RELATION BETWEEN STABILITY, DYNAMICS AND ENZYME-ACTIVITY IN 3-PHOSPHOGLYCERATE KINASES FROM YEAST AND THERMUS-THERMOPHILUS

被引:108
作者
VARLEY, PG [1 ]
PAIN, RH [1 ]
机构
[1] UNIV NEWCASTLE UPON TYNE, DEPT BIOCHEM & GENET, NEWCASTLE UPON TYNE NE2 4HH, ENGLAND
关键词
3-PHOSPHOGLYCERATE KINASE; STABILITY; DYNAMICS; FLUORESCENCE LIFETIME; THERMOPHILIC PROTEINS;
D O I
10.1016/0022-2836(91)90028-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
3-Phosphoglycerate kinases from yeast and the extreme thermophilic bacterium Thermus thermophilus HB8 have been used as models for investigating the relationship between stability, dynamics and activity. It was found that while at a given temperature the thermophilic protein is more stable, its conformational dynamics as measured by the ability of acrylamide to quench the fluorescence of a buried tryptophan as well as its specific activity, are both lower than for the mesophilic protein. As the temperature is increased, the thermodynamic stability of the thermophilic protein approaches that of the mesophilic protein at its working temperature. Its conformational dynamics and specific activity however were both shown to increase, until at the physiologically operational temperature, they become similar to those of the mesophilic enzyme at its operational temperature. These results confirm the proposal that a direct relationship and balance holds between thermodynamic stability, dynamics and specific activity in globular proteins. They demonstrate also the constraining effect of increased stability upon conformational dynamics and enzyme activity. © 1991.
引用
收藏
页码:531 / 538
页数:8
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