反硝化副球菌的S-甲酰谷胱甘肽水解酶与人类酯酶D同源：甲醛解毒的通用途径？
S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?
作者信息
Harms N, Ras J, Reijnders W N, van Spanning R J, Stouthamer A H
机构信息
Department of Microbial Physiology, Vrije Universiteit, Amsterdam, The Netherlands.
出版信息
J Bacteriol. 1996 Nov;178(21):6296-9. doi: 10.1128/jb.178.21.6296-6299.1996.
Abstract
Downstream of flhA, the Paracoccus denitrificans gene encoding glutathione-dependent formaldehyde dehydrogenase, an open reading frame was identified and called fghA. The gene product of fghA showed appreciable similarity with human esterase D and with the deduced amino acid sequences of open reading frames found in Escherichia coli, Haemophilus influenzae, and Saccharomyces cerevisiae. Mutating fghA strongly reduced S-formylglutathione hydrolase activity. The mutant was unable to grow on methanol and methylamine, indicating that the enzyme is essential for methylotrophic growth. S-Formylglutathione hydrolase appears to be part of a formaldehyde detoxification pathway that is universal in nature.
摘要
在编码谷胱甘肽依赖性甲醛脱氢酶的反硝化副球菌基因flhA的下游，鉴定出一个开放阅读框并将其命名为fghA。fghA的基因产物与人类酯酶D以及在大肠杆菌、流感嗜血杆菌和酿酒酵母中发现的开放阅读框推导的氨基酸序列具有明显的相似性。fghA发生突变会强烈降低S-甲酰谷胱甘肽水解酶的活性。该突变体无法在甲醇和甲胺上生长，这表明该酶对于甲基营养生长至关重要。S-甲酰谷胱甘肽水解酶似乎是自然界中普遍存在的甲醛解毒途径的一部分。
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