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
Marcus Elstner et al.
Journal of computational chemistry, 24(5), 565-581 (2003-03-13)
Parameters for the zinc ion have been developed in the self-consistent charge density functional tight-binding (SCC-DFTB) framework. The approach was tested against B3LYP calculations for a range of systems, including small molecules that contain the typical coordination environment of zinc
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
Gudrun Schürer et al.
Biochemistry, 43(18), 5414-5427 (2004-05-05)
The aminopeptidase of Aeromonas proteolytica (AAP) belongs to the group of metallo-hydrolases that require two divalent cations for full activity. Such binuclear metal centers are found in several aminopeptidases, raising the question whether a common mechanism, at least partly, is
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
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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