Analyzing the Binding of Co(II)-specific Inhibitors to the Methionyl Aminopeptidases from Escherichia coli and Pyrococcus furiosusJournal of Biological Inorganic Chemistry
Format of Original13 p.
Original Item IDdoi: 10.1007/s00775-009-0471-2; PubMed Central: PMCID 2678238
AbstractMethionine aminopeptidases (MetAPs) represent a unique class of protease that is capable of the hydrolytic removal of an N-terminal methionine residue from nascent polypeptide chains. MetAPs are physiologically important enzymes; hence, there is considerable interest in developing inhibitors that can be used as antiangiogenic and antimicrobial agents. A detailed kinetic and spectroscopic study has been performed to probe the binding of a triazole-based inhibitor and a bestatin-based inhibitor to both Mn(II)- and Co(II)-loaded type-I (Escherichia coli) and type-II (Pyrococcus furiosus) MetAPs. Both inhibitors were found to be moderate competitive inhibitors. The triazole-type inhibitor was found to interact with both active-site metal ions, while the bestatin-type inhibitor was capable of switching its mode of binding depending on the metal in the active site and the type of MetAP enzyme.
Citation InformationSanghamitra Mitra, George Sheppard, Jieyi Wang, Brian Bennett, et al.. "Analyzing the Binding of Co(II)-specific Inhibitors to the Methionyl Aminopeptidases from Escherichia coli and Pyrococcus furiosus" Journal of Biological Inorganic Chemistry (2009) ISSN: 0949-8257
Available at: http://works.bepress.com/richard_holz/98/