Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

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.

Biochem/physiol Actions

Thermostable methionine aminopeptidase, which specifically liberates the N-terminal methioinine from proteins and peptides.

General description

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.

X-ray crystallography of the structure of methionine aminopeptidase from Pyrococcus furiosus or PfMAP was performed at a resolution of 1.75A and showed that the protein consists of a catalytic domain containing two cobalt ions in the active site and a unique insertion domain which is specific to the prokaryotic form of the protein.

Legal Information

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Physical form

Solution containing 0.01% Tween^® 20, 0.1 mM CoCl₂, and 10 mM Tris-HCl, pH 7.5.

Unit Definition

One unit will hydrolyze 1 µmol of Met from Met-Pro-Ala-Ala-Gly in 1 minute at pH 7.5 at 37 °C.