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The enzyme is also known as yeast KEX2 protease, proteinase yscF, prohormone-processing endoprotease, paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, andrenorphin-Gly-generating enzyme, endoproteinase Kex2p, gene KEX2 dibasic proteinase, Kex 2p proteinase, Kex2
264:
endopeptidase, Kex2 endoprotease, Kex2 endoproteinase, Kex2 protease, proteinase Kex2p, Kex2-like precursor protein processing endoprotease, prohormone-processing KEX2 proteinase, prohormone-processing proteinase,
389:
Julius D, Brake A, Blair L, Kunisawa R, Thorner J (July 1984). "Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor".
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243:. It is a family of subtilisin-like peptidases. Even though there are a few prokaryote kexin-like peptidases, all kexins are eukaryotes. The enzyme is encoded by the yeast gene
905:
645:
482:
Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (October 1988). "Yeast KEX2 genes encodes an endopeptidase homologous to subtilisin-like serine proteases".
106:
94:
153:
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Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (February 1989). "Characterization of KEX2-encoded endopeptidase from yeast
Saccharomyces cerevisiae".
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247:, and usually referred to in the scientific community as Kex2p. It shares structural similarities with the bacterial protease
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Rockwell NC, Krysan DJ, Komiyama T, Fuller RS (December 2002). "Precursor processing by kex2/furin proteases".
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255:. In the mammal, kexin-like peptidases function in creating and regulating many differing proproteins.
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519:"Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease"
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Proceedings of the
National Academy of Sciences of the United States of America
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251:. The first mammalian homologue of this protein to be identified was
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317:. Methods in Enzymology. Vol. 244. Elsevier. pp. 175–88.
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268:, protease KEX2, Kex2 proteinase, and Kex2-like endoproteinase.
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213:, specifically a yeast serine peptidase, found in the budding
435:"Hormone processing and membrane-bound proteinases in yeast"
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227:
the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process
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315:Pro-protein convertases of subtilisin/kexin family
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517:Fuller RS, Brake A, Thorner J (March 1989).
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616:at the U.S. National Library of Medicine
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659:serine proteases/serine endopeptidases
433:Achstetter T, Wolf DH (January 1985).
36:
7:
1404:
1402:
451:10.1002/j.1460-2075.1985.tb02333.x
25:
239:precursors. The human homolog is
1406:
1389:
313:Seidah NG, Chrétien M (1994).
27:Prohormone-processing protease
1:
871:Urinary plasminogen activator
496:10.1016/s0006-291x(88)80832-5
30:For the Chinese gymnast, see
1422:. You can help Knowledge by
866:Tissue plasminogen activator
590:10.1016/0006-291x(89)92438-8
404:10.1016/0092-8674(84)90442-2
323:10.1016/0076-6879(94)44015-8
1490:
1401:
29:
1267:Michaelis–Menten kinetics
957:Proteinase 3/Myeloblastin
160:
1159:Diffusion-limited enzyme
618:Medical Subject Headings
55:Saccharomyces cerevisiae
1418:-related article is a
1011:Proprotein convertases
544:10.1073/pnas.86.5.1434
1252:Eadie–Hofstee diagram
1185:Allosteric regulation
861:Plasminogen activator
266:proprotein convertase
1262:Lineweaver–Burk plot
1001:Prolyl endopeptidase
535:1989PNAS...86.1434F
1221:Enzyme superfamily
1154:Enzyme promiscuity
154:XIV: 0.2 - 0.21 Mb
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1430:
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883:Complement system
675:Digestive enzymes
368:10.1021/cr010168i
332:978-0-12-182145-6
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16:(Redirected from
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1257:Hanes–Woolf plot
1200:Enzyme activator
1195:Enzyme inhibitor
1169:Enzyme catalysis
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1285:Oxidoreductases
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1247:Enzyme kinetics
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1231:List of enzymes
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1144:Catalytic triad
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1209:Classification
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608:External links
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1190:Cooperativity
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1149:Oxyanion hole
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1061:Streptokinase
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934:immune system
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923:C3-convertase
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231:alpha-factor
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220:S. cerevisiae
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107:RefSeq (Prot)
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95:RefSeq (mRNA)
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38:
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19:
1474:Enzyme stubs
1424:expanding it
1413:
1363:Translocases
1360:
1347:
1334:
1321:
1308:
1298:Transferases
1295:
1282:
1139:Binding site
851:fibrinolysis
849:
727:
693:Chymotrypsin
581:
577:
571:
526:
522:
512:
487:
483:
477:
445:(1): 173–7.
