A8200
氨基肽酶 来源于溶解蛋白单孢菌
lyophilized powder, 50-150 units/mg protein
别名:
AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase
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化学文摘社编号:
UNSPSC Code:
12352204
EC Number:
232-874-6
NACRES:
NA.54
MDL number:
Specific activity:
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
General description
一种含锌的酶。
Application
氨肽酶是一类分布广泛的蛋白酶家族，可用于研究蛋白质成熟、激素产生、吸收消化等许多重要的生物学过程。这种酶已被用来测量bestatin（一种蛋白酶抑制剂）与氨肽酶结合的动力学速率常数。
Biochem/physiol Actions
蛋白水解气单胞菌的氨肽酶参与蛋白质成熟、激素生成和肽消化。
蛋白质气单胞菌氨肽酶是一种金属酶，通过重组法测得，氨肽酶在一个单体中含有2个zn2 +原子，分子量约为29.5 kDa。这种酶具有高度的稳定性，即使在70℃的温度下也可稳定数小时。部分失活发生在8 M尿素中。最大的稳定性和活性在pH 8.0-8.5之间。蛋白纯化气单胞菌的氨肽酶可发挥酯酶的作用。
催化释放 N -末端氨基酸，优先释放亮氨酸，而不是谷氨酸或天冬氨酸。
Physical form
含 tricine 缓冲液（pH 8.0）、氯化锌和稳定剂的冻干粉。
Preparation Note
以0.9-1.1 mg / mL的浓度溶于水，形成澄清的无色溶液。
Other Notes
在25℃、pH 8.0条件下，每分钟可将1.0μ956摩尔的L-亮氨酸对硝基苯胺水解为L-亮氨酸和对硝基苯胺。
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
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
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
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
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