From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins
thiamine triphosphatase
Identifiers
SymbolTHTPA
NCBI gene 79178
HGNC 18987
RefSeq NM_024328
UniProt Q9BU02
Other data
EC number 3.6.1.28
Locus Chr. 14 q11.2
Search for
Structures Swiss-model
Domains InterPro

Thiamine-triphosphatase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction

thiamine triphosphate + H2O thiamine diphosphate + phosphate

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.

See also

References

  • 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.


From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins
thiamine triphosphatase
Identifiers
SymbolTHTPA
NCBI gene 79178
HGNC 18987
RefSeq NM_024328
UniProt Q9BU02
Other data
EC number 3.6.1.28
Locus Chr. 14 q11.2
Search for
Structures Swiss-model
Domains InterPro

Thiamine-triphosphatase is an enzyme involved in thiamine metabolism. It catalyzes the chemical reaction

thiamine triphosphate + H2O thiamine diphosphate + phosphate

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.

See also

References

  • 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.



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