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一般描述
Methionine aminopeptidase from Pyrococcus furiosus is a 32 kDa thermostable enzyme.[1] It belongs to type 2a class of methionine aminopeptidase. Methionine aminopeptidase maintains protein homeostasis and coordinates posttranslational modification of proteins in eukaryotes.[2]
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. [3]
应用
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. [4] It has also been used in a study to examine the binding of a new class of pseudopeptide analog inhibitors. [5]
生化/生理作用
Thermostable methionine aminopeptidase, which specifically liberates the N-terminal methioinine from proteins and peptides.
单位定义
One unit will hydrolyze 1 μmol of Met from Met-Pro-Ala-Ala-Gly in 1 minute at pH 7.5 at 37 °C.
外形
Solution containing 0.01% Tween® 20, 0.1 mM CoCl2, and 10 mM Tris-HCl, pH 7.5.
法律信息
TWEEN is a registered trademark of Croda International PLC
储存分类代码
12 - Non Combustible Liquids
WGK
WGK 2
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Advances in bacterial methionine aminopeptidase inhibition
Helgren TR, et al.
Current Topics in Medicinal Chemistry, 16(4), 397-414 (2016)
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
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
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
A new colorimetric assay for methionyl aminopeptidases: Examination of the binding of a new class of pseudopeptide analog inhibitors
Mitra, S., et al.
Analytical Biochemistry, 357, 7-7 (2006)
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