Solution structure and mechanism of the MutT pyrophosphohydrolase
Solution structure and mechanism of the MutT pyrophosphohydrolase
复制标题
DOI：
10.1002/9780470123195.ch6
复制
发表时间：
1999-01-01
期刊：
影响因子：
--
通讯作者：
Abeygunawardana, C
中科院分区：
文献类型：
--
作者：
Mildvan, AS;Weber, DJ;Abeygunawardana, C
The discovery of the MutT enzyme resulted from the observations that a mutant strain of Escherichia coli, mutT, showed a lo3*'fold increase in mutation frequency (Treffers et al., 1954), which consisted exclusively of unidirectional AT+ CG transversions (Yanofsky et al., 1966). Cloning of the mutT+ gene by complementation of the MutT--mutator phenotype, as well as its expression, purification, and characterization, yielded an enzyme that catalyzed the unusual hydrolysis of nucleoside triphosphates (NTP) to nucleoside monophosphates (NMP) and pyrophosphate (Bhatnagar and Bessman, 1988; Akiyama et al., 1989).
