Molecular and biochemical characterisation of Mycobacterium smegmatis alcohol dehydrogenase C.
Molecular and biochemical characterisation of Mycobacterium smegmatis alcohol dehydrogenase C.
复制标题
耻垢分枝杆菌醇脱氢酶 C 的分子和生化特征。
DOI：
10.1111/j.1574-6968.2001.tb10683.x
复制
发表时间：
2001
影响因子：
2.1
通讯作者：
J. Content
中科院分区：
文献类型：
--
作者：
A. Galamba;K. Soetaert;P. Buyssens;D. Monnaie;P. Jacobs;J. Content
克隆了耻垢分枝杆菌乙醇脱氢酶C（ADHC）的编码基因，并进行了序列测定。该基因编码的蛋白与结核分枝杆菌和牛分枝杆菌BCG ADHC的同源性为78%。分枝从M.酶的动力学参数表明，以NADPH为电子供体，该酶对脂肪醛和芳香醛底物具有强烈的选择性。就像M。牛BCG ADHC，这种酶更可能作为醛还原酶而不是作为醇脱氢酶。在快速生长且易于工程化的分枝杆菌物种中发现这种ADHC为利用这种M.作为一个方便的模型，这种醇脱氢酶在分枝杆菌的生理作用的研究。
The gene encoding of an alcohol dehydrogenase C (ADHC) from Mycobacterium smegmatis was cloned and sequenced. The protein encoded by this gene has 78% identity with Mycobacterium tuberculosis and Mycobacterium bovis BCG ADHC. The M. smegmatis ADHC was purified from M. smegmatis and the kinetic parameters of this enzyme showed that using NADPH as electron donor it has a strong preference for aliphatic and aromatic aldehyde substrates. Like the M. bovis BCG ADHC, this enzyme is more likely to act as an aldehyde reductase than as an alcohol dehydrogenase. The discovery of such an ADHC in a fast-growing, and easily engineered mycobacterial species opens the way to the utilisation of this M. smegmatis enzyme as a convenient model for the study of the physiological role of this alcohol dehydrogenase in mycobacteria.
DOI：
10.1016/s0021-9258(18)61070-1
发表时间：
1987-07
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
P. Matsudaira
通讯作者：
P. Matsudaira