Uncovering Robust Delactoylase and Depyruvoylase Activities of HDAC Isoforms
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F22%3A00558797" target="_blank" >RIV/86652036:_____/22:00558797 - isvavai.cz</a>
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acschembio.1c00863" target="_blank" >https://pubs.acs.org/doi/10.1021/acschembio.1c00863</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acschembio.1c00863" target="_blank" >10.1021/acschembio.1c00863</a>
Alternative languages
Result language
angličtina
Original language name
Uncovering Robust Delactoylase and Depyruvoylase Activities of HDAC Isoforms
Original language description
Zinc-dependent histone deacetylases (HDACs) and sirtuins (SIRT) represent two different classes of enzymes which are responsible for deacylation of modified lysine side chains. The repertoire of acyl residues on lysine side chains identified in vivo is rapidly growing, and very recently lysine lactoylation was described to be involved in metabolic reprogramming. Additionally, lysine pyruvoylation represents a marker for aging and liver cirrhosis. Here, we report a systematic analysis of acyl-specificity of human zinc-dependent HDAC and sirtuin isoforms. We identified HDAC3 as a robust delactoylase with several-thousand-fold higher activity as compared to SIRT2, which was claimed to be the major in vivo delactoylase. Additionally, we systematically searched for enzymes, capable of removing pyruvoyl residues from lysine side chains. Using model peptides, we uncovered high depyruvoylase activity for HDAC6 and HDAC8. Interestingly, such substrates have extremely low K-M values for both HDAC isoforms, pointing to possible in vivo functions.
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
<a href="/en/project/GA21-31806S" target="_blank" >GA21-31806S: Modulation of structural and functional properties of the HSP90 chaperone machinery by reversible acetylation</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ACS Chemical Biology
ISSN
1554-8929
e-ISSN
1554-8937
Volume of the periodical
17
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
1364-1375
UT code for WoS article
000813511100001
EID of the result in the Scopus database
2-s2.0-85132223467