추천 제품
재조합
expressed in E. coli
Quality Level
분석
≥93% (SDS-PAGE)
양식
solution
특이 활성도
0.5 units/mg protein
분자량
37 kDa by SDS-PAGE
UniProt 수납 번호
외래 활성
Other proteases, none detected
배송 상태
dry ice
저장 온도
−20°C
유전자 정보
Pyrococcus furiosus DSM 3638 ... PF0541(1468383)
관련 카테고리
일반 설명
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.
애플리케이션
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.
생화학적/생리학적 작용
Thermostable methionine aminopeptidase, which specifically liberates the N-terminal methioinine from proteins and peptides.
단위 정의
One unit will hydrolyze 1 μmol of Met from Met-Pro-Ala-Ala-Gly in 1 minute at pH 7.5 at 37 °C.
물리적 형태
Solution containing 0.01% Tween® 20, 0.1 mM CoCl2, and 10 mM Tris-HCl, pH 7.5.
법적 정보
TWEEN is a registered trademark of Croda International PLC
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
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
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 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
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)
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
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