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.应用： 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. 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.
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Methionine Aminopeptidase from Pyrococcus furiosus
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| CAS number | unknown | molecular formula | |
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