[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/2015\/02\/25\/adenosine-phosphate-deaminase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/2015\/02\/25\/adenosine-phosphate-deaminase-wikipedia\/","headline":"Adenosine-phosphate deaminase – Wikipedia","name":"Adenosine-phosphate deaminase – Wikipedia","description":"From Wikipedia, the free encyclopedia In enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction","datePublished":"2015-02-25","dateModified":"2015-02-25","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","url":"https:\/\/wikimedia.org\/api\/rest_v1\/media\/math\/render\/svg\/1c37b981df851b9e54e489e017b1481e37d418f3","height":"","width":""},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/2015\/02\/25\/adenosine-phosphate-deaminase-wikipedia\/","about":["Wiki"],"wordCount":3098,"articleBody":"From Wikipedia, the free encyclopediaIn enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction5′-AMP + H2O \u21cc{displaystyle rightleftharpoons } 5′-IMP + NH3Thus, the two substrates of this enzyme are 5′-AMP and H2O, whereas its two products are 5′-IMP and NH3.Table of ContentsClassification[edit]Reaction mechanism[edit]Species distribution[edit]Function[edit]Crystal Structure[edit]Active Site[edit]References[edit]Further reading[edit]Classification[edit]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 adenosine-phosphate aminohydrolase. Other names in common use include adenylate deaminase, adenine nucleotide deaminase, and adenosine (phosphate) deaminase.The EC number for adenosine-phosphate deaminase is [EC 3.5.4.17].[1] The class is (EC 3) for hydrolase. Hydrolases are enzymes that catalyze bond cleavage by reaction with water.[2] The sub-class refers to adenosine-phosphate deaminase acting on carbon-nitrogen bonds, other than peptide bonds. The sub-sub-class refers to the type of substrate the enzyme is binding to, in this case, cyclic amidines. The final number (17) indicates that adenosine-phosphate deaminase binds to 5′-adenosine monophosphate.[3][4]Reaction mechanism[edit]The pathway for adenosine-phosphate deaminase involves two substrates, 5′-adenosine monophosphate and water. This pathway is referred to as amidine hydrolysis. Adenosine-phosphate deaminase binds to 5′-AMP using water to break the C-N bond and replacing it with a carbonyl group. Ultimately, this produces 5′-IMP (Inosine monophosphate) and NH3 (ammonia). Substrate specificities of this class depend on their origin, however, all of them deaminate adenosine, 2′-deoxyadenosine, 5′-AMP, and 3′,5′-cyclic AMP. Inhibitors of adenosine-phosphate deaminase include Mn2+ (neutral or alkaline pH), F\u2212, Fe3+, CN\u2212, Co2+, Zn2+, and Hg2+.[1][5]Species distribution[edit]Adenosine-phosphate deaminase is found in most, if not all organisms in all tissues, however, muscle tissue is the richest source.[6] The basic pathway of adenosine-phosphate deaminase is to replace a C-N bond of a 5′-AMP to replace the carboxyl group forming 5′-IMP. 5′-IMP is then catalyzed by Inosine-5′-monophosphate dehydrogenase (IMPDH) in guanine nucleotide biosynthesis. This is at the center of cell growth and proliferation.[7] Specifically within marine mollusks, studies suggest that adenosine-phosphate deaminases are widely distributed across the phylum.[1] However, it was noticed that the pathways varied within each individual species, suggesting that different substrates are preferred within different species.[1] The source organisms for this enzyme are Porphyra crispata, Desulfovibrio desulfuricans, Aspergillus sp..