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However, it still has many arguments in the innate immune function, especially in model invertebrate animal. The proPO homologous-protein in mammal also does not have any immune activity. Thus, it might be difficult to conclude its function in immunity.
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Sánchez-Aparicio, JosĂ©-Emilio; Tiessler-Sala, Laura; Velasco-Carneros, Lorea; Roldán-MartĂn, Lorena; Sciortino, Giuseppe; MarĂ©chal, Jean-Didier (2021-01-25).
70:(PO). The conversion of prophenoloxidase to the active form of the enzyme can be brought about by minuscule amounts of molecules such as
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Söderhäll, K; Cerenius, L (1998). "Role of the prophenoloxidase-activating system in invertebrate immunity".
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294:"Prophenoloxidase activation is not required for survival to microbial infections in Drosophila"
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Cerenius, L; Söderhäll, K (2004). "The prophenoloxidase-activating system in invertebrates".
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of pathogens and damaged tissues. This important process is controlled by the enzyme
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Prophenoloxidase b hexamer, Marsupenaeus japonicus.
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107:Beck, Gregory; Habicht, Gail S. (November 1996).
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163:Journal of Chemical Information and Modeling
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35:found in some invertebrates, including
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292:Leclerc, V; Reichhart, JM (2006).
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109:"Immunity and the Invertebrates"
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271:10.1016/S0952-7915(98)80026-5
259:Current Opinion in Immunology
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674:. You can help Knowledge by
31:) is a modified form of the
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516:Michaelis–Menten kinetics
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408:Diffusion-limited enzyme
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175:10.1021/acs.jcim.0c00827
62:in invertebrates is the
670:-related article is a
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501:Eadie–Hofstee diagram
434:Allosteric regulation
216:Immunological Reviews
60:innate defense system
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511:Lineweaver–Burk plot
128:1996SciAm.275e..60B
116:Scientific American
33:complement response
470:Enzyme superfamily
403:Enzyme promiscuity
72:lipopolysaccharide
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169:(1): 311–323.
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53:metalloprotein
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78:and beta-1,3-
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76:peptidoglycan
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68:phenoloxidase
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731:Insect stubs
676:expanding it
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612:Translocases
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547:Transferases
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388:Binding site
304:(2): 231–5.
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184:10261/310255
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122:(5): 60–66.
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64:melanization
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51:-containing
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383:Active site
265:(1): 23–8.
715:Categories
586:Isomerases
560:Hydrolases
427:Regulation
222:: 116–26.
94:References
47:. It is a
465:EC number
193:1549-9596
489:Kinetics
413:Cofactor
376:Activity
328:16322759
298:EMBO Rep
244:10614298
236:15199959
201:33337144
58:A major
645:Biology
599:Ligases
369:Enzymes
319:1369246
279:9523106
144:8875808
124:Bibcode
80:glucans
37:insects
668:insect
631:Portal
573:Lyases
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49:copper
666:This
525:Types
240:S2CID
112:(PDF)
82:from
45:worms
41:crabs
29:proPO
672:stub
617:list
610:EC7
604:list
597:EC6
591:list
584:EC5
578:list
571:EC4
565:list
558:EC3
552:list
545:EC2
539:list
532:EC1
324:PMID
275:PMID
232:PMID
197:PMID
189:ISSN
140:PMID
43:and
314:PMC
306:doi
267:doi
224:doi
220:198
179:hdl
171:doi
132:doi
120:275
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27:(
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.