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(Top)
 


1 Structural studies  





2 References  














Adenine deaminase: Difference between revisions







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{{Short description|InterPro Family}}

{{enzyme

{{infobox enzyme

| Name = adenine deaminase

| Name = adenine deaminase

| EC_number = 3.5.4.2

| EC_number = 3.5.4.2

| CAS_number = 9027-68-3

| CAS_number = 9027-68-3

| GO_code = 0000034

| IUBMB_EC_number = 3/5/4/2

| GO_code = 0000034

| image = 2ics.jpg

| image =

| width = 270

| caption = adenine deaminase monomer, Enterococcus

| width =

| caption =

}}

}}

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]]

Line 15: Line 15:

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>]].



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]].



==Structural studies==

==Structural studies==

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==References==

==References==

{{reflist|1}}

{{reflist|1}}

* {{cite journal | author = Blauch M, Koch FC and Hane ME | date = 1939 | title = A study of xanthine oxidase of rat blood | journal = J. Biol. Chem. | volume = 130 | pages = 471&ndash;486 }}

* {{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&ndash;486 }}

* {{cite journal | author = Heppel LA, Hurwitz J and Horecker BL | date = 1957 | title = Adenine deaminase of Azotobacter vinelandii | journal = J. Am. Chem. Soc. | volume = 79 | pages = 630&ndash;633 | doi = 10.1021/ja01560a033 | issue = 3 }}

* {{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&ndash;633 | doi = 10.1021/ja01560a033 | issue = 3 }}



{{Carbon-nitrogen non-peptide hydrolases}}

{{Carbon-nitrogen non-peptide hydrolases}}

{{Enzymes}}

{{Enzymes}}

{{Portal bar|Molecular and Cellular Biology|border=no}}

{{Portal bar|Biology|border=no}}


{{hydrolase-stub}}



[[Category:EC 3.5.4]]

[[Category:EC 3.5.4]]

[[Category:Enzymes of known structure]]

[[Category:Enzymes of known structure]]



{{3.5-enzyme-stub}}


Latest revision as of 12:58, 26 August 2023

adenine deaminase
adenine deaminase monomer, Enterococcus
Identifiers
EC no.3.5.4.2
CAS no.9027-68-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Inenzymology, an adenine deaminase (EC 3.5.4.2) is an enzyme that catalyzes the chemical reaction

adenine + H2O hypoxanthine + NH3

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.

Structural studies[edit]

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2ICS.

References[edit]


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    This page was last edited on 26 August 2023, at 12:58 (UTC).

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