S-(hydroxymethyl)glutathione dehydrogenase

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

Boyer, P.D.; Lardy, H.; Myrback, K., eds. (1963). The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 203–221.
Rose ZB, Racker E (1966). "Formaldehyde dehydrogenase". Methods Enzymol. 9: 357–360. doi:10.1016/0076-6879(66)09073-6.
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. doi:10.1038/35068596. PMID 11260719.
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. 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. PMC 177813. PMID 8631716.

Oxidoreductases: alcohol oxidoreductases (EC 1.1)

1.1.1: NAD/NADP acceptor	3-hydroxyacyl-CoA dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase Alcohol dehydrogenase Aldo-keto reductase 1A1 1B1 1B10 1C1 1C3 1C4 7A2 Aldose reductase Beta-Ketoacyl ACP reductase Carbohydrate dehydrogenases Carnitine dehydrogenase D-malate dehydrogenase (decarboxylating) DXP reductoisomerase Glucose-6-phosphate dehydrogenase Glycerol-3-phosphate dehydrogenase HMG-CoA reductase IMP dehydrogenase Isocitrate dehydrogenase Lactate dehydrogenase L-threonine dehydrogenase L-xylulose reductase Malate dehydrogenase Malate dehydrogenase (decarboxylating) Malate dehydrogenase (NADP+) Malate dehydrogenase (oxaloacetate-decarboxylating) Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) Phosphogluconate dehydrogenase Sorbitol dehydrogenase Hydroxysteroid dehydrogenase: 3 Beta 3-beta-HSD NSDHL 11 Beta HSD11B1 HSD11B2 17 Beta

1.1.2: cytochrome acceptor	D-lactate dehydrogenase (cytochrome) D-lactate dehydrogenase (cytochrome c-553) Mannitol dehydrogenase (cytochrome)

1.1.3: oxygen acceptor	Glucose oxidase L-gulonolactone oxidase Xanthine oxidase

1.1.4: disulfide as acceptor	Vitamin K epoxide reductase Vitamin-K-epoxide reductase (warfarin-insensitive)

1.1.5: quinone/similar acceptor	Malate dehydrogenase (quinone) Quinoprotein glucose dehydrogenase

1.1.99: other acceptors	Choline dehydrogenase L2HGDH

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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