Description
Methionyl aminopeptidase (EC 3.4.11.18, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme. This enzyme catalyses the following chemical reaction:Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. This membrane-bound enzyme is present in both prokaryotes and eukaryotes.
Abbr
MAP, Recombinant (Pyrococcus furiosus)
Species
Pyrococcus furiosus
Applications
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.
Product Overview
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.
Form
Solution containing 0.01% Tween 20, 0.1 mM CoCl2, and 10 mM Tris-HCl, pH 7.5.
Enzyme Commission Number
EC 3.4.11.18
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.
Synonyms
Methionyl aminopeptidase; EC 3.4.11.18; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP
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