An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling,inhibitory studies and molecular modeling |
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| Authors: | Ewelina Węglarz-Tomczak Marcin Poręba Anna Byzia Łukasz Berlicki Bogusław Nocek Rory Mulligan Andrzej Joachimiak Marcin Drąg Artur Mucha |
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| Affiliation: | 1. Department of Bioorganic Chemistry, Faculty of Chemistry, Wroc?aw University of Technology, Wybrze?e Wyspiańskiego 27, 50-370 Wroc?aw, Poland;2. The Midwest Center for Structural Genomics, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA |
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| Abstract: | Neisseria meningitides is a gram-negative diplococcus bacterium and is the main causative agent of meningitis and other meningococcal diseases. Alanine aminopeptidase from N. meningitides (NmAPN) belongs to the family of metallo-exopeptidase enzymes, which catalyze the removal of amino acids from the N-terminus of peptides and proteins, and are found among all the kingdoms of life. NmAPN is suggested to be mostly responsible for proteolysis and nutrition delivery, similar to the orthologs from other bacteria. |
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| Keywords: | M1 aminopeptidase Neisseria meningitidis Fluorogenic substrates Organophosphorus inhibitors S1 and S1&prime binding sites specificity |
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