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ProteomicsChemical proteomics profiling of N-terminal and lysine acetyltransferases
Acetylation of amino groups is a prevalent protein modification in all kingdoms of life. Acetyl groups are transferred from Coenzyme A (CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA ...
ORGANISM(S): Homo Sapiens (human) 
2021-04-14 | PXD018544 | JPOST Repository
ProteomicsInvestigating peptide-Coenzyme A-conjugates as chemical probes for proteomic profiling of N-terminal and lysine acetyltransferases
Acetyl groups are transferred from Acetyl-Coenzyme A (Ac-CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA conjugates as KAT probes, we have synthesized peptide probes with CoA conjugate...
ORGANISM(S): Homo Sapiens (human) 
2022-05-02 | PXD032957 | JPOST Repository
ProteomicsA continuous assay set to screen and characterize novel protein N-acetyltransferases unveils rice GNAT2 activity
Protein N-acetyltransferases (NATs) belong to the Gcn5-related N-acetyltransferases (GNATs) superfamily. GNATs catalyze the transfer of acetyl from acetyl-CoA to the reactive amine moiety of a wide range of acceptors. NAT sequences are difficult to distinguish from other members of the GNAT superfam...
ORGANISM(S): Escherichia coli Oryza sativa (Rice) 
2022-04-04 | PXD030189 | Pride
Rice Acetylation Yeast Modifications Nata N-acetyltransferase Gnat 
ProteomicsGlobal acetylation profiling for multiple Arabidopsis thaliana plastid N-terminal acetyltransferases
Protein acetylation is a universally conserved modification occurring on N-termini (N-Terminal acetylation, NTA). Although recent reports indicate that NTA occur frequently in plant plastids, little is known about the machinery involved in plastid acetylation and why these modifications are that fre...
ORGANISM(S): Escherichia coli 
2020-07-13 | PXD016205 | Pride
Acetyltransferase N-acetylome N-terminal acetylation Quantitative proteomics Silpronaq Gap test 
UnknownBacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.
Not available
S-EPMC4795176 | biostudies-literature
UnknownCo-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases.
Not available
S-EPMC6962057 | biostudies-literature
UnknownDynamics-function relationship in the catalytic domains of N-terminal acetyltransferases.
Not available
S-EPMC7078549 | biostudies-literature
ProteomicsFast light changes promote distinct responses of plastid protein acetylation marks
Protein acetylation is a key recurring co- and posttranslational modification. How different types of acetylation respond to the same environmental stress is unknown. A member of the newly discovered family of plastid acetyltransferases (GNAT2), which is featuring both lysine- and N-terminal acetyl...
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress) 
2024-08-19 | PXD040517 | JPOST Repository
UnknownInvestigating Peptide-Coenzyme A Conjugates as Chemical Probes for Proteomic Profiling of N-Terminal and Lysine Acetyltransferases.
Not available
S-EPMC9541820 | biostudies-literature
UnknownFluorescence umpolung enables light-up sensing of N-acetyltransferases and nerve agents.
Not available
S-EPMC8222306 | biostudies-literature
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