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A8200

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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100 UNITS

$574.00

250 UNITS

$1,270.00

$574.00

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About This Item

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

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Product Name

Aminopeptidase from Aeromonas proteolytica, lyophilized powder, 50-150 units/mg protein

grade

Proteomics Grade

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

Quality Level

300

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This Item
P6236A9934P5380
Aminopeptidase from Aeromonas proteolytica lyophilized powder, 50-150 units/mg protein

Sigma-Aldrich

A8200

Aminopeptidase from Aeromonas proteolytica

Pyroglutamate Aminopeptidase from Pyrococcus furiosus recombinant, expressed in E. coli, ~90% (SDS-PAGE), ≥5.0 units/mg protein

Sigma-Aldrich

P6236

Pyroglutamate Aminopeptidase from Pyrococcus furiosus

Aminopeptidase I from Streptomyces griseus lyophilized powder, ≥200 units/mg protein

Sigma-Aldrich

A9934

Aminopeptidase I from Streptomyces griseus

Protease from Bacillus licheniformis Type VIII, lyophilized powder, 7-15 units/mg solid

Sigma-Aldrich

P5380

Protease from Bacillus licheniformis

specific activity

50-150 units/mg protein

specific activity

≥5.0 units/mg protein

specific activity

≥200 units/mg protein

specific activity

7-15 units/mg solid

grade

Proteomics Grade

grade

-

grade

-

grade

-

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

29.5 kDa

mol wt

24.072 kDa by amino acid sequence, 28 kDa by SDS-PAGE

mol wt

21 kDa by gel filtration, 33 kDa by SDS-PAGE

mol wt

27 kDa

solubility

H2O: soluble 0.9-1.1 mg/mL, clear, colorless

solubility

-

solubility

-

solubility

10 mM NaAc (pH 7.5) and 5 mM CaAc: soluble, clear, H2O: soluble, colorless

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

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.[1]

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.[2]
Aminopeptidase from Aeromonas proteolytica is involved in protein maturation, hormone production and peptide digestion.
Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

General description

A zinc-containing enzyme.

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.

Physical form

Lyophilized powder containing tricine buffer, pH 8.0, zinc chloride and stabilizer.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

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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Certificates of Analysis (COA)

Lot/Batch Number
0000483799
0000483799
0000463785
0000463785
0000463784

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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
G Van Heeke et al.
Biochimica et biophysica acta, 1131(3), 337-340 (1992-07-15)
The gene encoding the Vibrio proteolyticus aminopeptidase was cloned and sequenced and its amino acid sequence was deduced. The gene encodes a 54 kDa protein, larger than the previously reported size of 30 kDa for the purified aminopeptidase. Sequence alignments
L Ustynyuk et al.
Biochemistry, 38(35), 11433-11439 (1999-09-02)
Seven aliphatic and two aromatic alcohols were tested as reporters of the substrate selectivity of the aminopeptidase from Aeromonas proteolytica (AAP). This series of alcohols was chosen to systematically probe the effect of carbon chain length, steric bulk, and inhibitor
Krzysztof P Bzymek et al.
Inorganic chemistry, 44(23), 8574-8580 (2005-11-08)
Previous kinetic characterization of the glutamate 151 (E151)-substituted forms of the leucine aminopeptidase from Aeromonas proteolytica (Vibrio proteolyticus; AAP) has provided critical evidence that this residue functions as the general acid/base. The close proximity of similar glutamate residues to the
Carin C Stamper et al.
Biochemistry, 43(30), 9620-9628 (2004-07-28)
Binding of the competitive, slow-binding inhibitor bestatin ([(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoy]-leucine) to the aminopeptidase from Aeromonas proteolytica (AAP) was examined by both spectroscopic and crystallographic methods. Electronic absorption spectra of the catalytically competent [Co_(AAP)], [CoCo(AAP)], and [ZnCo(AAP)] enzymes recorded in the presence of
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