Thiamine-triphosphatase
From Infogalactic: the planetary knowledge core
| thiamin triphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.1.28 | ||||||||
| CAS number | Template:CAS | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
|
|||||||||
| thiamine triphosphatase | |
|---|---|
| Identifiers | |
| Symbol | THTPA |
| Entrez | 79178 |
| HUGO | 18987 |
| RefSeq | NM_024328 |
| UniProt | Q9BU02 |
| Other data | |
| EC number | 3.6.1.28 |
| Locus | Chr. 14 q11.2 |
Thiamine-triphosphatase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction
This enzyme belongs to the family of acid anhydride hydrolases, specifically those acting on phosphorus-containing anhydrides. Its systematic name is thiamine triphosphate phosphohydrolase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2JMU.
See also
References
- Lua error in package.lua at line 80: module 'strict' not found.
<templatestyles src="Asbox/styles.css"></templatestyles>
 |
This hydrolase article is a stub. You can help Wikipedia by expanding it. |
