S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: A universal pathway for formaldehyde detoxification?

被引:102
作者
Harms, N
Ras, J
Reijnders, WNM
vanSpanning, RJM
Stouthamer, AH
机构
[1] Department of Microbial Physiology, Vrije Universiteit
[2] Department of Microbial Physiology, Vrije Universiteit, 1081HV Amsterdam
关键词
D O I
10.1128/jb.178.21.6296-6299.1996
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Dowstream 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,vith 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 methglotrophic growth. S-Formylglutathione hydrolase appears to be part of a formaldehyde detoxification pathway that is universal in nature.
引用
收藏
页码:6296 / 6299
页数:4
相关论文
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