M6435
Methionine Aminopeptidase from Pyrococcus furiosus
≥93% (SDS-PAGE), recombinant, expressed in E. coli
Faça loginpara ver os preços organizacionais e de contrato
About This Item
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Produtos recomendados
recombinante
expressed in E. coli
Nível de qualidade
Ensaio
≥93% (SDS-PAGE)
Formulário
solution
atividade específica
0.5 units/mg protein
peso molecular
37 kDa by SDS-PAGE
nº de adesão UniProt
atividade externa
Other proteases, none detected
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
Informações sobre genes
Pyrococcus furiosus DSM 3638 ... PF0541(1468383)
Descrição geral
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.
Aplicação
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.
Ações bioquímicas/fisiológicas
Thermostable methionine aminopeptidase, which specifically liberates the N-terminal methioinine from proteins and peptides.
Definição da unidade
One unit will hydrolyze 1 μmol of Met from Met-Pro-Ala-Ala-Gly in 1 minute at pH 7.5 at 37 °C.
forma física
Solution containing 0.01% Tween® 20, 0.1 mM CoCl2, and 10 mM Tris-HCl, pH 7.5.
Informações legais
TWEEN is a registered trademark of Croda International PLC
Código de classe de armazenamento
12 - Non Combustible Liquids
Classe de risco de água (WGK)
WGK 2
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Escolha uma das versões mais recentes:
Já possui este produto?
Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.
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)
S Tsunasawa et al.
Journal of biochemistry, 122(4), 843-850 (1997-12-17)
A gene for a methionine aminopeptidase (MAP; EC 3.4.11.18), which catalyzes the removal of amino-terminal methionine from the growing peptide chain on the ribosome, has been cloned from the hyperthermophilic Archaeon, Pyrococcus furiosus, by a novel method effectively using its
T H Tahirov et al.
Journal of molecular biology, 284(1), 101-124 (1998-11-13)
The structure of methionine aminopeptidase from hyperthermophile Pyrococcus furiosus (PfMAP) with an optimal growth temperature of 100 degreesC was determined by the multiple isomorphous replacement method and refined in three different crystal forms, one monoclinic and two hexagonal, at resolutions
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
Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.
Entre em contato com a assistência técnica