Počet záznamů: 1
Uncovering Robust Delactoylase and Depyruvoylase Activities of HDAC Isoforms
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SYSNO ASEP 0558797 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Uncovering Robust Delactoylase and Depyruvoylase Activities of HDAC Isoforms Tvůrce(i) Zessin, M. (DE)
Meleshin, M. (DE)
Praetorius, L. (DE)
Sippl, W. (DE)
Bařinka, Cyril (BTO-N) RID, ORCID
Schutkowski, M. (DE)Celkový počet autorů 6 Zdroj.dok. ACS Chemical Biology. - : American Chemical Society - ISSN 1554-8929
Roč. 17, č. 6 (2022), s. 1364-1375Poč.str. 12 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova histone crotonylation ; lysine ; inhibitor ; substrate Vědní obor RIV EB - Genetika a molekulární biologie Obor OECD Biochemistry and molecular biology CEP GA21-31806S GA ČR - Grantová agentura ČR Způsob publikování Omezený přístup Institucionální podpora BTO-N - RVO:86652036 UT WOS 000813511100001 EID SCOPUS 85132223467 DOI 10.1021/acschembio.1c00863 Anotace 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. Pracoviště Biotechnologický ústav Kontakt Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Rok sběru 2023 Elektronická adresa https://pubs.acs.org/doi/10.1021/acschembio.1c00863
Počet záznamů: 1