Thiamine-triphosphatase: Difference between revisions
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{{enzyme |
{{infobox enzyme |
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| Name = thiamin triphosphatase |
| Name = thiamin triphosphatase |
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| EC_number = 3.6.1.28 |
| EC_number = 3.6.1.28 |
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| CAS_number = 9068-47-7 |
| CAS_number = 9068-47-7 |
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| GO_code = 0050333 |
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| IUBMB_EC_number = 3/6/1/28 |
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{{protein |
{{infobox protein |
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|Name=thiamine triphosphatase |
|Name=thiamine triphosphatase |
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|LocusSupplementaryData= |
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'''Thiamine |
'''Thiamine-triphosphatase''' is an [[enzyme]] involved in [[thiamine metabolism]]. It [[catalysis|catalyzes]] the [[chemical reaction]] |
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:thiamine triphosphate + H<sub>2</sub>O <math>\rightleftharpoons</math> thiamine diphosphate + phosphate |
:[[thiamine triphosphate]] + H<sub>2</sub>O <math>\rightleftharpoons</math> [[thiamine diphosphate]] + [[phosphate]] |
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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[thiamine triphosphate]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[thiamine diphosphate]] and [[phosphate]]. |
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==Structural studies== |
==Structural studies== |
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As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|2JMU}}. |
As of late 2007, only one [[tertiary structure|structure]] has been solved for this class of enzymes, with the [[Protein Data Bank|PDB]] accession code {{PDB link|2JMU}}. |
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==See also== |
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* [[Thiamine-diphosphate kinase]] |
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==References== |
==References== |
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{{ |
{{Reflist}} |
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* {{cite journal | |
* {{cite journal |vauthors=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 | issue = 7 | doi = 10.1016/S0021-9258(19)45498-7 | doi-access = free }} |
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{{Acid anhydride hydrolases}} |
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{{Enzymes}} |
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{{Portal bar|Biology|border=no}} |
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[[Category:EC 3.6.1]] |
[[Category:EC 3.6.1]] |
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[[Category:Enzymes of known structure]] |
[[Category:Enzymes of known structure]] |
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Latest revision as of 16:01, 26 August 2023
| thiamin triphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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.
