A8200
Aminopeptidase from Aeromonas proteolytica
lyophilized powder, 50-150 units/mg protein
Sinônimo(s):
AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase
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About This Item
Número CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Produtos recomendados
grau
Proteomics Grade
Nível de qualidade
forma
lyophilized powder
atividade específica
50-150 units/mg protein
peso molecular
29.5 kDa
composição
Protein, ~40% biuret
solubilidade
H2O: soluble 0.9-1.1 mg/mL, clear, colorless
atividade externa
endopeptidase, essentially free
temperatura de armazenamento
−20°C
Descrição geral
A zinc-containing enzyme.
Especificidade
Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Aplicação
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.
Ações bioquímicas/fisiológicas
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.
Definição da unidade
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.
forma física
Lyophilized powder containing tricine buffer, pH 8.0, zinc chloride and stabilizer.
Nota de preparo
Dissolves in water at 0.9-1.1 mg/mL concentration to form a clear, colorless solution.
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Órgãos-alvo
Respiratory system
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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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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