Haggarty N W, Dunbar B, Fothergill L A
EMBO J. 1983;2(7):1213-20. doi: 10.1002/j.1460-2075.1983.tb01569.x.
The complete amino acid sequence of human erythrocyte diphosphoglycerate mutase, comprising 239 residues, was determined. The sequence was deduced from the four cyanogen bromide fragments, and from the peptides derived from these fragments after digestion with a number of proteolytic enzymes. Comparison of this sequence with that of the yeast glycolytic enzyme, phosphoglycerate mutase, shows that these enzymes are 47% identical. Most, but not all, of the residues implicated as being important for the activity of the glycolytic mutase are conserved in the erythrocyte diphosphoglycerate mutase.
已确定由239个残基组成的人红细胞二磷酸甘油酸变位酶的完整氨基酸序列。该序列是从四个溴化氰片段以及用多种蛋白水解酶消化这些片段后得到的肽段推导出来的。将该序列与酵母糖酵解酶磷酸甘油酸变位酶的序列进行比较,结果表明这两种酶的序列一致性为47%。对糖酵解变位酶活性起重要作用的残基,大多数(但不是全部)在红细胞二磷酸甘油酸变位酶中保守。