一般描述
大肠杆菌来源焦磷酸酶（E-PP酶）适用 pH 范围更广，每个亚基含4个二价阳离子。 由175个氨基酸组成，活性位点腔内有附加天冬氨酸残基。从结构上看，E-PP酶是同型六聚体，具有六个相同的20 kDa亚基。镁是E-PP酶的辅因子。
应用
大肠杆菌来源无机焦磷酸酶用于测定泛素蛋白缀合物和泛素样蛋白缀合物。还用于一锅三酶体系合成Lewis x 抗原和唾液酸化Lewis x 抗原。
大肠杆菌来源无机焦磷酸酶用作转录缓冲液成分。
无机焦磷酸酶 (PPase) 是一种普遍存在的酶，可催化 PPi + H2O → 2Pi。
它在蛋白质、RNA 和 DNA 合成中发挥着重要作用。
它在蛋白质、RNA 和 DNA 合成中发挥着重要作用。
生化/生理作用
大肠杆菌来源焦磷酸酶（E-PP酶）对酵母和细菌是必不可少的酶活性位点残基与镁结合至关重要。
其他说明
一种每个亚基含有175个氨基酸残基的同型六聚体蛋白，其活性依赖于Mg2+，是一种相对耐热的蛋白质。
单位定义
在25 °C条件下，当pH为9时，一个单位每分钟将释放1.0 μ无机正磷酸盐。
外形
冻干粉，溶于含蛋白酶抑制剂的 Tris 缓冲盐中
警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
WGK
WGK 3
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
Ngoc Truongvan et al.
Nature communications, 13(1), 4789-4789 (2022-08-16)
The covalent modification of target proteins with ubiquitin or ubiquitin-like modifiers is initiated by E1 activating enzymes, which typically transfer a single modifier onto cognate conjugating enzymes. UBA6 is an unusual E1 since it activates two highly distinct modifiers, ubiquitin
Christopher E Berndsen et al.
Analytical biochemistry, 418(1), 102-110 (2011-07-21)
Ubiquitination is a widely studied regulatory modification involved in protein degradation, DNA damage repair, and the immune response. Ubiquitin is conjugated to a substrate lysine in an enzymatic cascade involving an E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and an
The structure of E. coli soluble inorganic pyrophosphatase at 2.7
Kankare J, et al.
Protein engineering, design & selection : PEDS, 7(7), 823-830 (1994)
Elodie Laine et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(25), 11277-11282 (2010-06-11)
Allostery plays a key role in the regulation of the activity and function of many biomolecules. And although many ligands act through allostery, no systematic use is made of it in drug design strategies. Here we describe a procedure for
Rahul Sadavarte et al.
Biotechnology progress, 33(1), 133-139 (2016-11-01)
Heterologous overexpression of genes in Escherichia coli has made it possible to obtain high titers of recombinant proteins. However, this can result in the formation of aggregated protein particles known as 'inclusion bodies'. Protein sequestered as inclusion body is inactive
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