嗜冷菌
不稳定性
嗜热菌
酶
热稳定性
灵活性(工程)
寒冷的气候
极端微生物
冷冲击域
生物
生物化学
生物圈
功能(生物学)
化学
细胞生物学
生态学
物理
核糖核酸
气象学
基因
统计
数学
作者
Khawar Sohail Siddiqui,Ricardo Cavicchioli
标识
DOI:10.1146/annurev.biochem.75.103004.142723
摘要
By far the largest proportion of the Earth's biosphere is comprised of organisms that thrive in cold environments (psychrophiles). Their ability to proliferate in the cold is predicated on a capacity to synthesize cold-adapted enzymes. These enzymes have evolved a range of structural features that confer a high level of flexibility compared to thermostable homologs. High flexibility, particularly around the active site, is translated into low-activation enthalpy, low-substrate affinity, and high specific activity at low temperatures. High flexibility is also accompanied by a trade-off in stability, resulting in heat lability and, in the few cases studied, cold lability. This review addresses the structure, function, and stability of cold-adapted enzymes, highlighting the challenges for immediate and future consideration. Because of the unique properties of cold-adapted enzymes, they are not only an important focus in extremophile biology, but also represent a valuable model for fundamental research into protein folding and catalysis.
科研通智能强力驱动
Strongly Powered by AbleSci AI