EC number:1.7.1.7
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.7 Acting on other nitrogenous compounds as donors |
| 1.7.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.7.1.7 | ||
|---|---|---|---|
| Description: | GMP reductase. | ||
| Alternative Name: |
NADPH:guanosine-5'-phosphate oxidoreductase (deaminating). NADPH:GMP oxidoreductase (deaminating). Guanylate reductase. Guanosine monophosphate reductase. Guanosine 5'-phosphate reductase. Guanosine 5'-monophosphate reductase. Guanosine 5'-monophosphate oxidoreductase. | ||
| Prosite: | PDOC00391; | ||
| PDB: |
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| Cath: | 3.20.20.70; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.7.1.7 |
| BRENDA Enzyme Link: | BRENDA 1.7.1.7 |
| KEGG Enzyme Link: | KEGG1.7.1.7 |
| BioCyc Enzyme Link: | BioCyc 1.7.1.7 |
| ExPASy Enzyme Link: | ExPASy1.7.1.7 |
| EC2PDB Enzyme Link: | EC2PDB 1.7.1.7 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.7.1.7 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.7.1.7 |
| IntEnz Enzyme Link: | IntEnz 1.7.1.7 |
| MEDLINE Enzyme Link: | MEDLINE 1.7.1.7 |
| RHEA:17185 | IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH |
| RULE(radius=1) | [*:1]-[n+;H0:2]1:[cH;+0:3]:[cH;+0:4]:[cH;+0:5]:[c;H0;+0:6](-[*:7]):[cH;+0:8]:1.[*:9]:[cH;+0:10]:[*:11].[NH3;+0:12]>>[*:1]-[N;H0;+0:2]1-[CH;+0:3]=[CH;+0:4]-[CH2;+0:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-1.[*:9]:[c;H0;+0:10](:[*:11])-[NH2;+0:12] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Guanosine 5'-monophosphate reductase from Leishmania donovani. A possible chemotherapeutic target. | Spector T, Jones TE | 1982 Dec 1 | 7159467 |
| Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-Resolution <sup>31</sup>P Field-Cycling NMR Relaxometry. | Rosenberg MM, Redfield AG, Roberts MF, Hedstrom L | 2018 Jun 5 | 29547266 |
| Substrate and Cofactor Dynamics on Guanosine Monophosphate Reductase Probed by High Resolution Field Cycling 31P NMR Relaxometry. | Rosenberg MM, Redfield AG, Roberts MF, Hedstrom L | 2016 Oct 28 | 27613871 |
| Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes. | Patton GC, Stenmark P, Gollapalli DR, Sevastik R, Kursula P, Flodin S, Schuler H, Swales CT, Eklund H, Himo F, Nordlund P, Hedstrom L | 2011 Oct 30 | 22037469 |
| Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP. | Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y | 2006 Feb 3 | 16359702 |
| NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. | Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y | 2002 Sep | 12009299 |