Substrate Scope for Human Histone Lysine Acetyltransferase KAT8.
Acetylation
Amino Acids
/ chemistry
Catalysis
Cell Nucleus
/ metabolism
Epigenesis, Genetic
Histone Acetyltransferases
/ genetics
Histones
/ chemistry
Humans
Kinetics
Lysine
/ chemistry
Lysine Acetyltransferases
/ metabolism
Peptides
/ chemistry
Protein Conformation
Protein Processing, Post-Translational
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substrate Specificity
acetylation
epigenetics
histone
lysine
posttranslational modifications
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
15 Jan 2021
15 Jan 2021
Historique:
received:
28
12
2020
revised:
12
01
2021
accepted:
13
01
2021
entrez:
20
1
2021
pubmed:
21
1
2021
medline:
24
4
2021
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 33467728
pii: ijms22020846
doi: 10.3390/ijms22020846
pmc: PMC7830570
pii:
doi:
Substances chimiques
Amino Acids
0
Histones
0
Peptides
0
Lysine Acetyltransferases
EC 2.3.1.32
Histone Acetyltransferases
EC 2.3.1.48
KAT8 protein, human
EC 2.3.1.48
Lysine
K3Z4F929H6
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : European Research Council
ID : 715691
Pays : International
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