Substrate Scope for Human Histone Lysine Acetyltransferase KAT8

International Journal of Molecular Sciences

卷:22

Jasmin Mecinović¹  Chiara Punzo¹  Giordano Proietti¹  Yali Wang² 

[1] Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark;

[2] Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands;

关键词: acetylation;    epigenetics;    histone;    lysine;    posttranslational modifications;   

DOI  :  10.3390/ijms22020846

来源: DOAJ

【 摘 要 】

Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16 (H4K16). Our synthetic and enzymatic studies on chemically and structurally diverse lysine mimics demonstrate that KAT8 also has a capacity to acetylate selected lysine analogues that possess subtle changes on the side chain and main chain. Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family.

【 授权许可】

Unknown