Difference between revisions of "Part:BBa K3895003"

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|[[File:T--SZ SHD--Z50.1.gif|200px|thumb|center|'''Figure 1.''' Swiss Model showing serine residues of KerAVDZ50.]]
 
|[[File:T--SZ SHD--Z50.1.gif|200px|thumb|center|'''Figure 1.''' Swiss Model showing serine residues of KerAVDZ50.]]
 
|[[File:T--SZ SHD--Z50.2.png|200px|thumb|center|''' Figure 2.''' Swiss Model showing hydrophobisity of KerAVDZ50.]]
 
|[[File:T--SZ SHD--Z50.2.png|200px|thumb|center|''' Figure 2.''' Swiss Model showing hydrophobisity of KerAVDZ50.]]
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|[[File:T--SZ SHD--Z50R.jpg|200px|thumb|center|''' Figure 3.''' Ramachandran Plot of KerAVDZ50.Z50 Ramachandran Favoured is 95.14%]]
 
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Revision as of 15:14, 10 October 2021


Keratinase kerAvDZ50

KerAVDZ50 is an extracellular serine thiol alkaline protease from Actinomadura viridilutea strain, which can be isolated from Algerian fishing port [1]. As a thermo-alkaline keratinases, it can function at a pH range of 7–12 and a temperature range of 35–80 °C.

Modeling

Figure 1. Swiss Model showing serine residues of KerAVDZ50.
Figure 2. Swiss Model showing hydrophobisity of KerAVDZ50.
Figure 3. Ramachandran Plot of KerAVDZ50.Z50 Ramachandran Favoured is 95.14%


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 577
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 382
    Illegal AgeI site found at 1120
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 322


Reference

Biochemical and molecular characterization of new keratinoytic protease from Actinomadura viridilutea DZ50. (n.d.). International Journal of Biological Macromolecules, 92, 299–315. https://doi.org/10.1016/j.ijbiomac.2016.07.009