アデニンホスホリボシルトランスフェラーゼ
- 同
- APRT
WordNet
- (biochemistry) purine base found in DNA and RNA; pairs with thymine in DNA and with uracil in RNA (同)A
PrepTutorEJDIC
- アデニン(肝臓・茶の葉から採れる塩基の一種)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2012/03/18 04:37:21」(JST)
[Wiki en表示]
Adenine phosphoribosyltransferase |
Ribbon diagram of a human APRT dimer, in complex with PRPP, adenine and ribose 5-phosphate. One magnesium ion visible in green. From PDB 1ZN7. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1OPU, 1ORE, 1ZN7, 1ZN8, 1ZN9
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Identifiers |
Symbols |
APRT; AMP |
External IDs |
OMIM: 102600 MGI: 88061 HomoloGene: 413 GeneCards: APRT Gene |
EC number |
2.4.2.7 |
Gene Ontology |
Molecular function |
• adenine binding
• adenine phosphoribosyltransferase activity
• AMP binding
• transferase activity, transferring glycosyl groups
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Cellular component |
• nucleus
• nucleolus
• cytoplasm
• cytoplasm
• cytosol
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Biological process |
• purine base metabolic process
• purine ribonucleoside salvage
• adenine salvage
• lactation
• grooming behavior
• nucleoside metabolic process
• purine-containing compound salvage
• small molecule metabolic process
• nucleobase-containing small molecule metabolic process
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Sources: Amigo / QuickGO |
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RNA expression pattern |
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More reference expression data |
Orthologs |
Species |
Human |
Mouse |
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Entrez |
353 |
11821 |
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Ensembl |
ENSG00000198931 |
ENSMUSG00000006589 |
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UniProt |
P07741 |
Q6PK77 |
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RefSeq (mRNA) |
NM_000485.2 |
NM_009698.2 |
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RefSeq (protein) |
NP_000476.1 |
NP_033828.2 |
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Location (UCSC) |
Chr 16:
88.88 – 88.88 Mb |
Chr 8:
125.1 – 125.1 Mb |
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PubMed search |
[1] |
[2] |
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Adenine phosphoribosyltransferase is an enzyme that in humans is encoded by the APRT gene.[1]
Contents
- 1 Function
- 2 Pathology
- 3 References
- 4 Further reading
- 5 External links
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Function
APRTase is an enzyme involved in the purine nucleotide salvage pathway. It functions as a catalyst in the reaction between adenine and phosphoribosyl pyrophosphate (PRPP) to form AMP.
APRT is functionally related to hypoxanthine-guanine phosphoribosyltransferase (HPRT).
Pathology
Deficiency of APRT in human beings may lead to kidney stones formed of adenine and salts.
2,8-Dihydroxy-adenine urolithiasis is also known as "adenine phosphoribosyltransferase deficiency".
Adenine phosphoribosyltransferase (APRT) deficiency is an uncommon genetic disorder that often causes kidney stones, and in some patients kidney failure. More than 300 individuals with this disease have been reported world-wide but it is not known how common this medical problem truly is. Patients with the disease deficiency lack the enzyme adenine phosphoribosyltransferase and therefore have difficulties breaking down dietary substances called purines, resulting in accumulation of a compound called 2,8-dihydroxyadenine (2,8-DHA) that is excreted by the kidneys. 2,8-DHA is poorly soluble in the urine leads to the formation of kidney stones and kidney injury. Interestingly, up to 70% of affected patients, have red hair or relatives with this hair color.
References
- ^ "Entrez Gene: APRT adenine phosphoribosyltransferase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=353.
Further reading
- Tischfield JA, Engle SJ, Gupta PK, et al. (1995). "Germline and somatic mutation at the APRT locus of mice and man.". Adv. Exp. Med. Biol. 370: 661–4. PMID 7660991.
- Takeuchi H, Kaneko Y, Fujita J, Yoshida O (1993). "A case of a compound heterozygote for adenine phosphoribosyltransferase deficiency (APRT*J/APRT*Q0) leading to 2,8-dihydroxyadenine urolithiasis: review of the reported cases with 2,8-dihydroxyadenine stones in Japan.". J. Urol. 149 (4): 824–6. PMID 8455250.
- Ludwig H, Kuzmits R, Pietschmann H, Müller MM (1980). "Enzymes of the purine interconversion system in chronic lymphatic leukemia: decreased purine nucleoside phosphorylase and adenosine deaminase activity.". Blut 39 (5): 309–15. doi:10.1007/BF01014193. PMID 116697.
