所有图片(3)
别名:
AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase
CAS号:
EC 号:
MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.54
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一般描述
一种含锌的酶。
特异性
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。
应用
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。
生化/生理作用
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。
单位定义
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。
外形
含 tricine 缓冲液（pH 8.0）、氯化锌和稳定剂的冻干粉。
制备说明
以0.9-1.1 mg / mL的浓度溶于水，形成澄清的无色溶液。
警示用语：
Danger
危险分类
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
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
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
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
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