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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
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
ProteomicsThe state transition acetyltransferase GNAT2 interacts with GNAT1 and GNAT3 in independent complexes
The acetylation of amino groups within proteins is one of the major posttranslational modifications (PTMs) in all organisms. N-terminal acetyltransferases (NATs) or lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from the donor substrate acetyl coenzyme A (Ac-CoA) to the t...
ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress) 
2024-08-19 | PXD044167 | JPOST Repository
ProteomicsGlobal profiling of acetylation reveals a new family with dual-specific lysine and N-terminal acetyltransferase activity in the plastids of Arabidopsis
Protein acetylation is a universally conserved modification occurring on N-termini (N--acetylation, NTA) and on internal lysines residues (-lysine-acetylation, KA). So far, NTA and KA were known to be supported by distinct families of enzymes (NATs and KATs, respectively), despite most of them sha...
ORGANISM(S): Escherichia Coli 
2020-07-07 | PXD015875 | JPOST Repository
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