PMID:8892832

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Citation

Harms, N, Ras, J, Reijnders, WN, van Spanning, RJ and Stouthamer, AH (1996) S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification? J. Bacteriol. 178:6296-9

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.

Links

PubMed PMC178503

Keywords

Adenosine Triphosphatases; Carboxylesterase; Carboxylic Ester Hydrolases/metabolism; Endopeptidase Clp; Formaldehyde/toxicity; Humans; Molecular Sequence Data; Mutation; Paracoccus denitrificans/enzymology; Paracoccus denitrificans/genetics; Sequence Homology, Amino Acid; Serine Endopeptidases/genetics; Thiolester Hydrolases/genetics; Thiolester Hydrolases/metabolism

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