524:
38:
1949:
753:
to make them produce chymosin during fermentation. The genetically modified microorganism is killed after fermentation and chymosin is isolated from the fermentation broth, so that the fermentation-produced chymosin (FPC) used by cheese producers does not contain any GM component or ingredient. FPC
783:
FPC contains only chymosin B, achieving a higher degree of purity compared with animal rennet. FPC can deliver several benefits to the cheese producer compared with animal or microbial rennet, such as higher production yield, better curd texture and reduced bitterness.
494:
of chymosin initiate enzyme binding to the substrate. When chymosin is not binding substrate, a beta-hairpin, sometimes referred to as "the flap," can hydrogen bond with the active site, therefore covering it and not allowing further binding of substrate.
740:
Because of the imperfections and scarcity of microbial and animal rennets, producers sought replacements. With the development of genetic engineering, it became possible to extract rennet-producing genes from animal stomach and insert them into certain
1389:
Bovine chymosins A and B differ by one amino acid residue. This is probably an alleic variant, according to
Uniprot:P00794. The two isoforms have identical catalytic activity, so any improvement in the product is due to the elimination of other
898:
Kitamura N, Tanimoto A, Hondo E, Andrén A, Cottrell DF, Sasaki M, Yamada J (August 2001). "Immunohistochemical study of the ontogeny of prochymosin--and pepsinogen-producing cells in the abomasum of sheep".
1127:
Newman M, Safro M, Frazao C, Khan G, Zdanov A, Tickle IJ, et al. (October 1991). "X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin".
768:
By 2008, approximately 80% to 90% of commercially made cheeses in the US and
Britain were made using FPC. The most widely used fermentation-produced chymosin is produced either using the fungus
754:
contains the identical chymosin as the animal source, but produced in a more efficient way. FPC products have been on the market since 1990 and are considered the ideal milk-clotting enzyme.
1428:"Peptide substrates for chymosin (rennin). Interaction sites in kappa-casein-related sequences located outside the (103-108)-hexapeptide region that fits into the enzyme's active-site cleft"
389:
in newborn mammals to curdle the milk they ingest, allowing a longer residence in the bowels and better absorption. Non-ruminant species that produce chymosin include pigs, cats, seals, and
816:"A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure"
863:
Lopes-Marques M, Ruivo R, Fonseca E, Teixeira A, Castro LF (November 2017). "Unusual loss of chymosin in mammalian lineages parallels neo-natal immune transfer strategies".
456:
203:
523:
335:
Historically, chymosin was obtained by extracting it from the stomachs of slaughtered calves. Today, most commercial chymosin used in cheese production is produced
1508:
660:
1273:
222:
396:
One study reported finding a chymosin-like enzyme in some human infants, but others have failed to replicate this finding. Humans have a
328:
to curdle the milk they ingest, allowing a longer residence in the bowels and better absorption. It is widely used in the production of
1528:
215:
665:
572:
1501:
1312:
1093:
1057:
166:
1969:
684:
1076:
Gilliland GL, Oliva MT, Dill J (1991). "Functional
Implications of the Three-Dimensional Structure of Bovine Chymosin".
1020:
1668:
1030:
543:
1494:
672:
758:
160:
142:
415:
In addition to the primate lineage leading up to humans, some other mammals have also lost the chymosin gene.
1824:
147:
815:
677:
227:
135:
1939:
1925:
1912:
1899:
1886:
1873:
1860:
1847:
1809:
424:
70:
1302:
1819:
1773:
1716:
1558:
1525:
1277:
163:
53:
87:
1721:
476:
37:
1742:
1661:
1486:
944:
Staff, Online
Mendelian Inheritance in Man (OMIM) Database. Last updated February 21, 1997
814:
Groves MR, Dhanaraj V, Badasso M, Nugent P, Pitts JE, Hoover DJ, Blundell TL (October 1998).
1814:
1175:
776:
722:
718:
401:
360:
123:
1367:
1350:
615:
8:
1778:
1481:
1221:
Harris TJ, Lowe PA, Lyons A, Thomas PG, Eaton MA, Millican TA, et al. (April 1982).
