Document Type




Format of Original

13 p.

Publication Date




Source Publication

Journal of Biological Inorganic Chemistry

Source ISSN


Original Item ID

doi: 10.1007/s00775-009-0471-2; PubMed Central: PMCID 2678238


Methionine 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.


Accepted version. Journal of Biological Inorganic Chemistry, Vol.14, No. 4 (May 2009): 573-585. DOI. © 2009 Springer. Used with permission.

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Brian Bennett was affiliated with Medical College of Wisconsin at the time of publication.

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Richard Holz was affiliated with Loyola University-Chicago at the time of publication.

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