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, S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are S-(hydroxymethyl)glutathione and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are S-formylglutathione, reduced NADH, and a proton. The enzyme can also use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.[1][2][3][4][5]
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
- ^ Enzyme 1.1.1.284 at KEGG Pathway Database.
- ^ 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.
- ^ 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.