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Evolutionary analysis of dipeptidyl peptidase I
ID Varda, Nina (Avtor), ID Novinec, Marko (Avtor)

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Izvleček
Human dipeptidyl peptidase I (DPPI) belongs to the family of papain-like cysteine peptidases. Its distinctive features are the unique exclusion domain which enables the eponymous activity and homotetramerization of DPPI, and its dependence on chloride ions for enzymatic activity. The oligomeric state of DPPI is unique in this family of predominantly monomeric peptidases. However, a distant DPPI ortholog from Plasmodium falciparum has been shown to be monomeric, indicating that the oligomeric state of DPPI varies between lineages. The aim of this work was to study the evolution of DPPI, with particular attention to the structural features that determine its characteristic enzymatic activity and preferences, and to reconstruct the evolution of its oligomerization. We analyzed fifty-seven selected sequences of DPPI and confirmed its presence in three lineages, namely, Amorphea (including animals and Amoebozoa), Alveolates and the metamonad Giardia. The amino acid residues that bind the chloride ion are highly conserved in all species, indicating that the dependence on chloride ions for activity is an evolutionarily conserved feature of DPPI. The number of N-glycosylation sites is significantly increased in animals, particularly vertebrates. Analysis of homology models and subunit contacts suggests that oligomerization is likely restricted to DPPIs in the Amorphea group.

Jezik:Angleški jezik
Ključne besede:oligomerization, molecular evolution, cathepsin C
Vrsta gradiva:Članek v reviji
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:FKKT - Fakulteta za kemijo in kemijsko tehnologijo
Status publikacije:Objavljeno
Različica publikacije:Objavljena publikacija
Leto izida:2022
Št. strani:12 str.
Številčenje:Vol. 23, iss. 3, art. 1852
PID:20.500.12556/RUL-137349 Povezava se odpre v novem oknu
UDK:577.15
ISSN pri članku:1661-6596
DOI:10.3390/ijms23031852 Povezava se odpre v novem oknu
COBISS.SI-ID:96531459 Povezava se odpre v novem oknu
Datum objave v RUL:13.06.2022
Število ogledov:808
Število prenosov:101
Metapodatki:XML DC-XML DC-RDF
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Gradivo je del revije

Naslov:International journal of molecular sciences
Skrajšan naslov:Int. j. mol. sci.
Založnik:MDPI
ISSN:1661-6596
COBISS.SI-ID:36217605 Povezava se odpre v novem oknu

Licence

Licenca:CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
Povezava:http://creativecommons.org/licenses/by/4.0/deed.sl
Opis:To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.
Začetek licenciranja:06.02.2022

Sekundarni jezik

Jezik:Slovenski jezik
Ključne besede:oligomerizacija, molekularna evolucija, katepsin C

Projekti

Financer:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:N1-0211
Naslov:Uvedba kooperativnosti v peptidaze za izboljšanje njihove aktivnosti in uravnavanja

Financer:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:P1-0140
Naslov:Proteoliza in njena regulacija

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