75179-85-0Relevant academic research and scientific papers
Novel CoA-polyamine conjugates for effective inhibition of spermine/spermidine-N1-acetyltransferase
Simonian, Alina,Khomutov, Alex,Hyvonen, Tapani,Grigorenko, Nikolay,Keinanen, Tuomo,Vepsalainen, Jouko,Alhonen, Leena,Janne, Juhani
, p. 1245 - 1248 (2007)
New mimics of the transition state of spermine/spermidine-N1- acetyltransferase reaction were prepared starting from aminooxy analogues of spermidine or spermine and SH-CoA. The activity depended on the structure of polyamine fragment of the conjugate and best of the synthesized compounds were active at micromolar concentrations. Copyright Taylor & Francis Group, LLC.
Cofactor Analogues as Active Site Probes in Lysine Acetyltransferases
Simon, Roman P.,Rumpf, Tobias,Linkuviene, Vaida,Matulis, Daumantas,Akhtar, Asifa,Jung, Manfred
, p. 2582 - 2597 (2019/03/17)
Lysine acetyltransferases (KATs, also termed histone acetyltransferases, HATs) catalyze the acetylation of substrate lysine residues by employing the cofactor acetyl-coenzyme A (AcCoA), thereby providing a dynamic control mechanism of protein function. Because of their major involvement in cell development and homeostasis, small-molecule modulators of KAT activity are urgently needed to assess their therapeutic potential and for probing their underlying biology. Recent advances in the field suggest that targeting the cofactor binding site represents a promising strategy for identifying potent and selective ligands. Here, we present the synthesis of two functional cofactor-based chemical probes and their usage as mechanistic tools in a broadly applicable assay platform. A fluorescence polarization (FP)-based binding assay was combined with biolayer interferometry competition analysis and a FP competition activity immunoassay to enable easy, reliable, and profound evaluation of ligands that target the KAT cofactor binding site.
A general scheme for synthesis of substrate-based polyketide labels for acyl carrier proteins
Leggans, Erick K.,Akey, David L.,Smith, Janet L.,Fecik, Robert A.
supporting information; experimental part, p. 5939 - 5942 (2010/11/18)
A general strategy to enzymatically label acyl carrier proteins (ACPs) of polyketide synthases has been developed. Incorporation of a chloromethyl ketone or vinyl ketone moiety into polyketide chain elongation intermediate mimics allows for the synthesis of CoA adducts. These CoA adducts undergo enzymatic reaction with Sfp, a phosphopantetheinyl transferase, to afford labeled CurB carrier proteins.
