EC number:1.8.1.12
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.8 Acting on a sulfur group of donors |
| 1.8.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.8.1.12 | ||
|---|---|---|---|
| Description: | Trypanothione-disulfide reductase. | ||
| Alternative Name: |
Trypanothione reductase. NADPH:trypanothione oxidoreductase. N(1),N(8)-bis(glutathionyl)spermidine reductase. | ||
| Prosite: | PDOC00073; | ||
| PDB: |
|
||
| Cath: | 3.30.390.30; 3.50.50.60; |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 1.8.1.12 |
| BRENDA Enzyme Link: | BRENDA 1.8.1.12 |
| KEGG Enzyme Link: | KEGG1.8.1.12 |
| BioCyc Enzyme Link: | BioCyc 1.8.1.12 |
| ExPASy Enzyme Link: | ExPASy1.8.1.12 |
| EC2PDB Enzyme Link: | EC2PDB 1.8.1.12 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.8.1.12 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.8.1.12 |
| IntEnz Enzyme Link: | IntEnz 1.8.1.12 |
| MEDLINE Enzyme Link: | MEDLINE 1.8.1.12 |
| RHEA:16757 | NADP(+) + trypanothione = H(+) + NADPH + trypanothione disulfide |
| RULE(radius=1) | ([*:1]-[SH;+0:2].[*:3]-[SH;+0:4]).[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1.[*:1]-[S;H0;+0:2]-[S;H0;+0:4]-[*:3] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies. | Gallwitz H, Bonse S, Martinez-Cruz A, Schlichting I, Schumacher K, Krauth-Siegel RL | 1999 Feb 11 | 9986706 |
| The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution. | Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN | 1996 Jan | 8771196 |
| Catalytic and potentiometric characterization of E201D and E201Q mutants of Trypanosoma congolense trypanothione reductase. | Zheng R, Cenas N, Blanchard JS | 1995 Oct 3 | 7548022 |
| Structure of trypanothione reductase from Crithidia fasciculata at 2.6 A resolution; enzyme-NADP interactions at 2.8 A resolution. | Bailey S, Fairlamb AH, Hunter WN | 1994 Mar 1 | 15299452 |