Methionine Aminopeptidase from Pyrococcus furiosus

3.4.11.18 ( BRENDA | IUBMB )

MFCD03457470

NA.54

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.

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.

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

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

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

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200

expressed in E. coli

≥93% (SDS-PAGE)

solution

0.5 units/mg protein

37 kDa by SDS-PAGE

P56218

Other proteases, none detected

dry ice

−20℃

Pyrococcus furiosus DSM 3638 ... PF0541(1468383)

12 - Non Combustible Liquids

WGK 2