348:
99:
65:
1179:
58:
1974:
1711:
1521:
1452:
1427:
1005:
924:
386:
1247:
1222:
1198:
1163:
178:
1457:
1414:
1372:
1308:
1252:
1203:
1144:
1140:
1117:
1099:
1089:
1053:
1026:
993:
974:
916:
912:
880:
840:
804:
770:
579:
317:
154:
1757:
1752:
1726:
1654:
1573:
1568:
1447:
1439:
1362:
1242:
1234:
1193:
1183:
1136:
1081:
1001:
966:
957:
Henschel MJ, Newport MJ, Parmar V (1987). "Gastric proteases in the human infant".
928:
908:
872:
830:
757:
FPC was the first artificially produced enzyme to be registered and allowed by the
713:
342:
282:
244:
1223:"Molecular cloning and nucleotide sequence of cDNA coding for calf preprochymosin"
1162:
Emtage JS, Angal S, Doel MT, Harris TJ, Jenkins B, Lilley G, Lowe PA (June 1983).
1804:
1788:
1701:
1047:
701:
336:
1085:
1080:. Advances in Experimental Medicine and Biology. Vol. 306. pp. 23–37.
876:
835:
625:
182:
1953:
1842:
1783:
1596:
1168:
Proceedings of the
National Academy of Sciences of the United States of America
198:
765:
was made with FPC and it has up to 80% of the global market share for rennet.
1963:
1747:
1706:
448:
440:
173:
1238:
1188:
1696:
1376:
920:
884:
468:
444:
1461:
1418:
1329:"Food Biotechnology in the United States: Science, Regulation, and Issues"
1256:
1207:
1148:
1103:
978:
844:
42:
Crystal structure of bovine chymosin complex with the inhibitor CP-113972.
1920:
1855:
1691:
1635:
1630:
1612:
762:
596:
464:
460:
111:
1591:
591:
452:
397:
1443:
1121:
970:
808:
584:
25:, an enzyme which takes part in regulation of arterial blood pressure.
1894:
1868:
1622:
491:
487:
483:
374:
1948:
1517:
945:
742:
436:
382:
378:
325:
321:
309:
1328:
862:
390:
130:
689:
1907:
1677:
1543:
1477:
1164:"Synthesis of calf prochymosin (prorennin) in Escherichia coli"
750:
696:
567:
472:
432:
409:
405:
329:
313:
210:
106:
94:
82:
1516:
1881:
1553:
746:
22:
946:
Chymosin pseudogene; CYMP prochymosin, included, in the OMIM
897:
813:
428:
291:
259:
253:
118:
1646:
320:
belonging to MEROPS A1 family. It is produced by newborn
297:
265:
1425:
400:
for chymosin that does not generate a protein, found on
1405:
Foltmann B (1966). "A review on prorennin and rennin".
404:. Humans have other proteins to digest milk, such as
1937:
1480:
online database for peptidases and their inhibitors:
1220:
1161:
1126:
956:
300:
294:
268:
262:
250:
288:
1407:
Comptes-Rendus des
Travaux du Laboratoire Carlsberg
1351:"Major technological advances and trends in cheese"
1296:
1294:
475:is broken, the hydrophobic groups unite and form a
285:
256:
247:
1426:Visser S, Slangen CJ, van Rooijen PJ (June 1987).
1078:Structure and Function of the Aspartic Proteinases
1075:
479:network that traps the aqueous phase of the milk.
1961:
1291:
1268:
1266:
1045:
423:Chymosin is used to bring about the extensive
377:, although it is best known to be produced by
1662:
1502:
799:
797:
435:-making. The native substrate of chymosin is
1348:
1342:
1263:
991:
1214:
1155:
1071:
1069:
1022:Cheese: Chemistry, Physics and Microbiology
891:
1669:
1655:
1509:
1495:
794:
522:
36:
1451:
1366:
1307:. UK: Wiley-Blackwell. pp. 100–101.
1246:
1197:
1187:
1049:Development of the gastrointestinal tract
858:
856:
854:
834:
507:gene and corresponding human pseudogene:
447:between amino acid residues 105 and 106,
1404:
1066:
459:. When the specific linkage between the
735:
1962:
1300:
1110:
940:
938:
851:
1650:
1490:
996:. In Rawlings ND, Salvesen G (eds.).
865:Molecular Phylogenetics and Evolution
418:
373:Chymosin is found in a wide range of
1321:
1349:Johnson ME, Lucey JA (April 2006).
