Methionine Aminopeptidase from Pyrococcus furiosus has been used in a study to analyze the binding of Co(II)-specific inhibitors to the methionyl aminopeptidases from Escherichia coli and Pyrococcus furiosus. It has also been used in a study to examine the binding of a new class of pseudopeptide analog inhibitors.
Methionine aminopeptidase from Pyrococcus furiosus is a 32 kDa thermostable enzyme. It belongs to type 2a class of methionine aminopeptidase. Methionine aminopeptidase maintains protein homeostasis and coordinates posttranslational modification of proteins in eukaryotes.
Thermostable methionine aminopeptidase, which specifically liberates the N-terminal methioinine from proteins and peptides.
