Postproline Cleaving Enzymes also Show Specificity to Reduced Cysteine
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F24%3A00602578" target="_blank" >RIV/61388971:_____/24:00602578 - isvavai.cz</a>
Alternative codes found
RIV/00216224:90242/24:00139174 RIV/00216208:11310/24:10489597
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acs.analchem.4c04277" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.analchem.4c04277</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.analchem.4c04277" target="_blank" >10.1021/acs.analchem.4c04277</a>
Alternative languages
Result language
angličtina
Original language name
Postproline Cleaving Enzymes also Show Specificity to Reduced Cysteine
Original language description
In proteomics, postproline cleaving enzymes (PPCEs), such as Aspergillus niger prolyl endopeptidase (AnPEP) and neprosin, complement proteolytic tools because proline is a stop site for many proteases. But while aiming at using AnPEP in online proteolysis, we found that this enzyme also displayed specificity to reduced cysteine. By LC-MS/MS, we systematically analyzed AnPEP sources and conditions that could affect this cleavage preference. Postcysteine cleavage was blocked by cysteine modifications, including disulfide bond formation, oxidation, and alkylation. The last modification explains why this activity has remained undetected so far. In the same experimental paradigm, neprosin mimicked this cleavage specificity. Based on these findings, PPCEs cleavage preferences should be redefined from post-Pro/Ala to post-Pro/Ala/Cys. Moreover, this evidence demands reconsidering PPCEs applications, whether cleaving Cys-rich proteins or assessing Cys status in proteins, and calls for revisiting the proposed enzymatic mechanism of these proteases.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Analytical Chemistry
ISSN
0003-2700
e-ISSN
1520-6882
Volume of the periodical
96
Issue of the periodical within the volume
48
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
19084-19092
UT code for WoS article
001358996800001
EID of the result in the Scopus database
2-s2.0-85209652247