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 |
Substrate | 4-methylumbelliferyl-acetate |
Gene_locus | parde-FGHA |
Family | A85-EsteraseD-FGH |
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