A8200

Sigma-Aldrich

Aminopeptidase from Aeromonas proteolytica

lyophilized powder, 50-150 units/mg protein

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:

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

Related Categories

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.

Packaging

100, 250 units in glass bottle

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

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Target Organs

Respiratory system

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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...
C Schalk et al.
Archives of biochemistry and biophysics, 294(1), 91-97 (1992-04-01)
The heat-stable aminopeptidase from Aeromonas proteolytica has been purified using two new procedures, with the aim of preparing large single crystals for X-ray analysis. In a first procedure, we tried to avoid any drastic conditions capable of inducing microheterogeneities in...
William T Desmarais et al.
Structure (London, England : 1993), 10(8), 1063-1072 (2002-08-15)
The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution...
D Mahadevan et al.
Protein science : a publication of the Protein Society, 8(11), 2546-2549 (1999-12-14)
The Aeromonas proteolytica aminopeptidase (AMP), Pseudomonas sp. (RS-16) carboxypeptidase G2 (CPG2), and Streptomyces griseus aminopeptidase (SGAP) are zinc dependent proteolytic enzymes with cocatalytic zinc ion centers and a conserved aminopeptidase fold. A BLAST search with the sequence of the solved...
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...

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