Thiamine-triphosphatase: Difference between revisions
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{{Acid anhydride hydrolases}} |
{{Acid anhydride hydrolases}} |
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{{hydrolase-stub}} |
{{hydrolase-stub}} |
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Revision as of 19:46, 22 January 2016
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
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2JMU.