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Methionine Aminopeptidase from Pyrococcus furiosus, Recombinant

Cat No.
NATE-0442
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)
Alias
MAP
Source
E. coli
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
CAS No.
9025-42-7
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.
Storage
−20°C
Synonyms
Methionyl aminopeptidase; EC 3.4.11.18; methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP
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CatalogNATE-1018
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SourceE. coli
CatalogEXWM-4014
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Source
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