腺苷脱氨酶

Adenosine deaminase (editase) domain
鉴定
标志	A_deamin
Pfam（蛋白家族查询站）	PF02137
InterPro（蛋白数据整合站）	IPR002466
PROSITE（蛋白数据站）	PDOC00419
SCOP（蛋白结构分类数据站）	1add
现有可用的蛋白结构：
Pfam	structures
PDB（蛋白质数据库）	RCSB PDB; PDBe
PDBsum（蛋白质三维结构站）	structure summary

Adenosine/AMP deaminase
	crystal structure of plasmodium yoelii adenosine deaminase (py02076)
鉴定
标志	A_deaminase
Pfam（蛋白家族查询站）	PF00962
Pfam宗系	CL0034
InterPro（蛋白数据整合站）	IPR001365
PROSITE（蛋白数据站）	PDOC00419
SCOP（蛋白结构分类数据站）	1add
现有可用的蛋白结构：
Pfam	structures
PDB（蛋白质数据库）	RCSB PDB; PDBe
PDBsum（蛋白质三维结构站）	structure summary

腺苷脱氨酶
	; 牛腺苷脱氨酶的丝带图。可见中央的锌离子。来自PDB 1VFL
有效结构
PDB	直系同源检索：PDBe, RCSB
PDB查询代码列表
	1M7M, 3IAR
标识
代号	ADA;
扩展标识	遗传学：608958 鼠基因：87916 同源基因：37249 GeneCards: ADA Gene
EC编号	3.5.4.4
基因本体论描述
分子功能	· purine nucleoside binding; · adenosine deaminase activity; · adenosine deaminase activity; · adenosine deaminase activity; · protein binding; · zinc ion binding; · zinc ion binding; · hydrolase activity; · metal ion binding;
细胞成分	· extracellular space; · cytoplasm; · lysosome; · cytosol; · plasma membrane; · external side of plasma membrane; · cell surface; · membrane; · cell junction; · cytoplasmic vesicle; · dendrite cytoplasm; · neuronal cell body; · cytoplasmic membrane-bounded vesicle lumen;
生物过程	· response to hypoxia; · in utero embryonic development; · trophectodermal cell differentiation; · liver development; · placenta development; · germinal center B cell differentiation; · positive regulation of germinal center formation; · negative regulation of leukocyte migration; · negative regulation of mature B cell apoptosis; · purine base metabolic process; · adenosine catabolic process; · adenosine catabolic process; · deoxyadenosine catabolic process; · cell adhesion; · aging; · nucleotide metabolic process; · purine ribonucleoside monophosphate biosynthetic process; · positive regulation of heart rate; · positive regulation of B cell proliferation; · purine nucleotide salvage; · positive regulation of T cell differentiation in thymus; · regulation of cell-cell adhesion mediated by integrin; · T cell activation; · response to hydrogen peroxide; · negative regulation of apoptosis; · purine-containing compound salvage; · regulation of circadian sleep/wake cycle, sleep; · positive regulation of smooth muscle contraction; · dATP catabolic process; · hypoxanthine biosynthetic process; · inosine biosynthetic process; · inosine biosynthetic process; · xanthine biosynthetic process; · positive regulation of alpha-beta T cell differentiation; · lung alveolus development; · Peyer's patch development; · embryonic digestive tract development; · negative regulation of inflammatory response; · positive regulation of calcium-mediated signaling; · positive regulation of T cell receptor signaling pathway; · nucleobase, nucleoside and nucleotide metabolic process; · negative regulation of adenosine receptor signaling pathway; · negative regulation of penile erection; · negative regulation of thymocyte apoptosis; · negative regulation of mucus secretion;
	Sources: Amigo / QuickGO
RNA表达模式
	更多表达数据
直系同源体
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A+医学百科 >> 腺苷脱氨酶

Adenosine/AMP deaminase N-terminal

鉴定

标志

A_deaminase_N

Pfam（蛋白家族查询站）

PF08451

InterPro（蛋白数据整合站）

IPR013659

现有可用的蛋白结构：
Pfam	structures
PDB（蛋白质数据库）	RCSB PDB; PDBe
PDBsum（蛋白质三维结构站）	structure summary

