S-(hydroxymethyl)glutathione dehydrogenase

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

+ NAD+
 
 
 
H+
S-(hydroxymethyl)glutathione dehydrogenase
 
H+
 
+ NADH
 

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

  1. Enzyme 1.1.1.284 at KEGG Pathway Database.
  2. 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.
  3. 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.
  4. 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.
  5. 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.