Enzyme

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     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.284
Description:S-(hydroxymethyl)glutathione dehydrogenase.
Alternative Name: NAD-linked formaldehyde dehydrogenase.
NAD-dependent formaldehyde dehydrogenase.
NAD- and glutathione-dependent formaldehyde dehydrogenase.
GS-FDH.
Glutathione-dependent formaldehyde dehydrogenase.
GD-FALDH.
Formic dehydrogenase.
Formaldehyde dehydrogenase (glutathione).
Formaldehyde dehydrogenase.
FDH.
Class III alcohol dehydrogenase.
Chi-ADH.
ADH3.
Prosite: PDOC00058;
PDB:
PDBScop
Cath: 3.40.50.720; 3.90.1590.10; 3.90.180.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.284
BRENDA Enzyme Link: BRENDA 1.1.1.284
KEGG Enzyme Link: KEGG1.1.1.284
BioCyc Enzyme Link: BioCyc 1.1.1.284
ExPASy Enzyme Link: ExPASy1.1.1.284
EC2PDB Enzyme Link: EC2PDB 1.1.1.284
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.284
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.284
IntEnz Enzyme Link: IntEnz 1.1.1.284
MEDLINE Enzyme Link: MEDLINE 1.1.1.284
MSA:

1.1.1.284;

Phylogenetic Tree:

1.1.1.284;

Uniprot:
M-CSA:
RHEA:19985 NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-formylglutathione
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]-[n+;H0:5]1:[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:1>>[*:1]-[CH;+0:2]=[O;H0;+0:3].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-[C;H0;+0:9](-[*:10])=[CH;+0:11]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides.Barber RD, Rott MA, Donohue TJ1996 Mar8631716
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.Ras J, Van Ophem PW, Reijnders WN, Van Spanning RJ, Duine JA, Stouthamer AH, Harms N1995 Jan7798140
A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans.Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS2001 Mar 2211260719
Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase.Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF2000 Sep 510978156

RHEA:19981 NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]-[n+;H0:5]1:[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:1>>[*:1]-[CH;+0:2]=[O;H0;+0:3].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-[C;H0;+0:9](-[*:10])=[CH;+0:11]-1
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides.Barber RD, Rott MA, Donohue TJ1996 Mar8631716
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.Ras J, Van Ophem PW, Reijnders WN, Van Spanning RJ, Duine JA, Stouthamer AH, Harms N1995 Jan7798140
A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans.Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS2001 Mar 2211260719
Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase.Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF2000 Sep 510978156