EC number:3.1.3.7
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.1 Acting on ester bonds |
| 3.1.3 Phosphoric-monoester hydrolases |
| ID: | 3.1.3.7 |
|---|---|
| Description: | 3'(2'),5'-bisphosphate nucleotidase. |
| Alternative Name: |
Phosphoadenylate 3'-nucleotidase. DPNPase. 3'-phosphoadenylylsulfate 3'-phosphatase. 3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase. |
| Cath: | 1.10.150.650; 3.20.20.140; 3.30.540.10; 3.40.190.80; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.3.7 |
| BRENDA Enzyme Link: | BRENDA 3.1.3.7 |
| KEGG Enzyme Link: | KEGG3.1.3.7 |
| BioCyc Enzyme Link: | BioCyc 3.1.3.7 |
| ExPASy Enzyme Link: | ExPASy3.1.3.7 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.3.7 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.3.7 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.3.7 |
| IntEnz Enzyme Link: | IntEnz 3.1.3.7 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.3.7 |
| RHEA:10040 | adenosine 3',5'-bisphosphate + H2O = AMP + phosphate |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A role for a lithium-inhibited Golgi nucleotidase in skeletal development and sulfation. | Frederick JP, Tafari AT, Wu SM, Megosh LC, Chiou ST, Irving RP, York JD | 2008 Aug 19 | 18695242 |
| Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase. | Hatzios SK, Iavarone AT, Bertozzi CR | 2008 May 27 | 18454554 |
| YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity. | Mechold U, Fang G, Ngo S, Ogryzko V, Danchin A | 2007 | 17586819 |
| Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate. | Spiegelberg BD, Xiong JP, Smith JJ, Gu RF, York JD | 1999 May 7 | 10224133 |