EC number:3.1.4.35
| ID: | 3.1.4.35 | ||
|---|---|---|---|
| Description: | 3',5'-cyclic-GMP phosphodiesterase. | ||
| Prosite: | PDOC00116; | ||
| PDB: |
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| Cath: | 1.10.1300.10; 3.30.450.40; 3.30.750.180; 3.60.21.10; 3.60.21.40; 4.10.1120.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.4.35 |
| BRENDA Enzyme Link: | BRENDA 3.1.4.35 |
| KEGG Enzyme Link: | KEGG3.1.4.35 |
| BioCyc Enzyme Link: | BioCyc 3.1.4.35 |
| ExPASy Enzyme Link: | ExPASy3.1.4.35 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.4.35 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.4.35 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.4.35 |
| IntEnz Enzyme Link: | IntEnz 3.1.4.35 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.4.35 |
| RHEA:16957 | 3',5'-cyclic GMP + H2O = GMP + H(+) |
| RULE(radius=1) | [*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[O;H0;+0:5]-[*:6].[OH2;+0:7]>>([*:6]-[OH;+0:5].[*:1]-[P;H0;+0:2](=[*:3])(-[*:4])-[OH;+0:7]) |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural basis for the catalytic mechanism of human phosphodiesterase 9. | Liu S, Mansour MN, Dillman KS, Perez JR, Danley DE, Aeed PA, Simons SP, Lemotte PK, Menniti FS | 2008 Sep 9 | 18757755 |
| Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by prenylation and interaction with a prenyl-binding protein. | Day JP, Cleghon V, Houslay MD, Davies SA | 2008 Sep 15 | 18503409 |
| A novel role for a Drosophila homologue of cGMP-specific phosphodiesterase in the active transport of cGMP. | Day JP, Houslay MD, Davies SA | 2006 Jan 15 | 16232123 |
| Identification and characterization of two unusual cGMP-stimulated phoshodiesterases in dictyostelium. | Bosgraaf L, Russcher H, Snippe H, Bader S, Wind J, Van Haastert PJ | 2002 Nov | 12429832 |