1018:
935:
13:
1397:
1052:. Hamilton, Ontario: B.C. Decker.
1006:10.1016/B978-0-12-382219-2.00005-3
14:
1986:
1470:
1368:10.3168/jds.S0022-0302(06)72186-5
901:Anatomia, Histologia, Embryologia
1947:
1046:Sanderson IR, Walker WA (1999).
913:10.1046/j.1439-0264.2001.00326.x
528:X-ray analysis of calf chymosin
281:
243:
1383:
1000:. Vol. 1. pp. 37–42.
998:Handbook of Proteolytic Enzymes
759:US Food and Drug Administration
1039:
1012:
985:
950:
503:Listed below are the ruminant
1:
1276:. GMO Compass. Archived from
787:
381:animals in the lining of the
368:
324:animals in the lining of the
1141:10.1016/0022-2836(91)90934-X
1129:Journal of Molecular Biology
992:Szecsi PB, Harboe M (2013).
482:Charge interactions between
7:
1970:Genes on human chromosome 1
1676:
1086:10.1007/978-1-4684-6012-4_3
1019:Fox PF (28 February 1999).
877:10.1016/j.ympev.2017.08.014
761:. In 1999, about 60% of US
642:chymosin pseudogene (human)
498:
455:. The resultant product is
10:
1991:
1331:. U.S. Department of State
1304:Technology of Cheesemaking
385:. Chymosin is produced by
20:
1833:
1825:Michaelis–Menten kinetics
1797:
1766:
1735:
1684:
1621:
1605:
1584:
1536:
836:10.1093/protein/11.10.833
712:
707:
695:
683:
671:
659:
651:
646:
641:
621:
611:
606:
602:
590:
578:
566:
558:
550:
538:
533:
521:
516:
221:
209:
197:
192:
188:
172:
153:
141:
129:
117:
105:
93:
81:
76:
64:
52:
47:
35:
30:
1717:Diffusion-limited enzyme
1559:Signal peptide peptidase
1355:Journal of Dairy Science
486:on the kappa-casein and
457:calcium phosphocaseinate
21:Not to be confused with
1432:The Biochemical Journal
1189:10.1073/pnas.80.12.3671
1227:Nucleic Acids Research
959:Biology of the Neonate
439:which is specifically
318:aspartic endopeptidase
1810:Eadie–Hofstee diagram
1743:Allosteric regulation
1239:10.1093/nar/10.7.2177
994:"Chapter 5: Chymosin"
1820:Lineweaver–Burk plot
777:Kluyveromyces lactis
736:Recombinant chymosin
361:Kluyveromyces lactis
1522:aspartate proteases
1180:1983PNAS...80.3671E
823:Protein Engineering
387:gastric chief cells
1779:Enzyme superfamily
1712:Enzyme promiscuity
463:(para-casein) and
419:Enzymatic reaction
1935:
1934:
1644:
1643:
1444:10.1042/bj2440553
1314:978-1-4051-8298-0
1095:978-1-4684-6014-8
1059:978-1-55009-081-9
971:10.1159/000242719
771:Aspergillus niger
733:
732:
729:
728:
635:
634:
631:
630:
350:Aspergillus niger
237:
236:
233:
232:
136:metabolic pathway
1982:
1952:
1951:
1943:
1815:Hanes–Woolf plot
1758:Enzyme activator
1753:Enzyme inhibitor
1727:Enzyme catalysis
1671:
1664:
1657:
1648:
1647:
1511:
1504:
1497:
1488:
1487:
1465:
1455:
1422:
1391:
1387:
1381:
1380:
1370:
1346:
1340:
1339:
1337:
1336:
1325:
1319:
1318:
1298:
1289:
1288:
1286:
1285:
1270:
1261:
1260:
1250:
1218:
1212:
1211:
1201:
1191:
1159:
1153:
1152:
1124:
1114:
1108:
1107:
1073:
1064:
1063:
1043:
1037:
1036:
1016:
1010:
1009:
989:
983:
982:
954:
948:
942:
933:
932:
895:
889:
888:
860:
849:
848:
838:
820:
811:
801:
639:
638:
604:
603:
546:
526:
514:
513:
510:
509:
364:
346:
343:Escherichia coli
307:
306:
303:
302:
299:
296:
293:
290:
287:
275:
274:
271:
270:
267:
264:
261:
258:
255:
252:
249:
190:
189:
40:
28:
27:
18:Class of enzymes
1990:
1989:
1985:
1984:
1983:
1981:
1980:
1979:
1960:
1959:
1958:
1946:
1938:
1936:
1931:
1843:Oxidoreductases
1829:
1805:Enzyme kinetics
1793:
1789:List of enzymes
1762:
1731:
1702:Catalytic triad
1680:
1675:
1645:
1640:
1617:
1601:
1580:
1532:
1515:
1473:
1468:
1400:
1398:Further reading
1395:
1394:
1388:
1384:
1347:
1343:
1334:
1332:
1327:
1326:
1322:
1315:
1301:Law BA (2010).
