Characterization of a Glycyl-Specific TET Aminopeptidase Complex from Pyrococcus horikoshii.

ABSTRACT: The TET peptidases are large self-compartmentalized complexes that form dodecameric particles. These metallopeptidases, members of the M42 family, are widely distributed in prokaryotes. Three different versions of TET complexes, with different substrate specificities, were found to coexist in the cytosol of the hyperthermophilic archaeon Pyrococcus horikoshii In the present work, we identified a novel type of TET complex that we named PhTET4. The recombinant PhTET4 enzyme was found to self-assemble as a tetrahedral edifice similar to other TET complexes. We determined PhTET4 substrate specificity using a broad range of monoacyl chromogenic and fluorogenic compounds. High-performance liquid chromatographic peptide degradation assays were also performed. These experiments demonstrated that P

SUBMITTER: Basbous H 

PROVIDER: S-EPMC6088168 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature