Biology:S-(hydroxymethyl)glutathione dehydrogenase
| S-(hydroxymethyl)glutathione dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 | ||||||||
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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)+ [math]\displaystyle{ \rightleftharpoons }[/math] 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
- The Enzymes. 7 (2nd ed.). New York: Academic Press. 1963. pp. 203–221.
- "Formaldehyde dehydrogenase". Methods Enzymol. 9: 357–360. 1966. doi:10.1016/0076-6879(66)09073-6.
- "A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans". Nature 410 (6827): 490–4. 2001. doi:10.1038/35068596. PMID 11260719. Bibcode: 2001Natur.410..490L.
- "Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase". Biochemistry 39 (35): 10720–9. 2000. doi:10.1021/bi9929711. PMID 10978156.
- "Impact of hypothermia on the immunologic response after trauma and elective surgery". Surg. Technol. Int. 14: 41–50. 2005. 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. PMID 7798140.
- "Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides". J. Bacteriol. 178 (5): 1386–93. 1996. doi:10.1128/jb.178.5.1386-1393.1996. PMID 8631716.
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