S-(hydroxymethyl)glutathione dehydrogenase
| 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 | ||||||||
| |||||||||
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
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2FZE and 2FZW.
References
[edit]- 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". Carbohydrate Metabolism. 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.
