A8200
Aminopeptidase from Aeromonas proteolytica
lyophilized powder, 50-150 units/mg protein
Synonyme(s) :
AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
EC Number:
232-874-6
NACRES:
NA.54
MDL number:
Specific activity:
50-150 units/mg protein
Service technique
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Proteomics Grade
Quality Level
form
lyophilized powder
specific activity
50-150 units/mg protein
mol wt
29.5 kDa
composition
Protein, ~40% biuret
solubility
H2O: soluble 0.9-1.1 mg/mL, clear, colorless
foreign activity
endopeptidase, essentially free
storage temp.
−20°C
General description
A zinc-containing enzyme.
Application
Aminopeptidases are a family of widely distributed proteases, which may be used to study many significant biological processes such as protein maturation, hormone production, and peptide digestion. The enzyme has been used to measure the kinetic rate constant for the binding of bestatin, a general protease inhibitor, to aminopeptidase.
Biochem/physiol Actions
Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn2+ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at temperatures of 70 °C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase.
Aminopeptidase from Aeromonas proteolytica is involved in protein maturation, hormone production and peptide digestion.
Physical form
Lyophilized powder containing tricine buffer, pH 8.0, zinc chloride and stabilizer.
Preparation Note
Dissolves in water at 0.9-1.1 mg/mL concentration to form a clear, colorless solution.
Other Notes
One unit will hydrolyze 1.0 μmole of L-leucine p-nitroanilide to L-leucine and p-nitroaniline per min at pH 8.0 at 25 °C.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Classe de stockage
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Contenu apparenté
James Kahn et al.
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 38(4), 238-241 (2011-05-14)
We have recently designed a biochemistry laboratory experiment for the purpose of providing students an advanced experience with enzyme kinetics and the kinetics of binding. Bestatin, a well-known and commercially available general protease inhibitor, is a slow-binding inhibitor of aminopeptidase
S Nirasawa et al.
The Biochemical journal, 341 ( Pt 1), 25-31 (1999-06-23)
An aminopeptidase from Aeromonas caviae T-64 was translated as a preproprotein consisting of three domains; a signal peptide (19 amino acid residues), an N-terminal propeptide (101 residues) and a mature region (273 residues). We demonstrated that a proteinase, which was
Krzysztof P Bzymek et al.
The Journal of biological chemistry, 279(30), 31018-31025 (2004-05-13)
Glutamate 151 has been proposed to act as the general acid/base during the peptide hydrolysis reaction catalyzed by the co-catalytic metallohydrolase from Aeromonas proteolytica (AAP). However, to date, no direct evidence has been reported for the role of Glu-151 during
Numéro d'article de commerce international
| Référence | GTIN |
|---|---|
| A8200-100UN | 04061833391303 |
| A8200-250UN | 04061833391310 |