嘌呤核苷磷酸化酶

嘌呤核苷磷酸化酶
嘌呤核苷磷酸化酶
	PDB rendering based on 1m73.
有效结构
PDB	直系同源检索：PDBe, RCSB
PDB查询代码列表
	1M73, 1PF7, 1PWY, 1RCT, 1RFG, 1RR6, 1RSZ, 1RT9, 1ULA, 1ULB, 1V2H, 1V3Q, 1V41, 1V45, 1YRY, 2A0W, 2A0X, 2A0Y, 2OC4, 2OC9, 2ON6, 2Q7O, 3BGS, 3D1V, 3GB9, 3GGS, 3K8O, 3K8Q
标识
代号	PNP; FLJ94043; FLJ97288; FLJ97312; MGC117396; MGC125915; MGC125916; NP; PRO1837; PUNP
扩展标识	遗传学：164050 鼠基因：97365 同源基因：227 GeneCards: PNP Gene
EC編號	2.4.2.1
基因本体论描述
分子功能	· nucleoside binding; · purine base binding; · purine-nucleoside phosphorylase activity; · purine-nucleoside phosphorylase activity; · drug binding; · phosphate binding;
细胞成分	· intracellular; · cytoplasm; · cytosol; · cytoskeleton;
生物过程	· nucleobase, nucleoside, nucleotide and nucleic acid metabolic process; · purine base metabolic process; · inosine catabolic process; · purine nucleotide catabolic process; · nicotinamide riboside catabolic process; · immune response; · nucleoside metabolic process; · NAD biosynthesis via nicotinamide riboside salvage pathway; · urate biosynthetic process; · positive regulation of T cell proliferation; · response to drug; · response to drug; · purine-containing compound salvage; · positive regulation of alpha-beta T cell differentiation; · nucleobase, nucleoside and nucleotide metabolic process; · interleukin-2 secretion;
	Sources: Amigo / QuickGO
RNA表达模式
	更多表达数据
直系同源体
物种	人类
Entrez	4860
Ensembl	ENSG00000198805
UniProt	P00491
mRNA序列	NM_000270.3
蛋白序列	NP_000261.2
基因位置	Chr 14:; 20.94 – 20.95 Mb
PubMed查询	[1]
	查; 论; 编;

嘌呤核苷磷酸化酶（PNPase）
識別
符號	NP
Entrez	4860
HUGO	7892
OMIM	164050
PDB	1RT9
UniProt	P00491
其他資料
EC編號	2.4.2.1
基因座	14 q13.1

嘌呤核苷磷酸化酶英語：Purine nucleoside phosphorylase，简写为PNPase)是参与嘌呤代谢的一种酶。嘌呤核苷磷酸化酶可以代谢腺苷到腺嘌呤，肌苷到次黄嘌呤，鸟苷到鸟嘌呤，并在这些反应中产生核糖-1-磷酸。

