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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关于此项目
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
David L Bienvenue et al.
Biochemistry, 42(36), 10756-10763 (2003-09-10)
The catalytic and structural properties of divalent metal ion cofactor binding sites in the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) from Haemophilus influenzae were investigated. Co(II)-substituted DapE enzyme was 25% more active than the Zn(II)-loaded form of the enzyme. Interestingly, Mn(II)
Brian Bennett et al.
Journal of the American Chemical Society, 124(44), 13025-13034 (2002-10-31)
The aminopeptidase from Aeromonas proteolytica (AAP) was titrated with copper, which bound sequentially at two distinct sites. Both the mono- and disubstituted forms of AAP exhibited catalytic hyperactivity relative to the native dizinc enzyme. Monosubstituted AAP exhibited an axial Cu(II)
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
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
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
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