巨大芽孢杆菌孢子和细胞中磷酸甘油酸磷酸变位酶的纯化及性质
Purification and properties of phosphoglycerate phosphomutase from spores and cells of Bacillus megaterium.
作者信息
Singh R P, Setlow P
出版信息
J Bacteriol. 1979 Feb;137(2):1024-7. doi: 10.1128/jb.137.2.1024-1027.1979.
Phosphoglycerate phosphomutase has been purified to homogeneity from vegetative cells and germinated spores of Bacillus megaterium, and the spore and cell enzymes appear identical. The enzyme is a monomer of molecular weight 61,000. The compound 2,3-diphosphoglyceric acid is not required for activity, but the enzyme has an absolute and specific requirement for Mn2+. The enzyme is inhibited by ethylenediaminetetraacetate and sulfhydryl reagents, has a pH optimum of about 8.0, and has Km values for 3-phosphoglyceric acid and Mn2+ of 5 x 10(-4) and 4 x 10(-5) M, respectively.
磷酸甘油酸磷酸变位酶已从巨大芽孢杆菌的营养细胞和萌发孢子中纯化至同质，且孢子和细胞中的酶看起来相同。该酶是分子量为61,000的单体。2,3 - 二磷酸甘油酸化合物对酶的活性并非必需，但该酶对Mn2+有绝对且特定的需求。该酶受乙二胺四乙酸和巯基试剂抑制，最适pH约为8.0，对3 - 磷酸甘油酸和Mn2+的Km值分别为5×10(-4) M和4×10(-5) M。
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