需要注意的是，PNPase这一简称还被用于另一个不相关的酶，多核苷酸磷酸化酶（Polynucleotide Phosphorylase）。

参见

磷酸化酶

深入阅读

Markert ML. Purine nucleoside phosphorylase deficiency.. Immunodeficiency reviews. 1991, 3 (1): 45–81. PMID 1931007.
Borgers M, Verhaegen H, De Brabander M; et al. Purine nucleoside phosphorylase in chronic lymphocytic leukemia (CLL).. Blood. 1978, 52 (5): 886–95. PMID 100152.
Aust MR, Andrews LG, Barrett MJ; et al. Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency.. Am. J. Hum. Genet. 1992, 51 (4): 763–72. PMC 1682776 . PMID 1384322.
Andrews LG, Markert ML. Exon skipping in purine nucleoside phosphorylase mRNA processing leading to severe immunodeficiency.. J. Biol. Chem. 1992, 267 (11): 7834–8. PMID 1560016.
Jonsson JJ, Williams SR, McIvor RS. Sequence and functional characterization of the human purine nucleoside phosphorylase promoter.. Nucleic Acids Res. 1991, 19 (18): 5015–20. PMC 328804 . PMID 1923769. doi:10.1093/nar/19.18.5015.
Ealick SE, Rule SA, Carter DC; et al. Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.. J. Biol. Chem. 1990, 265 (3): 1812–20. PMID 2104852.
Williams SR, Gekeler V, McIvor RS, Martin DW. A human purine nucleoside phosphorylase deficiency caused by a single base change.. J. Biol. Chem. 1987, 262 (5): 2332–8. PMID 3029074.
Williams SR, Goddard JM, Martin DW. Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization.. Nucleic Acids Res. 1984, 12 (14): 5779–87. PMC 320030 . PMID 6087295. doi:10.1093/nar/12.14.5779.
Pannicke U, Tuchschmid P, Friedrich W; et al. Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient.. Hum. Genet. 1997, 98 (6): 706–9. PMID 8931706. doi:10.1007/s004390050290.
Markert ML, Finkel BD, McLaughlin TM; et al. Mutations in purine nucleoside phosphorylase deficiency.. Hum. Mutat. 1997, 9 (2): 118–21. PMID 9067751. doi:10.1002/(SICI)1098-1004(1997)9:2<118::AID-HUMU3>3.0.CO;2-5.
Erion MD, Takabayashi K, Smith HB; et al. Purine nucleoside phosphorylase. 1. Structure-function studies.. Biochemistry. 1997, 36 (39): 11725–34. PMID 9305962. doi:10.1021/bi961969w.
Erion MD, Stoeckler JD, Guida WC; et al. Purine nucleoside phosphorylase. 2. Catalytic mechanism.. Biochemistry. 1997, 36 (39): 11735–48. PMID 9305963. doi:10.1021/bi961970v.
Stoeckler JD, Poirot AF, Smith RM; et al. Purine nucleoside phosphorylase. 3. Reversal of purine base specificity by site-directed mutagenesis.. Biochemistry. 1997, 36 (39): 11749–56. PMID 9305964. doi:10.1021/bi961971n.
Sasaki Y, Iseki M, Yamaguchi S; et al. Direct evidence of autosomal recessive inheritance of Arg24 to termination codon in purine nucleoside phosphorylase gene in a family with a severe combined immunodeficiency patient.. Hum. Genet. 1998, 103 (1): 81–5. PMID 9737781. doi:10.1007/s004390050787.
Sheppard TL, Ordoukhanian P, Joyce GF. A DNA enzyme with N-glycosylase activity.. Proc. Natl. Acad. Sci. U.S.A. 2000, 97 (14): 7802–7. PMC 16625 . PMID 10884411. doi:10.1073/pnas.97.14.7802.
Dalal I, Grunebaum E, Cohen A, Roifman CM. Two novel mutations in a purine nucleoside phosphorylase (PNP)-deficient patient.. Clin. Genet. 2001, 59 (6): 430–7. PMID 11453975. doi:10.1034/j.1399-0004.2001.590608.x.
Ivings L, Pennington SR, Jenkins R; et al. Identification of Ca2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: interaction with actin, clathrin and tubulin.. Biochem. J. 2002, 363 (Pt 3): 599–608. PMC 1222513 . PMID 11964161. doi:10.1042/0264-6021:3630599.
Falkenberg M, Gaspari M, Rantanen A; et al. Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA.. Nat. Genet. 2002, 31 (3): 289–94. PMID 12068295. doi:10.1038/ng909.
Stoychev G, Kierdaszuk B, Shugar D. Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems.. Eur. J. Biochem. 2002, 269 (16): 4048–57. PMID 12180982. doi:10.1046/j.1432-1033.2002.03097.x.

外部链接

（英文）人源PNP结构（页面存档备份，存于互联网档案馆）
（英文）细菌PNP结构（页面存档备份，存于互联网档案馆）
（英文）醫學主題詞表（MeSH）：Purine-Nucleoside+Phosphorylase

相关疾病

参见

深入阅读

外部链接