1299:
1292:
1283:
1281:
1272:
1271:
1264:
1219:
1215:
1160:
1156:
1135:(4): 1295–309.
1116:
1115:
1111:
1096:
1074:
1067:
1060:
1044:
1040:
1033:
1017:
1013:
990:
986:
955:
951:
943:
936:
896:
892:
861:
852:
818:
803:
802:
795:
790:
738:
542:
529:
501:
421:
371:
358:
340:
284:
280:
246:
242:
43:
26:
19:
12:
11:
5:
1988:
1978:
1977:
1972:
1957:
1956:
1933:
1932:
1930:
1929:
1916:
1903:
1890:
1877:
1864:
1851:
1837:
1835:
1831:
1830:
1828:
1827:
1822:
1817:
1812:
1807:
1801:
1799:
1795:
1794:
1792:
1791:
1786:
1781:
1776:
1770:
1768:
1767:Classification
1764:
1763:
1761:
1760:
1755:
1750:
1745:
1739:
1737:
1733:
1732:
1730:
1729:
1724:
1719:
1714:
1709:
1704:
1699:
1694:
1688:
1686:
1682:
1681:
1674:
1673:
1666:
1659:
1651:
1642:
1641:
1639:
1638:
1633:
1627:
1625:
1619:
1618:
1616:
1615:
1609:
1607:
1603:
1602:
1600:
1599:
1597:HIV-1 protease
1594:
1588:
1586:
1582:
1581:
1579:
1578:
1577:
1576:
1571:
1564:Beta secretase
1561:
1556:
1551:
1546:
1540:
1538:
1534:
1533:
1514:
1513:
1506:
1499:
1491:
1485:
1484:
1472:
1471:External links
1469:
1467:
1466:
1423:
1413:(8): 143–231.
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1382:
1341:
1320:
1313:
1290:
1262:
1233:(7): 2177–87.
1213:
1174:(12): 3671–5.
1154:
1109:
1094:
1065:
1058:
1038:
1031:
1011:
984:
949:
934:
890:
850:
829:(10): 833–40.
792:
791:
789:
786:
737:
734:
731:
730:
727:
726:
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710:
709:
705:
704:
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1968:
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1811:
1808:
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1800:
1796:
1790:
1787:
1785:
1784:Enzyme family
1782:
1780:
1777:
1775:
1772:
1771:
1769:
1765:
1759:
1756:
1754:
1751:
1749:
1748:Cooperativity
1746:
1744:
1741:
1740:
1738:
1734:
1728:
1725:
1723:
1720:
1718:
1715:
1713:
1710:
1708:
1707:Oxyanion hole
1705:
1703:
1700:
1698:
1695:
1693:
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1689:
1687:
1683:
1679:
1672:
1667:
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1634:
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1567:
1566:
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1547:
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1541:
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1530:
1527:
1523:
1519:
1512:
1507:
1505:
1500:
1498:
1493:
1492:
1489:
1483:
1479:
1475:
1474:
1463:
1459:
1454:
1449:
1445:
1441:
1437:
1433:
1429:
1424:
1420:
1416:
1412:
1408:
1403:
1402:
1386:
1378:
1374:
1369:
1364:
1361:(4): 1174–8.
1360:
1356:
1352:
1345:
1330:
1324:
1316:
1310:
1306:
1305:
1297:
1295:
1280:on 2015-03-26
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1055:
1051:
1050:
1042:
1034:
1032:9780834213388
1028:
1024:
1023:
1015:
1007:
1003:
999:
995:
988:
980:
976:
972:
968:
965:(5): 268–72.