腺苷脱氨酶（英语：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。

反应

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。

病理学

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。

参考文献

深入阅读

da Cunha JG. [Adenosine deaminase. A pluridisciplinary enzyme]. Acta médica portuguesa. 1992, 4 (6): 315–23. PMID 1807098.
Franco R, Casadó V, Ciruela F, et al.. Cell surface adenosine deaminase: much more than an ectoenzyme. Prog. Neurobiol.. 1997, 52 (4): 283–94. doi:10.1016/S0301-0082(97)00013-0. PMID 9247966.
Valenzuela A, Blanco J, Callebaut C, et al.. HIV-1 envelope gp120 and viral particles block adenosine deaminase binding to human CD26. Adv. Exp. Med. Biol.. 1997, 421: 185–92. PMID 9330696.
Moriwaki Y, Yamamoto T, Higashino K. Enzymes involved in purine metabolism--a review of histochemical localization and functional implications. Histol. Histopathol.. 1999, 14 (4): 1321–40. PMID 10506947.
Hirschhorn R. Identification of two new missense mutations (R156C and S291L) in two ADA- SCID patients unusual for response to therapy with partial exchange transfusions. Hum. Mutat.. 1993, 1 (2): 166–8. doi:10.1002/humu.1380010214. PMID 1284479.
Berkvens TM, van Ormondt H, Gerritsen EJ, et al.. Identical 3250-bp deletion between two AluI repeats in the ADA genes of unrelated ADA-SCID patients. Genomics. 1990, 7 (4): 486–90. doi:10.1016/0888-7543(90)90190-6. PMID 1696926.
Aran JM, Colomer D, Matutes E, et al.. Presence of adenosine deaminase on the surface of mononuclear blood cells: immunochemical localization using light and electron microscopy. J. Histochem. Cytochem.. 1991, 39 (8): 1001–8. PMID 1856451.
Bielat K, Tritsch GL. Ecto-enzyme activity of human erythrocyte adenosine deaminase. Mol. Cell. Biochem.. 1989, 86 (2): 135–42. doi:10.1007/BF00222613. PMID 2770711.
Hirschhorn R, Tzall S, Ellenbogen A, Orkin SH. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC303706/ Identification of a point mutation resulting in a heat-labile adenosine deaminase (ADA) in two unrelated children with partial ADA deficiency]. J. Clin. Invest.. 1989, 83 (2): 497–501. doi:10.1172/JCI113909. PMID 2783588. PMC 303706.
Murray JL, Perez-Soler R, Bywaters D, Hersh EM. Decreased adenosine deaminase (ADA) and 5'nucleotidase (5NT) activity in peripheral blood T cells in Hodgkin disease. Am. J. Hematol.. 1986, 21 (1): 57–66. doi:10.1002/ajh.2830210108. PMID 3010705.
Wiginton DA, Kaplan DJ, States JC, et al.. Complete sequence and structure of the gene for human adenosine deaminase. Biochemistry. 1987, 25 (25): 8234–44. doi:10.1021/bi00373a017. PMID 3028473.
Akeson AL, Wiginton DA, Dusing MR, et al.. Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts. J. Biol. Chem.. 1988, 263 (31): 16291–6. PMID 3182793.
Glader BE, Backer K. Elevated red cell adenosine deaminase activity: a marker of disordered erythropoiesis in Diamond-Blackfan anaemia and other haematologic diseases. Br. J. Haematol.. 1988, 68 (2): 165–8. doi:10.1111/j.1365-2141.1988.tb06184.x. PMID 3348976.
Petersen MB, Tranebjaerg L, Tommerup N, et al.. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC1049896/ New assignment of the adenosine deaminase gene locus to chromosome 20q13 X 11 by study of a patient with interstitial deletion 20q]. J. Med. Genet.. 1987, 24 (2): 93–6. doi:10.1136/jmg.24.2.93. PMID 3560174. PMC 1049896.
Orkin SH, Goff SC, Kelley WN, Daddona PE. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC366780/ Transient expression of human adenosine deaminase cDNAs: identification of a nonfunctional clone resulting from a single amino acid substitution]. Mol. Cell. Biol.. 1985, 5 (4): 762–7. PMID 3838797. PMC 366780.
Valerio D, Duyvesteyn MG, Dekker BM, et al.. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC554205/ Adenosine deaminase: characterization and expression of a gene with a remarkable promoter]. EMBO J.. 1985, 4 (2): 437–43. PMID 3839456. PMC 554205.
Bonthron DT, Markham AF, Ginsburg D, Orkin SH. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC423929/ Identification of a point mutation in the adenosine deaminase gene responsible for immunodeficiency]. J. Clin. Invest.. 1985, 76 (2): 894–7. doi:10.1172/JCI112050. PMID 3839802. PMC 423929.
Daddona PE, Shewach DS, Kelley WN, et al.. Human adenosine deaminase. cDNA and complete primary amino acid sequence. J. Biol. Chem.. 1984, 259 (19): 12101–6. PMID 6090454.
Valerio D, Duyvesteyn MG, Meera Khan P, et al.. Isolation of cDNA clones for human adenosine deaminase. Gene. 1984, 25 (2-3): 231–40. doi:10.1016/0378-1119(83)90227-5. PMID 6198240.