A4987
Aminopeptidase His-tagged from Vibrio proteolyticus
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About This Item
Recommended Products
recombinant
expressed in E. coli
Quality Level
grade
Proteomics Grade
form
powder
specific activity
50-100 U/mg
shelf life
2 yr
shipped in
wet ice
storage temp.
−20°C
Unit Definition
One unit will hydrolyze 1.0 micromole of Leucine P-Nitroanilide to L-Leucine and P-Nitroaniline per minute at pH 8.0 at 25°C.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Niloufar J Ataie et al.
Biochemistry, 47(29), 7673-7683 (2008-06-26)
The chemical properties of zinc make it an ideal metal to study the role of coordination strain in enzymatic rate enhancement. The zinc ion and the protein residues that are bound directly to the zinc ion represent a functional charge/dipole
David L Bienvenue et al.
Biochemistry, 42(36), 10756-10763 (2003-09-10)
The catalytic and structural properties of divalent metal ion cofactor binding sites in the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae were investigated. Co(II)-substituted DapE enzyme was 25% more active than the Zn(II)-loaded form of the enzyme. Interestingly, Mn(II)
Kiet T Nguyen et al.
Methods in molecular medicine, 142, 117-130 (2008-04-26)
The emergence of bacterial pathogens resistant to current antibiotics has caused an urgent demand for new treatments. Peptide deformylase (PDF) has become an exciting target for designing novel antibiotics. To facilitate the screening of PDF inhibitors, three robust, coupled assays
K M Huntington et al.
Biochemistry, 38(47), 15587-15596 (1999-11-26)
Peptide-derived thiols of the general structure N-mercaptoacyl-leucyl-p-nitroanilide (1a-c) were synthesized and found to be potent, slow-binding inhibitors of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potencies (K(I)) of these inhibitors against AAP range from 2.5 to 57 nM exceeding
Brian Bennett et al.
Journal of the American Chemical Society, 124(44), 13025-13034 (2002-10-31)
The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which bound sequentially at two distinct sites. Both the mono- and disubstituted forms of AAP exhibited catalytic hyperactivity relative to the native dizinc enzyme. Monosubstituted AAP exhibited an axial Cu(II)
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