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A8200

Sigma-Aldrich

Aminopeptidase from Aeromonas proteolytica

lyophilized powder, 50-150 units/mg protein

Synonym(s):

AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase

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About This Item

CAS Number:
37288-67-8
Enzyme Commission number:
3.4.11.10 (BRENDA, IUBMB)
EC Number:
232-874-6
MDL number:
MFCD00166325
UNSPSC Code:
12352204
NACRES:
NA.54

grade

Proteomics Grade

Quality Level

300

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.

Specificity

Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

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

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.

Unit Definition

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.

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.

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Precautionary Statements

P302 + P352 - P305 + P351 + P338

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

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

A8200-BULK:
A8200-100UN:
A8200-250UN:
A8200-VAR:
A8200-250UN-PW:
A8200-100UN-PW:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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