White P J, Nairn J, Price N C, Nimmo H G, Coggins J R, Hunter I S
Department of Biochemistry, University of Glasgow, United Kingdom.
J Bacteriol. 1992 Jan;174(2):434-40. doi: 10.1128/jb.174.2.434-440.1992.
The enzyme 3-phosphoglycerate mutase was purified 192-fold from Streptomyces coelicolor, and its N-terminal sequence was determined. The enzyme is tetrameric with a subunit Mr of 29,000. It is 2,3-bisphosphoglycerate dependent and inhibited by vanadate. The gene encoding the enzyme was cloned by using a synthetic oligonucleotide probe designed from the N-terminal peptide sequence, and the complete coding sequence was determined. The deduced amino acid sequence is 64% identical to that of the phosphoglycerate mutase of Saccharomyces cerevisiae and has substantial identity to those of other phosphoglycerate mutases.
从天蓝色链霉菌中纯化出3-磷酸甘油酸变位酶,纯化倍数为192倍,并测定了其N端序列。该酶为四聚体,亚基分子量为29,000。它依赖2,3-二磷酸甘油酸,并受钒酸盐抑制。利用根据N端肽序列设计的合成寡核苷酸探针克隆了编码该酶的基因,并测定了完整的编码序列。推导的氨基酸序列与酿酒酵母的磷酸甘油酸变位酶的氨基酸序列有64%的同一性,与其他磷酸甘油酸变位酶的氨基酸序列也有显著的同一性。