Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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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PMID:S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification? 889 32

We have examined the induction of glutathione-dependent formaldehyde dehydrogenase (GS-FDH) activity in Escherichia coli and Hemophilus influenza. Formaldehyde was found to induce enzyme activity in both E. coli and H. influenza at concentrations between 0.6 and 20 ppm. Higher formaldehyde concentrations were toxic. Methanol concentrations up to 20% (200,000 ppm) and sodium formate concentrations up to 2% (20,000 ppm) gave negligible amounts of induction. The basic mechanism of induction was probed by inducing GS-FDH activity in the presence of rifampicin to inhibit RNA synthesis or chloramphenicol to inhibit protein synthesis. Both reagents inhibited GS-FDH induction, demonstrating that regulation occurs at the level of transcription. These results indicate that at least one function of GS-FDH in Gram-negative bacteria is to detoxify exogenous formaldehyde encountered in their environment and that GS-FDH inducibility may be a common feature of Gram-negative bacteria.
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PMID:Induction of glutathione-dependent formaldehyde dehydrogenase activity in Escherichia coli and Hemophilus influenza. 933 39