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{{infobox enzyme
In [[enzymology]], a '''thiamine-triphosphatase''' ({{EC number|3.6.1.28}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
| Name = thiamin triphosphatase
| EC_number = 3.6.1.28
| CAS_number = 9068-47-7
| GO_code = 0050333
| image =
| width =
| caption =
}}
{{infobox protein
|Name=thiamine triphosphatase
|caption=
|image=
|width=
|HGNCid=18987
|Symbol=THTPA
|AltSymbols=
|EntrezGene=79178
|OMIM=
|RefSeq=NM_024328
|UniProt=Q9BU02
|PDB=
|ECnumber=3.6.1.28
|Chromosome=14
|Arm=q
|Band=11.2
|LocusSupplementaryData=
}}
'''Thiamine-triphosphatase''' is an [[enzyme]] involved in [[thiamine metabolism]]. It [[catalysis|catalyzes]] the [[chemical reaction]]


: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]]


This enzyme belongs to the family of [[acid anhydride hydrolase]]s, specifically those acting on phosphorus-containing anhydrides. Its [[List of enzymes|systematic name]] is thiamine triphosphate phosphohydrolase.
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]].

This enzyme belongs to the family of [[hydrolase]]s, 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==
==Structural studies==


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}}.

==See also==
* [[Thiamine-diphosphate kinase]]


==References==
==References==
{{reflist|1}}
{{Reflist}}
* {{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&ndash;9 | pmid = 4335862 | issue = 7 | doi = 10.1016/S0021-9258(19)45498-7 | doi-access = free }}
{{Enzyme references|EC_number=3.6.1.28|IUBMB_EC_number=3/6/1/28}}
* {{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&ndash;9 | pmid = 4335862 }}


{{Acid anhydride hydrolases}}
==External links==
{{Enzymes}}
::''The [[CAS registry number]] for this enzyme class is {{CAS registry|9068-47-7}}.''
{{Portal bar|Biology|border=no}}
{{Enzyme links|EC_number=3.6.1.28|IUBMB_EC_number=3/6/1/28}}

===Gene Ontology (GO) codes===
{{GO code links | GO_code=0050333 | name=thiamin-triphosphatase}}

{{hydrolase-stub}}


[[Category:EC 3.6.1]]
[[Category:EC 3.6.1]]
[[Category:Enzymes of known structure]]
[[Category:Enzymes of known structure]]


{{3.6-enzyme-stub}}

Latest revision as of 16:01, 26 August 2023

thiamin triphosphatase
Identifiers
EC no.3.6.1.28
CAS no.9068-47-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
thiamine triphosphatase
Identifiers
SymbolTHTPA
NCBI gene79178
HGNC18987
RefSeqNM_024328
UniProtQ9BU02
Other data
EC number3.6.1.28
LocusChr. 14 q11.2
Search for
StructuresSwiss-model
DomainsInterPro

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

[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.