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M6435 Sigma

Methionine Aminopeptidase from Pyrococcus furiosus

≥93% (SDS-PAGE), recombinant, expressed in E. coli



Related Categories Application Index, Biochemicals and Reagents, Enzymes, Inhibitors, and Substrates, Methionine Aminopeptidase, Proteases & Protein Sequencing,
recombinant   expressed in E. coli
assay   ≥93% (SDS-PAGE)
mol wt   mol wt 37 kDa by SDS-PAGE
foreign activity   Other proteases, none detected
shipped in   dry ice
storage temp.   −20°C
Gene Information   Pyrococcus furiosus DSM 3638 ... PF0541(1468383)


Biochem/physiol Actions

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

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.

Physical form

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


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.

General description

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.

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Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis

Certificate of Origin

Protocols & Articles
Peer-Reviewed Papers


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