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Merck

M6435

Sigma-Aldrich

Methionine Aminopeptidase from Pyrococcus furiosus

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

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About This Item

Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

assay

≥93% (SDS-PAGE)

form

solution

specific activity

0.5 units/mg protein

mol wt

37 kDa by SDS-PAGE

UniProt accession no.

foreign activity

Other proteases, none detected

shipped in

dry ice

storage temp.

−20°C

Gene Information

Pyrococcus furiosus DSM 3638 ... PF0541(1468383)

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.

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.

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.

Legal Information

TWEEN is a registered trademark of Croda International PLC

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexperssion in Escherichia coli of the gene, and characteristics of the enzyme
Tsunasawa S, et al.
Journal of Biochemistry, 122(4), 843-850 (1997)
Advances in bacterial methionine aminopeptidase inhibition
Helgren TR, et al.
Current Topics in Medicinal Chemistry, 16(4), 397-414 (2016)
R A Bradshaw et al.
Trends in biochemical sciences, 23(7), 263-267 (1998-08-11)
Removal of the initiator methionine and/or acetylation of the alpha-amino group are among the earliest possible chemical modifications that occur during protein synthesis in eukaryotes. These events are catalyzed by methionine aminopeptidase and N alpha-acetyltransferase, respectively. Recent advances in the
Sanghamitra Mitra et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 14(4), 573-585 (2009-02-10)
Methionine aminopeptidases (MetAPs) represent a unique class of protease that is capable of the hydrolytic removal of an N-terminal methionine residue from nascent polypeptide chains. MetAPs are physiologically important enzymes; hence, there is considerable interest in developing inhibitors that can
A Ben-Bassat et al.
Journal of bacteriology, 169(2), 751-757 (1987-02-01)
Methionine aminopeptidase (MAP) catalyzes the removal of amino-terminal methionine from proteins. The Escherichia coli map gene encoding this enzyme was cloned; it consists of 264 codons and encodes a monomeric enzyme of 29,333 daltons. In vitro analyses with purified enzyme

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