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{{Short description|InterPro Family}} |
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{{enzyme |
{{infobox enzyme |
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| Name = adenine deaminase |
| Name = adenine deaminase |
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| EC_number = 3.5.4.2 |
| EC_number = 3.5.4.2 |
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| CAS_number = 9027-68-3 |
| CAS_number = 9027-68-3 |
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| GO_code = 0000034 |
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| IUBMB_EC_number = 3/5/4/2 |
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| image = 2ics.jpg |
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| width = 270 |
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| caption = adenine deaminase monomer, Enterococcus |
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In [[enzymology]], an '''adenine deaminase''' ({{EC number|3.5.4.2}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
In [[enzymology]], an '''adenine deaminase''' ({{EC number|3.5.4.2}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
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Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenine]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[hypoxanthine]] and [[ammonia|NH<sub>3</sub>]]. |
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenine]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[hypoxanthine]] and [[ammonia|NH<sub>3</sub>]]. |
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This enzyme belongs to the family of [[hydrolase]]s, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is '''adenine aminohydrolase'''. Other names in common use include '''adenase''', '''adenine aminase''', and '''ADase'''. This enzyme participates in [[purine metabolism]]. |
This enzyme belongs to the family of [[hydrolase]]s, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The [[List of enzymes|systematic name]] of this enzyme class is '''adenine aminohydrolase'''. Other names in common use include '''adenase''', '''adenine aminase''', and '''ADase'''. This enzyme participates in [[purine metabolism]]. |
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==Structural studies== |
==Structural studies== |
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==References== |
==References== |
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{{reflist|1}} |
{{reflist|1}} |
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* {{cite journal | |
* {{cite journal |vauthors=Blauch M, Koch FC, Hane ME | date = 1939 | title = A study of xanthine oxidase of rat blood | journal = J. Biol. Chem. | volume = 130 | pages = 471–486 }} |
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* {{cite journal | |
* {{cite journal |vauthors=Heppel LA, Hurwitz J, Horecker BL | date = 1957 | title = Adenine deaminase of Azotobacter vinelandii | journal = J. Am. Chem. Soc. | volume = 79 | pages = 630–633 | doi = 10.1021/ja01560a033 | issue = 3 }} |
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{{Carbon-nitrogen non-peptide hydrolases}} |
{{Carbon-nitrogen non-peptide hydrolases}} |
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{{Enzymes}} |
{{Enzymes}} |
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[[Category:EC 3.5.4]] |
[[Category:EC 3.5.4]] |
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[[Category:Enzymes of known structure]] |
[[Category:Enzymes of known structure]] |
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adenine deaminase | |||||||||
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adenine deaminase monomer, Enterococcus
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Identifiers | |||||||||
EC no. | 3.5.4.2 | ||||||||
CAS no. | 9027-68-3 | ||||||||
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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Inenzymology, an adenine deaminase (EC 3.5.4.2) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are adenine and H2O, whereas its two products are hypoxanthine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is adenine aminohydrolase. Other names in common use include adenase, adenine aminase, and ADase. This enzyme participates in purine metabolism.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2ICS.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
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3.5.1: Linear amides / Amidohydrolases |
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3.5.2: Cyclic amides/ Amidohydrolases |
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3.5.3: Linear amidines/ Ureohydrolases |
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3.5.4: Cyclic amidines/ Aminohydrolases |
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3.5.5: Nitriles/ Aminohydrolases |
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3.5.99: Other |
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Activity |
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Regulation |
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Classification |
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Kinetics |
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Types |
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This EC 3.5 enzyme-related article is a stub. You can help Wikipedia by expanding it. |