442:
438:
428:
395:
391:
384:
359:
355:
349:
314:
308:
297:. Retrieved
293:
262:
259:Nomenclature
244:
237:killer toxin
218:
209:-processing
195:
194:
152:
1134:Active site
756:Factor XIIa
736:Factor VIIa
720:Coagulation
174:Swiss-model
112:NP_014161.1
45:Identifiers
1463:Categories
1337:Isomerases
1311:Hydrolases
1178:Regulation
1038:Subtilisin
980:Batroxobin
761:Kallikrein
751:Factor XIa
741:Factor IXa
708:Pancreatic
703:Neutrophil
299:2020-03-24
272:References
249:subtilisin
207:prohormone
170:Structures
165:Search for
148:Chromosome
130:Other data
83:HomoloGene
1469:EC 3.4.21
1216:EC number
1066:Cathepsin
1052:Sedolisin
1028:Prostasin
746:Factor Xa
233:pheromone
225:catalyzes
203:3.4.21.61
141:3.4.21.61
136:EC number
1240:Kinetics
1164:Cofactor
1127:Activity
967:Venombin
952:Tryptase
947:Granzyme
901:Factor I
896:Factor D
891:Factor B
731:Thrombin
728:factors:
698:Elastase
420:37772545
376:12475200
211:protease
184:InterPro
50:Organism
32:He Kexin
1396:Biology
1350:Ligases
1120:Enzymes
1006:Pronase
996:Acrosin
942:Chymase
856:Plasmin
688:Trypsin
598:2647083
563:2646633
531:Bibcode
504:2845974
469:3894003
412:6430565
341:7845206
290:"Kexin"
205:) is a
180:Domains
119:UniProt
1416:enzyme
1382:Portal
1324:Lyases
1033:Reelin
975:Ancrod
932:Other
666:3.4.21
620:(MeSH)
596:
561:
554:286710
551:
502:
467:
460:554167
457:
418:
410:
374:
339:
329:
223:). It
124:D6W0V5
76:855483
71:Entrez
62:Symbol
1414:This
1276:Types
1042:Furin
989:Other
916:MASP2
911:MASP1
841:KLK15
836:KLK14
831:KLK13
826:KLK12
821:KLK11
816:KLK10
614:Kexin
416:S2CID
253:furin
241:PCSK4
229:yeast
215:yeast
196:Kexin
88:22495
40:Kexin
1420:stub
1368:list
1361:EC7
1355:list
1348:EC6
1342:list
1335:EC5
1329:list
1322:EC4
1316:list
1309:EC3
1303:list
1296:EC2
1290:list
1283:EC1
1056:TPP1
906:MASP
811:KLK9
806:KLK8
801:KLK7
796:KLK6
791:KLK5
786:KLK4
781:KLK3
776:KLK2
771:KLK1
594:PMID
559:PMID
500:PMID
465:PMID
408:PMID
392:Cell
372:PMID
337:PMID
327:ISBN
245:KEX2
235:and
65:KEX2
18:Kex2
1046:S1P
766:PSA
586:doi
582:159
549:PMC
539:doi
492:doi
488:156
455:PMC
447:doi
400:doi
364:doi
360:102
319:doi
1465::
663:EC
657::
592:.
580:.
557:.
547:.
537:.
527:86
525:.
521:.
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406:.
396:37
394:.
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335:.
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279:^
200:EC
1451:e
1444:t
1437:v
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1301:(
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1288:(
1112:e
1105:t
1098:v
1076:G
1071:A
1054:/
1048:4
1044:/
1040:/
1021:2
1016:1
853::
668:)
661:(
647:e
640:t
633:v
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494::
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449::
443:4
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217:(
198:(
34:.
20:)
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