P6675
脯氨酸二肽酶 来源于猪肾脏
lyophilized powder, ≥100 units/mg protein
别名:
亚胺二肽酶, 氨酰基-L-脯氨酸水解酶, 脯氨酸二肽酶, 蛋白酶
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关于此项目
化学文摘社编号:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-791-5
MDL number:
Specific activity:
≥100 units/mg protein
form
lyophilized powder
specific activity
≥100 units/mg protein
composition
Protein, 20-74% Lowry
storage temp.
−20°C
Quality Level
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General description
脯氨酸蛋白酶是一种胞内外肽酶。它是一种同二聚酶，在其活性位点中需要二价阳离子（如锰）作为辅因子才能发挥其功能。
Application
来自猪肾脏的蛋白酶已用于：
- 酶水解猪乳中的蛋白质和多肽中的 L-谷氨酰胺的回收
- 脱脂乳蛋白水解法测定 ε-（γ-谷氨酰基）赖氨酸和游离氨基酸
- 测定其对肠球菌素 A 2000 活性的影响
脯氨酸蛋白酶在脯氨酸的循环利用和胶原蛋白的生产中具有重要作用。它被用来研究导致脯氨酸酶缺乏的 PEPD 基因的突变。它用于水解具有 C 末端脯氨酸或羟脯氨酸残基的蛋白质。在研究膜蛋白的酶促甲基化反应时，来自猪肾脏的脯氨酸蛋白酶（货号 P6675）已用于水解氨基末端的肽键。
Biochem/physiol Actions
脯氨酸蛋白酶是催化 α-羧基与脯氨酸或羟脯氨酸之间的酰亚胺键水解的酶。该蛋白质形成同二聚体，该同二聚体水解具有 C 末端脯氨酸或羟脯氨酸残基的二肽或三肽。
脯氨酸酶基因的罕见突变会引起缺陷，导致亚氨基二肽尿大量增加，血浆中含脯氨酸的二肽升高、反复感染、智力低下和皮肤损伤。
Physical form
以含有 Tris 缓冲盐和 MnCl2 的冻干粉末形式提供。
Other Notes
在 pH 8.0，40 °C 条件下，1 个单位将每分钟水解 1.0 μmole Gly-Pro。
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
法规信息
低风险生物材料
此项目有
Mehmet A Altay et al.
Scandinavian journal of clinical and laboratory investigation, 71(7), 576-582 (2011-08-13)
We aimed to investigate serum prolidase activity and to find out its association with oxidative-antioxidative status in patients with idiopathic clubfoot and during the course of the disease. Oxidative status parameters, including total free sulfhydryl groups (-SH), total antioxidant capacity
Roberta Besio et al.
Clinica chimica acta; international journal of clinical chemistry, 412(19-20), 1814-1820 (2011-06-28)
Prolidase is a metallo-exopeptidase hydrolyzing X-Pro and X-Hyp dipeptides. Its absence or reduced level is typical in prolidase deficiency (PD) patients, and altered prolidase activity was reported in various diseases. Therefore, standardized and accurate measurement of prolidase activity is essential
Marta E Alberto et al.
Inorganic chemistry, 50(8), 3394-3403 (2011-03-24)
The catalytic hydrolysis of the Gly-Pro substrate by the bimetallic prolidase active site model cluster has been investigated at the DF/B3LYP level of theory, in order to provide fundamental insights into the still poorly understood mechanism of prolidase catalysis. To
Jian An Chen et al.
Biochimica et biophysica acta, 1814(12), 1677-1685 (2011-08-31)
Allosteric behavior and substrate inhibition are unique characteristics of Lactococcus lactis prolidase. We hypothesized that charged residues (Asp36, His38, Glu39, and Arg40), present on one loop essential for catalysis, interact with residues in or near the active site to impart
Influence of transglutaminase treatment of skim milk on the formation of varepsilon-(Γ-glutamyl) lysine and the susceptibility of individual proteins towards crosslinking
Sharma R, et al.
International dairy journal, 11(10), 785-793 (2001)
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