Thiamine-triphosphatase: Difference between revisions
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{{enzyme |
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| Name = thiamin-triphosphatase |
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| EC_number = 3.6.1.28 |
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| CAS_number = 9068-47-7 |
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| GO_code = 0050333 |
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}} |
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{{protein |
{{protein |
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|Name=thiamine triphosphatase |
|Name=thiamine triphosphatase |
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==References== |
==References== |
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{{reflist|1}} |
{{reflist|1}} |
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{{Enzyme references|EC_number=3.6.1.28|IUBMB_EC_number=3/6/1/28}} |
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* {{cite journal | author = Hashitani Y, Cooper JR | date = 1972 | title = The partial purification of thiamine triphosphatase from rat brain | journal = J. Biol. Chem. | volume = 247 | pages = 2117–9 | pmid = 4335862 }} |
* {{cite journal | author = Hashitani Y, Cooper JR | date = 1972 | title = The partial purification of thiamine triphosphatase from rat brain | journal = J. Biol. Chem. | volume = 247 | pages = 2117–9 | pmid = 4335862 }} |
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==External links== |
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::''The [[CAS registry number]] for this enzyme class is {{CAS registry|9068-47-7}}.'' |
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===Gene Ontology (GO) codes=== |
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{{GO code links | GO_code=0050333 | name=thiamin-triphosphatase}} |
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{{hydrolase-stub}} |
{{hydrolase-stub}} |
Revision as of 18:30, 9 August 2009
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 acid anhydride hydrolase which acts upon thiamine triphosphate. In enzymology, a thiamine-triphosphatase (EC 3.6.1.28) is an enzyme that catalyzes the chemical reaction
- thiamine triphosphate + H2O thiamine diphosphate + phosphate
Thus, the two substrates of this enzyme are thiamine triphosphate and H2O, whereas its two products are thiamine diphosphate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is thiamine-triphosphate phosphohydrolase. This enzyme participates in thiamine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2JMU.