EC 1.1.1.284 - S-(hydroxymethyl)glutathione dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.1.1.284

Names

Accepted name:
S-(hydroxymethyl)glutathione dehydrogenase
Other names:
NAD-linked formaldehyde dehydrogenase [incorrect]
formaldehyde dehydrogenase [incorrect]
formic dehydrogenase [incorrect]
class III alcohol dehydrogenase
ADH3
χ-ADH
FDH [incorrect]
formaldehyde dehydrogenase (glutathione) [incorrect]
glutathione-dependent formaldehyde dehydrogenase [incorrect]
GS-FDH [incorrect]
NAD-dependent formaldehyde dehydrogenase
GD-FALDH
NAD- and glutathione-dependent formaldehyde dehydrogenase
Systematic name:
S-(hydroxymethyl)glutathione:NAD+ oxidoreductase

Reactions

Comments:

The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UM-BBD , UniPathway
Protein domains and families: PROSITE:PDOC00058
Structural data: CSA , EC2PDB
Gene Ontology: GO:0051903
CAS Registry Number: 9028-84-6
UniProtKB/Swiss-Prot: (44) [show] [UniProt]

References

  1. Jakoby, W.B.
    Aldehyde dehydrogenases.
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes, 2nd ed. vol. 7, Academic Press, New York, 1963, 203-221
  2. Rose, Z.B. and Racker, E.
    Formaldehyde dehydrogenase.
    Methods Enzymol. 9: 357-360 (1966).
  3. Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S.
    A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans.
    Nature 410: 490-494 (2001). [PMID: 11260719]
  4. Sanghani, P.C., Stone, C.L., Ray, B.D., Pindel, E.V., Hurley, T.D. and Bosron, W.F.
    Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase.
    Biochemistry 39: 10720-10729 (2000). [PMID: 10978156]
  5. Van Ophem, P.W. and Duine, J.A.
    NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase.
    FEMS Microbiol. Lett. 116: 87-94 (1994).
  6. Ras, J., Van Ophem, P.W., Reijnders, W.N.M., Van Spanning, R.J.M., Duine, J.A., Stouthamer, A.H. and Harms, N.
    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: 247-251 (1995). [PMID: 7798140]
  7. Barber, R.D., Rott, M.A. and Donohue, T.J.
    Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides.
    J Bacteriol 178: 1386-1393 (1996). [PMID: 8631716]

[EC 1.1.1.284 created 2005 (EC 1.2.1.1 created 1961, modified 1982, modified 2002, part-transferred 2005 to EC 1.1.1.284)]