:and
1303:PMID
1254:PMID
1205:PMID
1170:PMID
1111:PMID
1052:PMID
1017:PMID
947:PMID
912:PMID
904:ISSN
856:PMID
821:PMID
786:PMID
751:PMID
692:PMID
644:PMID
582:PMID
544:PMID
393:1lvb
308:1lvm
281:The
263:and
208:NCBI
165:PDBe
120:KEGG
40:1lvb
1494:PMC
1484:doi
1472:116
1435:PMC
1427:doi
1385:PMC
1377:doi
1338:doi
1328:".
1293:PMC
1285:doi
1281:436
1244:doi
1197:doi
1193:166
1160:PMC
1150:doi
1101:PMC
1091:doi
1079:110
1044:doi
1040:216
1007:PMC
997:doi
939:doi
935:106
896:doi
882:294
848:doi
844:171
813:doi
809:105
778:doi
774:172
741:PMC
731:doi
682:doi
678:277
634:PMC
624:doi
574:doi
534:PMC
526:doi
389:PDB
304:PDB
250:of
184:PMC
156:PDB
36:PDB
2232::
1831:L2
1827:L1
1585:EC
1579::
1502:.
1492:.
1482:.
1470:.
1466:.
1443:.
1433:.
1423:25
1421:.
1417:.
1393:.
1383:.
1373:16
1371:.
1367:.
1344:.
1334:38
1332:.
1301:.
1291:.
1279:.
1275:.
1252:.
1240:14
1238:.
1234:.
1211:.
1203:.
1191:.
1168:.
1158:.
1148:.
1136:.
1132:.
1109:.
1099:.
1089:.
1077:.
1073:.
1050:.
1038:.
1015:.
1005:.
995:.
983:.
979:.
967:^
953:.
945:.
933:.
910:.
902:.
894:.
880:.
868:^
854:.
842:.
819:.
807:.
784:.
772:.
749:.
739:.
729:.
719:85
717:.
713:.
690:.
676:.
672:.
656:^
642:.
632:.
622:.
612:85
610:.
606:.
594:^
580:.
570:19
568:.
556:^
542:.
532:.
522:40
520:.
516:.
504:^
486:^
391::
351:,
347:,
306::
273:.
234:,
229:EC
38::
2208::
2194:)
2190:(
2181:)
2177:(
2168:)
2164:(
2155:)
2151:(
2142:)
2138:(
2129:)
2125:(
2116:)
2112:(
1936:e
1929:t
1922:v
1851:Z
1846:W
1841:S
1836:O
1829:/
1822:K
1817:H
1812:F
1807:C
1802:B
1590:)
1583:(
1569:e
1562:t
1555:v
1510:.
1486::
1478::
1451:.
1429::
1401:.
1379::
1352:.
1340::
1309:.
1287::
1260:.
1246::
1219:.
1199::
1176:.
1152::
1144::
1138:8
1117:.
1093::
1085::
1058:.
1046::
1023:.
999::
991::
985:6
961:.
941::
918:.
898::
862:.
850::
827:.
815::
792:.
780::
757:.
733::
725::
698:.
684::
650:.
626::
618::
588:.
576::
550:.
528::
498:.
227:(
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