EC number:3.6.1.28
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.6 Acting on acid anhydrides |
| 3.6.1 In phosphorus-containing anhydrides |
| ID: | 3.6.1.28 |
|---|---|
| Description: | Thiamine-triphosphatase. |
| Alternative Name: |
ThTPase. |
| Cath: | 2.40.320.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.6.1.28 |
| BRENDA Enzyme Link: | BRENDA 3.6.1.28 |
| KEGG Enzyme Link: | KEGG3.6.1.28 |
| BioCyc Enzyme Link: | BioCyc 3.6.1.28 |
| ExPASy Enzyme Link: | ExPASy3.6.1.28 |
| EC2PDB Enzyme Link: | EC2PDB 3.6.1.28 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.6.1.28 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.6.1.28 |
| IntEnz Enzyme Link: | IntEnz 3.6.1.28 |
| MEDLINE Enzyme Link: | MEDLINE 3.6.1.28 |
| RHEA:11744 | H2O + thiamine triphosphate = H(+) + phosphate + thiamine diphosphate |
| 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 | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase. | Delvaux D, Kerff F, Murty MR, Lakaye B, Czerniecki J, Kohn G, Wins P, Herman R, Gabelica V, Heuze F, Tordoir X, Marée R, Matagne A, Charlier P, De Pauw E, Bettendorff L | 2013 Oct | 23707715 |
| Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase. | Song J, Bettendorff L, Tonelli M, Markley JL | 2008 Apr 18 | 18276586 |