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<p>建立内容为“{{PBB|geneid=100}} {{Infobox protein family | Symbol = A_deaminase | Name = Adenosine/AMP deaminase | image = PDB 2amx EBI.jpg | width = | caption = crystal stru…”的新页面</p> <p><b>新页面</b></p><div>{{PBB|geneid=100}}<br /> {{Infobox protein family<br /> | Symbol = A_deaminase<br /> | Name = Adenosine/AMP deaminase<br /> | image = PDB 2amx EBI.jpg<br /> | width = <br /> | caption = crystal structure of plasmodium yoelii adenosine deaminase (py02076)<br /> | Pfam = PF00962<br /> | Pfam_clan = CL0034 <br /> | InterPro = IPR001365<br /> | SMART = <br /> | PROSITE = PDOC00419<br /> | MEROPS = <br /> | SCOP = 1add<br /> | TCDB = <br /> | OPM family = <br /> | OPM protein = <br /> | CAZy = <br /> | CDD = <br /> }}<br /> {{Infobox protein family<br /> | Symbol = A_deamin<br /> | Name = Adenosine deaminase (editase) domain<br /> | image = <br /> | width = <br /> | caption = crystal structure of the catalytic domain of an adenosine deaminase that acts on rna (hadar2) bound to inositol hexakisphosphate (ihp)<br /> | Pfam = PF02137<br /> | Pfam_clan = <br /> | InterPro = IPR002466<br /> | SMART = <br /> | PROSITE = PDOC00419<br /> | MEROPS = <br /> | SCOP = 1add<br /> | TCDB = <br /> | OPM family = <br /> | OPM protein = <br /> | CAZy = <br /> | CDD = <br /> }}<br /> {{Infobox protein family<br /> | Symbol = A_deaminase_N<br /> | Name = Adenosine/AMP deaminase N-terminal<br /> | image = <br /> | width = <br /> | caption = crystal structure of human adenosine deaminase growth factor, adenosine deaminase type 2 (ada2) complexed with transition state analogue, coformycin<br /> | Pfam = PF08451<br /> | Pfam_clan = <br /> | InterPro = IPR013659<br /> | SMART = <br /> | PROSITE = <br /> | MEROPS = <br /> | SCOP = <br /> | TCDB = <br /> | OPM family = <br /> | OPM protein = <br /> | CAZy = <br /> | CDD = <br /> }}<br /> '''腺苷脱氨酶'''（{{lang-en|Adenosine deaminase}}）的是一种参与[[嘌呤代谢]]作用的酶。它是用作拆解食物组织中的[[核酸]]中的[[腺苷]]。<br /> <br /> ==反应==<br /> <br /> 腺苷脱氨酶对腺苷进行不可逆转的[[脱氨作用]],转化腺苷为相关的[[核苷]][[肌苷]],移除[[氨基酸]]组。<br /> <br /> ==[[病理学]]==<br /> <br /> 腺苷脱氨酶的[[突变基因]]使之不容易被表达,这是一些[[免疫缺陷病]]（ SCID ）的原因。[[基因突变]]令ADA被过度产生是[[溶血性贫血]]原因之一。有一些证据表明，一个不同的allelle (ADA2)可能会导致[[自闭症]]。<br /> <br /> ==参考文献==<br /> <br /> {{Reflist|2}}<br /> <br /> ==深入阅读==<br /> <br /> {{refbegin | 2}}<br /> <br /> {{PBB_Further_reading <br /> | citations = <br /> *{{cite journal | author=da Cunha JG |title=[Adenosine deaminase. A pluridisciplinary enzyme] |journal=Acta médica portuguesa |volume=4 |issue= 6 |pages= 315–23 |year= 1992 |pmid= 1807098 |doi= }}<br /> *{{cite journal | author=Franco R, Casadó V, Ciruela F, ''et al.'' |title=Cell surface adenosine deaminase: much more than an ectoenzyme |journal=Prog. Neurobiol. |volume=52 |issue= 4 |pages= 283–94 |year= 1997 |pmid= 9247966 |doi=10.1016/S0301-0082(97)00013-0 }}<br /> *{{cite journal | author=Valenzuela A, Blanco J, Callebaut C, ''et al.'' |title=HIV-1 envelope gp120 and viral particles block adenosine deaminase binding to human CD26 |journal=Adv. Exp. Med. Biol. |volume=421 |issue= |pages= 185–92 |year= 1997 |pmid= 9330696 |doi= }}<br /> *{{cite journal | author=Moriwaki Y, Yamamoto T, Higashino K |title=Enzymes involved in purine metabolism--a review of histochemical localization and functional implications |journal=Histol. Histopathol. |volume=14 |issue= 4 |pages= 1321–40 |year= 1999 |pmid= 10506947 |doi= }}<br /> *{{cite journal | author=Hirschhorn R |title=Identification of two new missense mutations (R156C and S291L) in two ADA- SCID patients unusual for response to therapy with partial exchange transfusions |journal=Hum. Mutat. |volume=1 |issue= 2 |pages= 166–8 |year= 1993 |pmid= 1284479 |doi= 10.1002/humu.1380010214 }}<br /> *{{cite journal | author=Berkvens TM, van Ormondt H, Gerritsen EJ, ''et al.'' |title=Identical 3250-bp deletion between two AluI repeats in the ADA genes of unrelated ADA-SCID patients |journal=Genomics |volume=7 |issue= 4 |pages= 486–90 |year= 1990 |pmid= 1696926 |doi=10.1016/0888-7543(90)90190-6 }}<br /> *{{cite journal | author=Aran JM, Colomer D, Matutes E, ''et al.'' |title=Presence of adenosine deaminase on the surface of mononuclear blood cells: immunochemical localization using light and electron microscopy |journal=J. Histochem. Cytochem. |volume=39 |issue= 8 |pages= 1001–8 |year= 1991 |pmid= 1856451 |doi= }}<br /> *{{cite journal | author=Bielat K, Tritsch GL |title=Ecto-enzyme activity of human erythrocyte adenosine deaminase |journal=Mol. Cell. Biochem. |volume=86 |issue= 2 |pages= 135–42 |year= 1989 |pmid= 2770711 |doi=10.1007/BF00222613 }}<br /> *{{cite journal | author=Hirschhorn R, Tzall S, Ellenbogen A, Orkin SH |title=Identification of a point mutation resulting in a heat-labile adenosine deaminase (ADA) in two unrelated children with partial ADA deficiency |journal=J. Clin. Invest. |volume=83 |issue= 2 |pages= 497–501 |year= 1989 |pmid= 2783588 |doi=10.1172/JCI113909 | pmc=303706 }}<br /> *{{cite journal | author=Murray JL, Perez-Soler R, Bywaters D, Hersh EM |title=Decreased adenosine deaminase (ADA) and 5'nucleotidase (5NT) activity in peripheral blood T cells in Hodgkin disease |journal=Am. J. Hematol. |volume=21 |issue= 1 |pages= 57–66 |year= 1986 |pmid= 3010705 |doi=10.1002/ajh.2830210108 }}<br /> *{{cite journal | author=Wiginton DA, Kaplan DJ, States JC, ''et al.'' |title=Complete sequence and structure of the gene for human adenosine deaminase |journal=Biochemistry |volume=25 |issue= 25 |pages= 8234–44 |year= 1987 |pmid= 3028473 |doi=10.1021/bi00373a017 }}<br /> *{{cite journal | author=Akeson AL, Wiginton DA, Dusing MR, ''et al.'' |title=Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 16291–6 |year= 1988 |pmid= 3182793 |doi= }}<br /> *{{cite journal | author=Glader BE, Backer K |title=Elevated red cell adenosine deaminase activity: a marker of disordered erythropoiesis in Diamond-Blackfan anaemia and other haematologic diseases |journal=Br. J. Haematol. |volume=68 |issue= 2 |pages= 165–8 |year= 1988 |pmid= 3348976 |doi=10.1111/j.1365-2141.1988.tb06184.x }}<br /> *{{cite journal | author=Petersen MB, Tranebjaerg L, Tommerup N, ''et al.'' |title=New assignment of the adenosine deaminase gene locus to chromosome 20q13 X 11 by study of a patient with interstitial deletion 20q |journal=J. Med. Genet. |volume=24 |issue= 2 |pages= 93–6 |year= 1987 |pmid= 3560174 |doi=10.1136/jmg.24.2.93 | pmc=1049896 }}<br /> *{{cite journal | author=Orkin SH, Goff SC, Kelley WN, Daddona PE |title=Transient expression of human adenosine deaminase cDNAs: identification of a nonfunctional clone resulting from a single amino acid substitution |journal=Mol. Cell. Biol. |volume=5 |issue= 4 |pages= 762–7 |year= 1985 |pmid= 3838797 |doi= | pmc=366780 }}<br /> *{{cite journal | author=Valerio D, Duyvesteyn MG, Dekker BM, ''et al.'' |title=Adenosine deaminase: characterization and expression of a gene with a remarkable promoter |journal=EMBO J. |volume=4 |issue= 2 |pages= 437–43 |year= 1985 |pmid= 3839456 |doi= | pmc=554205 }}<br /> *{{cite journal | author=Bonthron DT, Markham AF, Ginsburg D, Orkin SH |title=Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency |journal=J. Clin. Invest. |volume=76 |issue= 2 |pages= 894–7 |year= 1985 |pmid= 3839802 |doi=10.1172/JCI112050 | pmc=423929 }}<br /> *{{cite journal | author=Daddona PE, Shewach DS, Kelley WN, ''et al.'' |title=Human adenosine deaminase. cDNA and complete primary amino acid sequence |journal=J. Biol. Chem. |volume=259 |issue= 19 |pages= 12101–6 |year= 1984 |pmid= 6090454 |doi= }}<br /> *{{cite journal | author=Valerio D, Duyvesteyn MG, Meera Khan P, ''et al.'' |title=Isolation of cDNA clones for human adenosine deaminase |journal=Gene |volume=25 |issue= 2-3 |pages= 231–40 |year= 1984 |pmid= 6198240 |doi=10.1016/0378-1119(83)90227-5 }}<br /> }}<br /> <br /> {{refend}}<br /> {{PDB Gallery|geneid=100}}<br /> {{碳-氮非肽水解酶}}<br /> {{核苷酸代谢酶类}}<br /> [[Category:酶]] [[Category:EC 3.5.4]] [[Category:免疫兴奋药]]<br /> ==参考来源==<br /> *[http://zh.wikipedia.org/wiki/%E8%85%BA%E8%8B%B7%E8%84%AB%E6%B0%A8%E9%85%B6 维基百科-腺苷脫氨酶]</div>

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