| EC Tree |
| 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: |
|
||
| Cath: | 3.40.50.720; 3.90.1590.10; 3.90.180.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| 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: | |
|---|---|
| Phylogenetic Tree: | |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. | Barber RD, Rott MA, Donohue TJ | 1996 Mar | 8631716 |
| 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 N | 1995 Jan | 7798140 |
| A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. | Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS | 2001 Mar 22 | 11260719 |
| Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. | Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF | 2000 Sep 5 | 10978156 |
| 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 |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. | Barber RD, Rott MA, Donohue TJ | 1996 Mar | 8631716 |
| 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 N | 1995 Jan | 7798140 |
| A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. | Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS | 2001 Mar 22 | 11260719 |
| Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. | Sanghani PC, Stone CL, Ray BD, Pindel EV, Hurley TD, Bosron WF | 2000 Sep 5 | 10978156 |