[5]Function[edit]Within the cell, adenosine-phosphate deaminase is found within all tissues, but particularly higher in concentration within muscle tissue.[6] Kinetic properties of the enzyme vary widely based on the source and purification of the enzyme.[6] Adenosine-phosphate deaminase binds to 5′-AMP performing hydrolysis, using water to break the C-N bond of the amino group attached to 5′-AMP. This results in binding 5′-IMP is then catalyzed by Inosine-5′-monophosphate dehydrogenase (IMPDH), facilitating guanine nucleotide biosynthesis.[7] The initial step of AMP degradation is the conversion to xanthine into alternative routes, xanthosine or hypoxanthine.[8]Crystal Structure[edit]Molecular weight of adenosine-phosphate deaminase is 30000-60000 Da[5] or 15223 Da.[9] The number of amino acid sequences is 135. There are 0 transmembrane helices.[9]Active Site[edit]The turnover number for adenosine-phosphate deaminase is 690 ATP, 630 ADP, and 710 AMP. The km value is 0.047 for 5′-AMP. the pH optimum is 6.0-6.8 for 5′-AMP, however the pH range is 4-8 with a temperature optimum of 55\u00a0\u00b0C.[5] Natural substrates for this enzyme are 5′-AMP and H2O. The substrate spectrum is as follows:[5]Adenosine + H2OAdenosine phosphates + H2ONAD+ +  H2OdATP +  H2OdADP +  H2OdAMP +  H2ODeoxyadenosine +  H2OThe product spectrum is as follows:[5]Inosine + NH3Inosine phosphates + NH3Nicotinamide-hypoxanthine-dinucleotide + NH3dITP + NH3dIDP + NH3dIMP + NH3Deoxyinosine + NH3References[edit]^ a b c d Uchida H, Narita Y, Masuda A, Matsui Y, Chen YX, Takahashi I, Maeda S, Nomura A (January 1995). “Purification and Some Properties of Adenosine (Phosphate) Deaminase from the Liver of the Squid Todarodes pacificus”. Bioscience, Biotechnology, and Biochemistry. 59 (7): 1276\u20131280. doi:10.1271\/bbb.59.1276. ISSN\u00a00916-8451.^ Bornscheuer UT, Kazlauskas RJ (2006). Hydrolases in Organic Synthesis: Regio- and Stereoselective Biotransformatics (2nd\u00a0ed.). Wiley-Blackwell. p.\u00a01. ISBN\u00a0978-3-527-60712-9.^ “EC 3.5.4”. iubmb.qmul.ac.uk. Retrieved 2022-10-21.^ “EC 3.5.4.17”. iubmb.qmul.ac.uk. Retrieved 2022-10-21.^ a b c d e f Schomburg D, Salzmann M (1991). Enzyme Handbook 4. Springer. pp.\u00a01059\u20131062. ISBN\u00a0978-3-642-84437-9.^ a b c Smiley KL, Suelter CH (April 1967). “Univalent cations as allosteric activators of muscle adenosine 5′-phosphate deaminase”. The Journal of Biological Chemistry. 242 (8): 1980\u20131981. doi:10.1016\/S0021-9258(18)96097-7. PMID\u00a06024785.^ a b Fotie J (2018-04-16). “Inosine 5′-Monophosphate Dehydrogenase (IMPDH) as a Potential Target for the Development of a New Generation of Antiprotozoan Agents”. Mini Reviews in Medicinal Chemistry. 18 (8): 656\u2013671. doi:10.2174\/1389557516666160620065558. PMID\u00a027334467.^ “MetaCyc Reaction: 3.5.4.6\/3.5.4.17”. Biocyc.org. 1 March 2012.^ a b “Information on EC 3.5.4.17 – adenosine-phosphate deaminase – BRENDA Enzyme Database”. www.brenda-enzymes.org. Retrieved 2022-10-21.Further reading[edit]Su JC, Li CC, Ting CC (February 1966). “A new adenylate deaminase from red marine alga Porphyra crispata”. Biochemistry. 5 (2): 536\u2013543. doi:10.1021\/bi00866a020. PMID\u00a05940938.Yates MG (February 1969). “A non-specific adenine nucleotide deaminase from desulfovibrio desulfuricans”. Biochimica et Biophysica Acta (BBA) – Enzymology. 171 (2): 299\u2013310. doi:10.1016\/0005-2744(69)90163-6. PMID\u00a05773435.  "},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/2015\/02\/25\/adenosine-phosphate-deaminase-wikipedia\/#breadcrumbitem","name":"Adenosine-phosphate deaminase – Wikipedia"}}]}]