古菌中磷酸甘油酸变位酶的分子特征

Molecular characterization of phosphoglycerate mutase in archaea.

作者信息

van der Oost John, Huynen Martijn A, Verhees Corné H

机构信息

Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen, The Netherlands.

出版信息

FEMS Microbiol Lett. 2002 Jun 18;212(1):111-20. doi: 10.1111/j.1574-6968.2002.tb11253.x.

DOI:10.1111/j.1574-6968.2002.tb11253.x

PMID:12076796

Abstract

The interconversion of 3-phosphoglycerate and 2-phosphoglycerate during glycolysis and gluconeogenesis is catalyzed by phosphoglycerate mutase (PGM). In bacteria and eukaryotes two structurally distinct enzymes have been found, a cofactor-dependent and a cofactor-independent (iPGM) type. Sequence analysis of archaeal genomes did not find PGMs of either kind, but identified a new family of proteins, distantly related to iPGMs. In this study, these predicted archaeal PGMs from Pyrococcus furiosus and Methanococcus jannaschii have been functionally produced in Escherichia coli, and characterization of the purified proteins has confirmed that they are iPGMs. Analysis of the available microbial genomes indicates that this new type of iPGM is widely distributed among archaea and also encoded in several bacteria. In addition, as has been demonstrated in certain bacteria, some archaea appear to possess an alternative, cofactor-dependent PGM.

摘要

糖酵解和糖异生过程中3-磷酸甘油酸和2-磷酸甘油酸的相互转化由磷酸甘油酸变位酶（PGM）催化。在细菌和真核生物中已发现两种结构不同的酶，一种是依赖辅因子的类型，另一种是不依赖辅因子的（iPGM）类型。对古菌基因组的序列分析未发现这两种类型的PGM，但鉴定出了一个与iPGM有远缘关系的新蛋白质家族。在本研究中，来自嗜热栖热菌和詹氏甲烷球菌的这些预测的古菌PGM已在大肠杆菌中实现功能表达，对纯化蛋白的特性分析证实它们是iPGM。对现有微生物基因组的分析表明，这种新型iPGM广泛分布于古菌中，并且在几种细菌中也有编码。此外，正如在某些细菌中所证实的那样，一些古菌似乎还拥有另一种依赖辅因子的PGM。