964:
960:
953:
947:
941:
939:
930:
926:
922:
918:
914:
910:
906:
902:
894:
886:
882:
878:
874:
870:
866:
859:
857:
855:
846:
842:
837:
832:
828:
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559:Alt. symbols
504:
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471:) groups of
469:glycopeptide
445:peptide bond
422:
414:
402:chromosome 1
395:
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359:
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341:
334:
277:
239:
238:
100:BRENDA entry
15:
1692:Active site
1613:Nepenthesin
1390:impurities.
763:hard cheese
647:Identifiers
616:Swiss-model
534:Identifiers
465:hydrophilic
461:hydrophobic
316:. It is an
88:IntEnz view
48:Identifiers
1964:Categories
1895:Isomerases
1869:Hydrolases
1736:Regulation
1592:Plasmepsin
1585:Pathogenic
1537:Vertebrate
1335:2006-08-14
1284:2011-03-03
1274:"Chymosin"
788:References
708:Other data
612:Structures
607:Search for
544:Bos taurus
492:aspartates
488:glutamates
484:histidines
453:methionine
398:pseudogene
369:Occurrence
157:structures
124:KEGG entry
71:9001-98-3
1975:EC 3.4.23
1774:EC number
1623:Cathepsin
1518:Proteases
1125:;
871:: 78–86.
812:;
774:or using
702:NR_003599
661:NCBI gene
517:Chymosin
375:tetrapods
312:found in
77:Databases
1798:Kinetics
1722:Cofactor
1685:Activity
1549:Chymosin
1377:16537950
921:11534329
885:28851538
743:bacteria
626:InterPro
539:Organism
499:Examples
467:(acidic
437:K-casein
383:abomasum
379:ruminant
326:abomasum
322:ruminant
310:protease
240:Chymosin
228:proteins
216:articles
204:articles
161:RCSB PDB
59:3.4.23.4
31:Chymosin
1954:Biology
1908:Ligases
1678:Enzymes
1482:A01.006
1462:3128264
1453:1148031
1419:5330666
1257:6283469
1208:6304731
1176:Bibcode
1149:1942052
1104:1812710
979:3118972
929:7552821
845:9862200
622:Domains
592:UniProt
443:at the
441:cleaved
354:awamori
183:QuickGO
148:profile
131:MetaCyc
66:CAS no.
1940:Portal
1882:Lyases
1544:Pepsin
1529:3.4.23
1478:MEROPS
1460:
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1248:320601
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1206:
1199:394112
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1029:
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843:
751:yeasts
719:Chr. 1
697:RefSeq
690:118943
666:643160
652:Symbol
597:P00794
573:529879
568:Entrez
551:Symbol
473:casein
433:cheese
410:lipase
406:pepsin
391:chicks
357:, and
330:cheese
314:rennet
278:rennin
211:PubMed
193:Search
179:AmiGO
167:PDBsum
107:ExPASy
95:BRENDA
83:IntEnz
54:EC no.
1834:Types
1606:Plant
1554:Renin
925:S2CID
819:(PDF)
747:fungi
723:p13.3
714:Locus
352:var.
308:is a
143:PRIAM
23:renin
1926:list
1919:EC7
1913:list
1906:EC6
1900:list
1893:EC5
1887:list
1880:EC4
1874:list
1867:EC3
1861:list
1854:EC2
1848:list
1841:EC1
1476:The
1458:PMID
1415:PMID
1373:PMID
1309:ISBN
1253:PMID
1204:PMID
1145:PMID
1122:4CMS
1100:PMID
1090:ISBN
1054:ISBN
1027:ISBN
975:PMID
917:PMID
881:PMID
841:PMID
809:1CZI
685:OMIM
678:2588
673:HGNC
655:CYMP
585:4CMS
490:and
451:and
429:curd
427:and
408:and
223:NCBI
164:PDBe
119:KEGG
1448:PMC
1440:doi
1436:244
1363:doi
1243:PMC
1235:doi
1194:PMC
1184:doi
1137:doi
1133:221
1118:PDB
1082:doi
1002:doi
967:doi
909:doi
873:doi
869:116
831:doi
805:PDB
749:or
580:PDB
562:CPC
554:Cym
505:Cym
339:in
276:or
199:PMC
155:PDB
1966::
1526:EC
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269:n
266:ɪ
263:s
260:ə
257:m
251:k
248:ˈ
245:/
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