J. Bacteriol., Nov 1996, 6296-6299, Vol 178, No. 21
Copyright © 1996, American Society for Microbiology

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

N Harms, J Ras, WN Reijnders, RJ van Spanning and AH Stouthamer
Department of Microbial Physiology, Vrije Universiteit, Amsterdam, The Netherlands. harms@bio.vu.nl.

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.

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