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大肠杆菌的两种类似磷酸甘油酸变位酶。

The two analogous phosphoglycerate mutases of Escherichia coli.

作者信息

Fraser H I, Kvaratskhelia M, White M F

机构信息

Department of Biochemistry, University of Dundee, UK.

出版信息

FEBS Lett. 1999 Jul 23;455(3):344-8. doi: 10.1016/s0014-5793(99)00910-2.

DOI:10.1016/s0014-5793(99)00910-2
PMID:10437801
Abstract

The glycolytic enzyme phosphoglycerate mutase exists in two evolutionarily unrelated forms. Vertebrates have only the 2,3-bisphosphoglycerate-dependent enzyme (dPGM), whilst higher plants have only the cofactor-independent enzyme (iPGM). Certain eubacteria possess genes encoding both enzymes, and their respective metabolic roles and activities are unclear. We have over-expressed, purified and characterised the two PGMs of Escherichia coli. Both are expressed at high levels, but dPGM has a 10-fold higher specific activity than iPGM. Differential inhibition by vanadate was observed. The presence of an integral manganese ion in iPGM was confirmed by EPR spectroscopy.

摘要

糖酵解酶磷酸甘油酸变位酶以两种在进化上不相关的形式存在。脊椎动物仅具有依赖2,3-二磷酸甘油酸的酶(dPGM),而高等植物仅具有不依赖辅因子的酶(iPGM)。某些真细菌拥有编码这两种酶的基因,但其各自的代谢作用和活性尚不清楚。我们已经对大肠杆菌的两种PGM进行了过表达、纯化和表征。两者均高水平表达,但dPGM的比活性比iPGM高10倍。观察到钒酸盐的差异抑制作用。通过电子顺磁共振光谱证实了iPGM中存在一个完整的锰离子。

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