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首页> 外文期刊>Protein Expression and Purification >Expression, purification, and characterization of a functionally active Mycobacterium tuberculosis UDP-glucose pyrophosphorylase
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Expression, purification, and characterization of a functionally active Mycobacterium tuberculosis UDP-glucose pyrophosphorylase

机译：具有功能活性的结核分枝杆菌UDP-葡萄糖焦磷酸化酶的表达，纯化和鉴定

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摘要

Tuberculosis, which is caused by Mycobacterium tuberculosis, remains to be a global health problem. The thick and complex cell envelope has been implicated in many aspects of the pathogenicity of M. tuberculosis. M. tuberculosis UDP-glucose pyrophosphorylase (UGP, coded by galU, Rv0993) is involved in cell envelope precursor synthesis. UGP catalyzes the reversible formation of UDP-glucose and inorganic pyrophosphate from UTP and glucose 1-phosphate (Glc-1-P). Bacterial UGPs are completely unrelated to their eukaryotic counterparts. This enzyme is recognized as a virulence factor in several bacterial species and is conserved among mycobacterial species, which makes it a good target for mycobacterial pathogenicity research. The recombinant M. tuberculosis UGP (rMtUGP) was purified in Escherichia coli and found to be stable and catalytically active. The effects of pH, temperature and Mg2+ on enzyme activity were characterized. In addition, subcellular localization studies revealed that most of M. tuberculosis UGP protein was located in the cell wall. The purification and characterization of M. tuberculosis UGP may help to decipher the pathogenicity of M. tuberculosis. (C) 2008 Elsevier Inc. All rights reserved.
机译：由结核分枝杆菌引起的结核病仍然是全球健康问题。厚而复杂的细胞包膜与结核分枝杆菌的致病性的许多方面有关。结核分枝杆菌UDP-葡萄糖焦磷酸化酶（UGP，由galU编码，Rv0993）参与细胞包膜前体的合成。 UGP催化UTP和1-磷酸葡萄糖（Glc-1-P）可逆地形成UDP-葡萄糖和无机焦磷酸盐。细菌UGP与它们的真核对应物完全无关。这种酶在几种细菌中被认为是一种致病因子，在分枝杆菌中是保守的，这使其成为分枝杆菌致病性研究的良好靶标。重组结核分枝杆菌UGP（rMtUGP）在大肠杆菌中纯化，发现是稳定的并具有催化活性。表征了pH，温度和Mg2 +对酶活性的影响。此外，亚细胞定位研究表明，结核分枝杆菌UGP蛋白大多数位于细胞壁中。结核分枝杆菌UGP的纯化和表征可能有助于破译结核分枝杆菌的致病性。 （C）2008 Elsevier Inc.保留所有权利。

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