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

J Bacteriol. 1996 Nov;178(21):6296-9. doi: 10.1128/jb.178.21.6296-6299.1996.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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


  • Formaldehyde
  • Carboxylic Ester Hydrolases
  • Carboxylesterase
  • ESD protein, human
  • Thiolester Hydrolases
  • s-formylglutathione hydrolase
  • Serine Endopeptidases
  • Endopeptidase Clp
  • Adenosine Triphosphatases

Associated data

  • GENBANK/U32703
  • GENBANK/U34346
  • GENBANK/X88851