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• W2199660586 abstract "Methionine aminopeptidases (MetAPs) are metalloenzymes that cleave the N-terminal methionine from newly synthesized peptides and proteins. These MetAP enzymes are present in bacteria, and knockout experiments have shown that MetAP activity is essential for cell life, suggesting that MetAPs are good antibacterial drug targets. MetAP enzymes are also present in the human host and selectivity is essential. There have been significant structural biology efforts and over 65 protein crystal structures of bacterial MetAPs are deposited into the PDB. This review highlights the available crystallographic data for bacterial MetAPs. Structural comparison of bacterial MetAPs with human MetAPs highlights differences that can lead to selectivity. In addition, this review includes the chemical diversity of molecules that bind and inhibit the bacterial MetAP enzymes. Analysis of the structural biology and chemical space of known bacterial MetAP inhibitors leads to a greater understanding of this antibacterial target and the likely development of potential antibacterial agents. Keywords: Antibacterial, Metalloenzyme, Methionine aminopeptidase (MetAP), Protein crystal structure." @default.
• W2199660586 created "2016-06-24" @default.
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• W2199660586 creator A5005027480 @default.
• W2199660586 date "2015-10-14" @default.
• W2199660586 modified "2023-10-02" @default.
• W2199660586 title "Advances in Bacterial Methionine Aminopeptidase Inhibition" @default.
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• W2199660586 doi "https://doi.org/10.2174/1568026615666150813145410" @default.
• W2199660586 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5009474" @default.
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• W2199660586 hasPublicationYear "2015" @default.
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