- Johnson LA, Gordon RB, Emmerson BT (1977). "Adenine phosphoribosyltransferase: a simple spectrophotometric assay and the incidence of mutation in the normal population.". Biochem. Genet. 15 (3–4): 265–72. doi:10.1007/BF00484458. PMID 869896.
- Kamatani N, Hakoda M, Otsuka S, et al. (1992). "Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients". J. Clin. Invest. 90 (1): 130–5. doi:10.1172/JCI115825. PMC 443071. PMID 1353080. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=443071.
- Chen J, Sahota A, Laxdal T, et al. (1992). "Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient". Am. J. Hum. Genet. 49 (6): 1306–11. PMC 1686459. PMID 1746557. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1686459.
- Mimori A, Hidaka Y, Wu VC, et al. (1991). "A mutant allele common to the type I adenine phosphoribosyltransferase deficiency in Japanese subjects". Am. J. Hum. Genet. 48 (1): 103–7. PMC 1682758. PMID 1985452. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1682758.
- Chen J, Sahota A, Stambrook PJ, Tischfield JA (1991). "Polymerase chain reaction amplification and sequence analysis of human mutant adenine phosphoribosyltransferase genes: the nature and frequency of errors caused by Taq DNA polymerase". Mutat. Res. 249 (1): 169–76. doi:10.1016/0027-5107(91)90143-C. PMID 2067530.
- Gathof BS, Sahota A, Gresser U, et al. (1992). "Identification of a splice mutation at the adenine phosphoribosyltransferase locus in a German family". Klin. Wochenschr. 69 (24): 1152–5. doi:10.1007/BF01815434. PMID 2135300.
- Kamatani N, Kuroshima S, Hakoda M, et al. (1990). "Crossovers within a short DNA sequence indicate a long evolutionary history of the APRT*J mutation". Hum. Genet. 85 (6): 600–4. doi:10.1007/BF00193582. PMID 2227951.
- Kamatani N, Kuroshima S, Terai C, et al. (1989). "Detection of an amino acid substitution in the mutant enzyme for a special type of adenine phosphoribosyltransferase (APRT) deficiency by sequence-specific protein cleavage". Am. J. Hum. Genet. 45 (2): 325–31. PMC 1683345. PMID 2502918. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1683345.
- Hidaka Y, Tarlé SA, Fujimori S, et al. (1988). "Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese". J. Clin. Invest. 81 (3): 945–50. doi:10.1172/JCI113408. PMC 442550. PMID 3343350. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442550.
- Wilson JM, O'Toole TE, Argos P, et al. (1986). "Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme". J. Biol. Chem. 261 (29): 13677–83. PMID 3531209.
- Broderick TP, Schaff DA, Bertino AM, et al. (1987). "Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement". Proc. Natl. Acad. Sci. U.S.A. 84 (10): 3349–53. doi:10.1073/pnas.84.10.3349. PMC 304867. PMID 3554238. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304867.
- Hidaka Y, Palella TD, O'Toole TE, et al. (1987). "Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme". J. Clin. Invest. 80 (5): 1409–15. doi:10.1172/JCI113219. PMC 442397. PMID 3680503. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442397.
- Hidaka Y, Tarlé SA, O'Toole TE, et al. (1988). "Nucleotide sequence of the human APRT gene". Nucleic Acids Res. 15 (21): 9086. doi:10.1093/nar/15.21.9086. PMC 306432. PMID 3684585. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=306432.
- Chen J, Sahota A, Martin GF, et al. (1993). "Analysis of germline and in vivo somatic mutations in the human adenine phosphoribosyltransferase gene: mutational hot spots at the intron 4 splice donor site and at codon 87". Mutat. Res. 287 (2): 217–25. doi:10.1016/0027-5107(93)90014-7. PMID 7685481.
- Sahota A, Chen J, Boyadjiev SA, et al. (1994). "Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis". Hum. Mol. Genet. 3 (5): 817–8. doi:10.1093/hmg/3.5.817. PMID 7915931.
