Harms_1996_J.Bacteriol_178_6296

Reference

Title : S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification. - Harms_1996_J.Bacteriol_178_6296
Author(s) : Harms N , Ras J , Reijnders WNM , van Spanning RJM , Stouthamer AH
Ref : Journal of Bacteriology , 178 :6296 , 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.

PubMedSearch : Harms_1996_J.Bacteriol_178_6296
PubMedID: 8892832
Gene_locus related to this paper: parde-FGHA

Related information

Citations formats

Harms N, Ras J, Reijnders WNM, van Spanning RJM, Stouthamer AH (1996)
S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification.
Journal of Bacteriology 178 :6296

Harms N, Ras J, Reijnders WNM, van Spanning RJM, Stouthamer AH (1996)
Journal of Bacteriology 178 :6296