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S-(hydroxymethyl)glutathione dehydrogenase
Identifiers
EC no. 1.1.1.284
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a S-(hydroxymethyl)glutathione dehydrogenase ( EC 1.1.1.284) is an enzyme that catalyzes the chemical reaction

S-(hydroxymethyl)glutathione + NAD(P)+ S-formylglutathione + NAD(P)H + H+

The 3 substrates of this enzyme are S-(hydroxymethyl)glutathione, NAD+, and NADP+, whereas its 4 products are S-formylglutathione, NADH, NADPH, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is S-(hydroxymethyl)glutathione:NAD+ oxidoreductase. Other names in common use include NAD-linked formaldehyde dehydrogenase (incorrect), formaldehyde dehydrogenase (incorrect), formic dehydrogenase (incorrect), class III alcohol dehydrogenase, ADH3, &chi, -ADH, FDH (incorrect), formaldehyde dehydrogenase (glutathione) (incorrect), GS-FDH (incorrect), glutathione-dependent formaldehyde dehydrogenase (incorrect), NAD-dependent formaldehyde dehydrogenase, GD-FALDH, and NAD- and glutathione-dependent formaldehyde dehydrogenase. This enzyme participates in methane metabolism.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2FZE and 2FZW.

References

  • Boyer, P.D.; Lardy, H.; Myrback, K., eds. (1963). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 203–221.
  • Rose ZB, Racker E (1966). Formaldehyde dehydrogenase. Methods Enzymol. Vol. 9. pp. 357–360. doi: 10.1016/0076-6879(66)09073-6. ISBN  978-0-12-181809-8.
  • Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS (2001). "A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans". Nature. 410 (6827): 490–4. Bibcode: 2001Natur.410..490L. doi: 10.1038/35068596. PMID  11260719. S2CID  21280374.
  • Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF (2000). "Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase". Biochemistry. 39 (35): 10720–9. doi: 10.1021/bi9929711. PMID  10978156.
  • Probst C, Grotz M, Krettek C, Pape HC (2005). "Impact of hypothermia on the immunologic response after trauma and elective surgery". Surg. Technol. Int. 14: 41–50. PMID  16525953.
  • Stouthamer AH; Harms N (1995). "Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth". J. Bacteriol. 177 (1): 247–51. doi: 10.1128/jb.177.1.247-251.1995. PMC  176581. PMID  7798140.
  • Barber RD, Rott MA, Donohue TJ (1996). "Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides". J. Bacteriol. 178 (5): 1386–93. doi: 10.1128/jb.178.5.1386-1393.1996. PMC  177813. PMID  8631716.