嗜酸嗜热古细菌嗜酸热原体中葡萄糖脱氢酶的纯化与特性分析
Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.
作者信息
Smith L D, Budgen N, Bungard S J, Danson M J, Hough D W
机构信息
Department of Biochemistry, University of Bath, U.K.
出版信息
Biochem J. 1989 Aug 1;261(3):973-7. doi: 10.1042/bj2610973.
Abstract
Glucose dehydrogenase was purified to homogeneity from the thermoacidophilic archaebacterium Thermoplasma acidophilum. The enzyme is a tetramer of polypeptide chain Mr 38,000 +/- 3000, it is catalytically active with both NAD+ and NADP+ cofactors, and it is thermostable and remarkably resistant to a variety of organic solvents. The amino acid composition was determined and compared with those of the glucose dehydrogenases from the archaebacterium Sulfolobus solfataricus and the eubacteria Bacillus subtilis and Bacillus megaterium. The N-terminal amino acid sequence of the Thermoplasma acidophilum enzyme was determined to be: (S/T)-E-Q-K-A-I-V-T-D-A-P-K-G-G-V-K-Y-T-T-I-D-M-P-E.
摘要
从嗜热嗜酸古细菌嗜酸热原体中纯化得到了均一的葡萄糖脱氢酶。该酶是一种分子量为38,000±3000的多肽链四聚体，对NAD⁺和NADP⁺两种辅因子均具有催化活性，具有热稳定性且对多种有机溶剂具有显著抗性。测定了其氨基酸组成，并与嗜热栖热硫化叶菌古细菌以及枯草芽孢杆菌和巨大芽孢杆菌真细菌的葡萄糖脱氢酶的氨基酸组成进行了比较。确定嗜酸热原体酶的N端氨基酸序列为：(S/T)-E-Q-K-A-I-V-T-D-A-P-K-G-G-V-K-Y-T-T-I-D-M-P-E。
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