Jolly L, Wu S, van Heijenoort J, de Lencastre H, Mengin-Lecreulx D, Tomasz A
Laboratoire des Enveloppes Bactériennes et des Peptides, Unité de Recherche Associée, Centre National de la Recherche Scientifique, Université Paris-Sud, Orsay, France.
J Bacteriol. 1997 Sep;179(17):5321-5. doi: 10.1128/jb.179.17.5321-5325.1997.
The femR315 gene was recently identified by Tn551 insertional mutagenesis as one of the new auxiliary genes, the alteration of which resulted in a drastically reduced methicillin resistance of the Staphylococcus aureus strain COL. femR315 (also known as femD) theoretically encoded a protein of 451 amino acids showing significant amino acid sequence homology with phosphoglucomutases and similar enzymes catalyzing the isomerization of hexoses and hexosamine phosphates (S. Wu, H. de Lencastre, A. Sali, and A. Tomasz, Microb. Drug Resist. 2:277-286, 1996). We describe here the overproduction and purification of the FemR315 protein as well as its identification as the phosphoglucosamine mutase which catalyzes the formation of glucosamine-1-phosphate from glucosamine-6-phosphate, the first step in the reaction sequence leading to the essential peptidoglycan precursor UDP-N-acetylglucosamine. On the basis of these findings, we propose to change the names femR315 and femD to the functionally more appropriate name glmM.
femR315基因最近通过Tn551插入诱变被鉴定为新的辅助基因之一，其改变导致金黄色葡萄球菌COL菌株的耐甲氧西林能力大幅降低。femR315（也称为femD）理论上编码一种451个氨基酸的蛋白质，与磷酸葡萄糖变位酶和催化己糖及己糖胺磷酸异构化的类似酶具有显著的氨基酸序列同源性（S. Wu、H. de Lencastre、A. Sali和A. Tomasz，《微生物药物抗性》2：277 - 286，1996）。我们在此描述了FemR315蛋白的过量表达和纯化，以及将其鉴定为磷酸葡糖胺变位酶，该酶催化从6 - 磷酸葡糖胺形成1 - 磷酸葡糖胺，这是导致必需肽聚糖前体UDP - N - 乙酰葡糖胺的反应序列中的第一步。基于这些发现，我们建议将femR315和femD的名称改为功能上更合适的名称glmM。
