Thiamine-triphosphatase
Thiamine-triphosphatase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction
- thiamine triphosphate + H2O thiamine diphosphate + phosphate
| thiamin triphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.1.28 | ||||||||
| CAS number | 9068-47-7 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
| thiamine triphosphatase | |
|---|---|
| Identifiers | |
| Symbol | THTPA |
| NCBI gene | 79178 |
| HGNC | 18987 |
| RefSeq | NM_024328 |
| UniProt | Q9BU02 |
| Other data | |
| EC number | 3.6.1.28 |
| Locus | Chr. 14 q11.2 |
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.
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See also
References
- Hashitani Y, Cooper JR (1972). "The partial purification of thiamine triphosphatase from rat brain". J. Biol. Chem. 247 (7): 2117–9. PMID 4335862.
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