Thiamine-triphosphatase
Appearance
(Redirected from ThTPase)
thiamin triphosphatase | |||||||||
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Identifiers | |||||||||
EC no. | 3.6.1.28 | ||||||||
CAS no. | 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 | ||||||||
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thiamine triphosphatase | |||||||
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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 | ||||||
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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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2JMU.
See also
[edit]References
[edit]- Hashitani Y, Cooper JR (1972). "The partial purification of thiamine triphosphatase from rat brain". J. Biol. Chem. 247 (7): 2117–9. doi:10.1016/S0021-9258(19)45498-7. PMID 4335862.