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• W2334165275 abstract "Methionine aminopeptidases (MetAPs) are essential enzymes that make them good drug targets in cancer and microbial infections. MetAPs remove the initiator methionine from newly synthesized peptides in every living cell. MetAPs are broadly divided into type I and type II classes. Both prokaryotes and eukaryotes contain type I MetAPs, while eukaryotes have additional type II MetAP enzyme. Although several inhibitors have been reported against type I enzymes, subclass specificity is scarce. Here, using the fine differences in the entrance of the active sites of MetAPs from Mycobacterium tuberculosis , Enterococcus faecalis , and human, three hotspots have been identified and pyridinylpyrimidine-based molecules were selected from a commercial source to target these hotspots. In the biochemical evaluation, many of the 38 compounds displayed differential behavior against these three enzymes. Crystal structures of four selected inhibitors in complex with human MetAP1b and molecular modeling studies provided the basis for the binding specificity." @default.
• W2334165275 created "2016-06-24" @default.
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• W2334165275 date "2013-06-27" @default.
• W2334165275 modified "2023-09-23" @default.
• W2334165275 title "Identification, Biochemical and Structural Evaluation of Species-Specific Inhibitors against Type I Methionine Aminopeptidases" @default.
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• W2334165275 doi "https://doi.org/10.1021/jm400395p" @default.
• W2334165275 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23767698" @default.
• W2334165275 hasPublicationYear "2013" @default.
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