External links
- MeSH Adenine+phosphoribosyltransferase
PDB gallery
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1ore: Human Adenine Phosphoribosyltransferase
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1zn7: Human Adenine Phosphoribosyltransferase Complexed with PRPP, ADE and R5P
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1zn8: Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution
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1zn9: Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms
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Transferases: glycosyltransferases (EC 2.4)
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2.4.1: Hexosyl-
transferases |
Glucosyl-
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Phosphorylase (Starch, Glycogen, Myo-) · Glycogen synthase · Debranching enzyme · Branching enzyme · 1,3-beta-glucan synthase · Ceramide glucosyltransferase
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Galactosyl-
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Lactose synthase · B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase · Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1)
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Glucuronosyl-
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B3GAT1, B3GAT2, B3GAT3
UGT1A1, UGT1A3, UGT1A4, UGT1A5, UGT1A6, UGT1A7, UGT1A8, UGT1A9, UGT1A10
UGT2A1, UGT2A2, UGT2A3, UGT2B4, UGT2B7, UGT2B10, UGT2B11, UGT2B15, UGT2B17, UGT2B28
Hyaluronan synthase: HAS1 · HAS2 · HAS3
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Fucosyl-
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POFUT1 · POFUT2 · FUT1 · FUT2 · FUT3 · FUT4 · FUT5 · FUT6 · FUT7 · FUT8 · FUT9 · FUT10 · FUT11
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Mannosyl-
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Dolichyl-phosphate-mannose-protein mannosyltransferase (POMT1, POMT2) · DPM1 · DPM3
ALG1 · ALG2 · ALG3 · ALG6 · ALG8 · ALG9 · ALG12
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2.4.2: Pentosyl-
transferases |
Ribose
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ADP-ribosyltransferase
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NAD +:diphthamide ADP-ribosyltransferase (Diphtheria toxin)
NAD(P)+:arginine ADP-ribosyltransferase (Pertussis toxin · Cholera toxin)
Poly ADP ribose polymerase
Sirtuin
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Phosphoribosyltransferase
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Adenine phosphoribosyltransferase · Hypoxanthine-guanine phosphoribosyltransferase · Uracil phosphoribosyltransferase · Amidophosphoribosyltransferase
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Other
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Purine nucleoside phosphorylase: Thymidine phosphorylase (ECGF1)
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Other
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Xylosyltransferase · Arabinosyltransferase (Indolylacetylinositol arabinosyltransferase)
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2.4.99: Sialyl
transferases |
Beta-galactoside alpha-2,6-sialyltransferase · Monosialoganglioside sialyltransferase · ST8SIA4
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 3.1.3.48
- 3.4.21
- 4.1
- 5.1
- 6.1-3
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Metabolism: amino acid metabolism · nucleotide enzymes
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Purine metabolism |
Anabolism
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R5P->IMP: Ribose-phosphate diphosphokinase · Amidophosphoribosyltransferase · Phosphoribosylglycinamide formyltransferase · AIR synthetase (FGAM cyclase) · Phosphoribosylaminoimidazole carboxylase · Phosphoribosylaminoimidazolesuccinocarboxamide synthase · IMP synthase
IMP->AMP: Adenylosuccinate synthase · Adenylosuccinate lyase · reverse (AMP deaminase)
IMP->GMP: IMP dehydrogenase · GMP synthase · reverse (GMP reductase)
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Nucleotide salvage
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Hypoxanthine-guanine phosphoribosyltransferase · Adenine phosphoribosyltransferase
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Catabolism
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Adenosine deaminase · Purine nucleoside phosphorylase · Guanine deaminase · Xanthine oxidase · Urate oxidase
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Pyrimidine metabolism |
Anabolism
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CAD (Carbamoyl phosphate synthase II, Aspartate carbamoyltransferase, Dihydroorotase)
Dihydroorotate dehydrogenase · Orotidine 5'-phosphate decarboxylase/Uridine monophosphate synthetase
CTP synthase
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Catabolism
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Dihydropyrimidine dehydrogenase · Dihydropyrimidinase/DPYS · Beta-ureidopropionase/UPB1
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Deoxyribonucleotides |
Ribonucleotide reductase · Nucleoside-diphosphate kinase · DCMP deaminase · Thymidylate synthase · Dihydrofolate reductase
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- Induction of DNA Demethylation Depending on Two Sets of Sox2 and Adjacent Oct3/4 Binding Sites (Sox-Oct Motifs) within the Mouse H19/Insulin-like Growth Factor 2 (Igf2) Imprinted Control Region.
- Hori N, Yamane M, Kouno K, Sato K.SourceFrom the Division of Molecular Biology, Faculty of Medicine, Department of Molecular and Cellular Biology, School of Life Sciences and.
- The Journal of biological chemistry.J Biol Chem.2012 Dec 21;287(52):44006-16. doi: 10.1074/jbc.M112.424580. Epub 2012 Oct 31.
