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.
CITATION STYLE
Harms, N., Ras, J., Reijnders, W. N. M., Van Spanning, R. J. M., & Stouthamer, A. H. (1996). S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: A universal pathway for formaldehyde detoxification? Journal of Bacteriology, 178(21), 6296–6299. https://doi.org/10.1128/jb.178.21.6296-6299.1996
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