Le Boulch P, Joulin V, Garel M C, Rosa J, Cohen-Solal M
INSERM U. 91, Hôpital Henri Mondor, Créteil, France.
Biochem Biophys Res Commun. 1988 Oct 31;156(2):874-81. doi: 10.1016/s0006-291x(88)80925-2.
Cloning and sequencing of a murine cDNA with the entire coding region of 2,3-bisphosphoglycerate mutase is reported, as a prerequisite for further expression studies of this erythroid specific enzyme in Friend mouse erythroleukemia cells. A comparison between species of the deduced amino acid sequences of these proteins shows 20 substitutions between mouse and human and 21 between mouse and rabbit: none of these substitutions are in positions assumed to be in the active site. Amino acid alignment with the other related enzymes, the phosphoglycerate mutases, in combination with crystallographic data from yeast phosphoglycerate mutase, gives some insight into the structure/function correlation for this protein family. Amino acid residues which are most likely critical for either 2,3-bisphosphoglycerate mutase or phosphoglycerate mutase function are pointed out. Concerning the phylogenetic analysis, phosphoglycerate mutases B and M from mammalians appear to have diverged with the yeast enzyme from a common ancestor, before the emergence of the 2,3-bisphosphoglycerate mutases.
报道了小鼠2,3-二磷酸甘油酸变位酶完整编码区cDNA的克隆与测序，这是在Friend小鼠红白血病细胞中进一步研究这种红系特异性酶表达的前提条件。这些蛋白质推导氨基酸序列的种间比较显示，小鼠与人之间有20个替换，小鼠与兔之间有21个替换：这些替换均不在假定的活性位点位置。与其他相关酶磷酸甘油酸变位酶的氨基酸比对，结合酵母磷酸甘油酸变位酶的晶体学数据，为该蛋白家族的结构/功能相关性提供了一些见解。指出了对2,3-二磷酸甘油酸变位酶或磷酸甘油酸变位酶功能最可能至关重要的氨基酸残基。关于系统发育分析，哺乳动物的磷酸甘油酸变位酶B和M似乎在2,3-二磷酸甘油酸变位酶出现之前就已与酵母酶从共同祖先分化而来。