- DNA demethylation is used to establish and maintain an unmethylated state. The molecular mechanisms to induce DNA demethylation at a particular genomic locus remain unclear. The mouse H19/insulin-like growth factor 2 (Igf2) imprinted control region (ICR) is a methylation state-sensitive insulator th
- PMID 23115243
- Quinolinate salvage and insights for targeting NAD biosynthesis in group A Streptococci.
- Sorci L, Blaby IK, Rodionova IA, De Ingeniis J, Tkachenko S, de Crécy-Lagard V, Osterman AL.SourceSanford-Burnham Medical Research Institute, La Jolla, California, USA.
- Journal of bacteriology.J Bacteriol.2012 Nov 30. [Epub ahead of print]
- The essential coenzyme nicotinamide adenine dinucleotide (NAD) plays important roles in metabolic reactions and cell regulation in all organisms. As such NAD synthesis has been investigated as a source for novel antibacterial targets. Cross-species genomics-based reconstructions of NAD metabolism in
- PMID 23204464
- Down-regulation of NAMPT expression by miR-182 is involved in Tat-induced HIV-1 long terminal repeat (LTR) transactivation.
- Chen XY, Zhang HS, Wu TC, Sang WW, Ruan Z.SourceCollege of Life Science & Bioengineering, Beijing University of Technology, Pingleyuan 100#, District of Chaoyang, Beijing 100124, China.
- The international journal of biochemistry & cell biology.Int J Biochem Cell Biol.2012 Nov 12;45(2):292-298. doi: 10.1016/j.biocel.2012.11.002. [Epub ahead of print]
- Tat's transactivating activity is controlled by sirtuin 1 (SIRT1) that connects HIV transcription with the metabolic state of the cell. Nicotinamide phosphoribosyltransferase (NAMPT) is a key enzyme in the salvaging pathway for the synthesis of nicotinamide adenine dinucleotide (NAD(+)) that is invo
- PMID 23153509
Japanese Journal
- 本邦初のAPRT*Q0(M1V)変異によるAPRT欠損症の1例
- 池田 裕一,渡辺 常樹,藤本 陽子 [他]
- 泌尿器科紀要 57(1), 15-19, 2011-01
- … revised versionのpdfは、泌尿器科紀要vol.58 no.7 p.365-(2012年7月発行)Adenine phosphoribosyltransferase (APRT) deficiency is an enzyme deficiency associated with purine metabolism, a hereditary disease that causes recurrent 2, 8-DHA stone formation due to a complete or partial APRT defect and slowly damages the renal function. …
- NAID 40019362669
- Adenine phosphoribosyltransferase欠損症による小児2,8-dihydroxyadenine結石の1例
- 高尾 智也,河崎 正裕
- 日本小児外科学会雑誌 46(5), 880-883, 2010-08-20
- … 症例は1歳11か月の女児で尿路感染を主訴に紹介された.腹部CTで,放射線透過性の尿路結石嵌頓による両側水腎症を認め緊急腎瘻造設術と経尿道的尿管結石破砕術を行った.結石は2,8-dihydroxyadenineと分析された.またPCR法による遺伝子検査でadenine phosphoribosyltransferase欠損症と診断された.両側水腎症はESWLで改善したが,結石は残存している.現在,少量アロプリノール内服で経過観察中である. …
- NAID 110007682260
Related Links
- Adenine phosphoribosyltransferase (APRT) deficiency is an inherited condition that affects the kidneys and urinary tract. The most common feature of this condition is recurrent kidney stones; urinary tract stones are also ...
- TEXT Description The APRT gene encodes adenine phosphoribosyltransferase (EC 2.4.2.7), an enzyme that catalyzes the formation of AMP from adenine and ...
★リンクテーブル★
[★]
- 英
- adenine phosphoribosyltransferase, APRT
- 関
- HGPRT
- AMPのサルベージ経路において、アデニンと5-ホスホリボシル二リン酸からAMPを生成する酵素
- アデニン + PRPP ⇔ AMP + PPi
臨床関連
[★]
アデニンホスホリボシルトランスフェラーゼ
- 同
- adenine phosphoribosyltransferase
- 同
- adenine phosphoribosyltransferase
[★]
- 関
- adenine phosphoribosyltransferase
[★]
- 同
- adenine phosphoribosyltransferase
[★]
ホスホリボシルトランスフェラーゼ、ホスホリボシル基転移酵素