ATP diphosphatase: Difference between revisions
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{{Short description|Class of enzymes}} |
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{{infobox enzyme |
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| Name = ATP diphosphatase |
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| EC_number = 3.6.1.8 |
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| CAS_number = 37289-25-1 |
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| GO_code = 0047693 |
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}} |
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In [[enzymology]], an '''ATP diphosphatase''' ({{EC number|3.6.1.8}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
In [[enzymology]], an '''ATP diphosphatase''' ({{EC number|3.6.1.8}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[adenosine monophosphate|AMP]] and [[diphosphate]]. |
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[adenosine monophosphate|AMP]] and [[diphosphate]]. |
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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 '''ATP diphosphohydrolase (diphosphate-forming)'''. Other names in common use include '''ATPase''', '''ATP pyrophosphatase''', '''adenosine triphosphate pyrophosphatase''', and '''ATP diphosphohydrolase [ambiguous]'''. This enzyme participates in [[purine metabolism]] and [[pyrimidine metabolism]]. |
This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The [[List of enzymes|systematic name]] of this enzyme class is '''ATP diphosphohydrolase (diphosphate-forming)'''. Other names in common use include '''ATPase''', '''ATP pyrophosphatase''', '''adenosine triphosphate pyrophosphatase''', and '''ATP diphosphohydrolase [ambiguous]'''. This enzyme participates in [[purine metabolism]] and [[pyrimidine metabolism]]. |
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==References== |
==References== |
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{{reflist|1}} |
{{reflist|1}} |
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{{Enzyme references|EC_number=3.6.1.8|IUBMB_EC_number=3/6/1/8}} |
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* {{cite journal | |
* {{cite journal | vauthors = JOHNSON M, KAYE MA, HEMS R, KREBS HA | date = 1953 | title = Enzymic hydrolysis of adenosine phosphates by cobra venom | journal = Biochem. J. | volume = 54 | pages = 625–9 | pmid = 13058963 | issue = 4 | pmc = 1269107 }} |
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{{Acid anhydride hydrolases}} |
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==External links== |
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{{Enzymes}} |
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::''The [[CAS registry number]] for this enzyme class is {{CAS registry|37289-25-1}}.'' |
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{{Portal bar|Biology|border=no}} |
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{{Enzyme links|EC_number=3.6.1.8|IUBMB_EC_number=3/6/1/8}} |
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===Gene Ontology (GO) codes=== |
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{{GO code links | GO_code=0047693 | name=ATP diphosphatase}} |
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[[Category:EC 3.6.1]] |
[[Category:EC 3.6.1]] |
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[[Category:Enzymes of unknown structure]] |
[[Category:Enzymes of unknown structure]] |
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Latest revision as of 13:16, 26 August 2023
| ATP diphosphatase | |||||||||
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| Identifiers | |||||||||
| EC no. | 3.6.1.8 | ||||||||
| CAS no. | 37289-25-1 | ||||||||
| 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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In enzymology, an ATP diphosphatase (EC 3.6.1.8) is an enzyme that catalyzes the chemical reaction
- ATP + H2O AMP + diphosphate
Thus, the two substrates of this enzyme are ATP and H2O, whereas its two products are AMP and diphosphate.
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 ATP diphosphohydrolase (diphosphate-forming). Other names in common use include ATPase, ATP pyrophosphatase, adenosine triphosphate pyrophosphatase, and ATP diphosphohydrolase [ambiguous]. This enzyme participates in purine metabolism and pyrimidine metabolism.
References
[edit]- HEPPEL LA, HILMOE RJ (1953). "Mechanism of enzymatic hydrolysis of adenosinetriphosphate". J. Biol. Chem. 202 (1): 217–26. PMID 13061448.
- JOHNSON M, KAYE MA, HEMS R, KREBS HA (1953). "Enzymic hydrolysis of adenosine phosphates by cobra venom". Biochem. J. 54 (4): 625–9. PMC 1269107. PMID 13058963.
