ヒポキサンチンホスホリボシルトランスフェラーゼ
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/10/25 13:58:04」(JST)
[Wiki ja表示]
ヒポキサンチン-グアニンホスホリボシルトランスフェラーゼ
ヒポキサンチン-グアニンホスホリボシルトランスフェラーゼ（英: Hypoxanthine-guanine phosphoribosyltransferase; HGPRT, HPRT[1]、EC 2.4.2.8）は、プリン代謝酵素の1つ。
目次
- 1 反応
- 2 突然変異
- 3 関連項目
- 4 脚注
- 5 参考文献
- 6 外部リンク
反応
この酵素は以下の反応を行う。
| 反応物 |
生成物 |
記述 |
| ヒポキサンチン |
イノシン酸（イノシン一リン酸、IMP） |
- |
| グアニン |
グアニル酸（グアニン一リン酸、GMP） |
この反応をするときのみしばしばHGPRTと呼ばれる。 |
| キサンチン |
キサンチル酸（キサントシン一リン酸、XMP） |
- |
この酵素は主に退化したDNAからプリンの再合成を行う。その役割は、グアニンとホスホリボシル二リン酸（PRPP）からのGMPの合成、および、ヒポキサンチンとPRPPからのIMPの合成である。
突然変異
遺伝子の突然変異は高尿酸血症を誘引する。
- レッシュ・ナイハン症候群はHPRTの突然変異で起こる。
- いくつかの変異は痛風に繋がる。
関連項目
脚注
- ^ Entrez Gene: hypoxanthine phosphoribosyltransferase 1 (Lesch-Nyhan syndrome)
参考文献
- Sculley DG, Dawson PA, Emmerson BT, Gordon RB (1993). "A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency.". Hum. Genet. 90 (3): 195-207. PMID 1487231.
- Davidson BL, Tarlé SA, Van Antwerp M, et al. (1991). "Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency.". Am. J. Hum. Genet. 48 (5): 951-8. PMID 2018042.
- Stout JT, Caskey CT (1986). "HPRT: gene structure, expression, and mutation.". Annu. Rev. Genet. 19: 127-48. doi:10.1146/annurev.ge.19.120185.001015. PMID 3909940.
- Sege-Peterson K, Chambers J, Page T, et al. (1993). "Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency.". Hum. Mol. Genet. 1 (6): 427-32. PMID 1301916.
- Lightfoot T, Joshi R, Nuki G, Snyder FF (1992). "The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction.". Hum. Genet. 88 (6): 695-6. PMID 1551676.
- Yamada Y, Goto H, Ogasawara N (1992). "Identification of two independent Japanese mutant HPRT genes using the PCR technique.". Adv. Exp. Med. Biol. 309B: 121-4. PMID 1840476.
- Sculley DG, Dawson PA, Beacham IR, et al. (1991). "Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification.". Hum. Genet. 87 (6): 688-92. PMID 1937471.
- Tarlé SA, Davidson BL, Wu VC, et al. (1991). "Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects.". Genomics 10 (2): 499-501. PMID 2071157.
- Gordon RB, Sculley DG, Dawson PA, et al. (1991). "Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE).". J. Inherit. Metab. Dis. 13 (5): 692-700. PMID 2246854.
- Edwards A, Voss H, Rice P, et al. (1990). "Automated DNA sequencing of the human HPRT locus.". Genomics 6 (4): 593-608. PMID 2341149.
- Gibbs RA, Nguyen PN, Edwards A, et al. (1990). "Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families.". Genomics 7 (2): 235-44. PMID 2347587.
- Skopek TR, Recio L, Simpson D, et al. (1990). "Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures.". Hum. Genet. 85 (1): 111-6. PMID 2358296.
- Davidson BL, Tarlé SA, Palella TD, Kelley WN (1989). "Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts.". J. Clin. Invest. 84 (1): 342-6. PMID 2738157.
- Ogasawara N, Stout JT, Goto H, et al. (1989). "Molecular analysis of a female Lesch-Nyhan patient.". J. Clin. Invest. 84 (3): 1024-7. PMID 2760209.
- Yang TP, Stout JT, Konecki DS, et al. (1988). "Spontaneous reversion of novel Lesch-Nyhan mutation by HPRT gene rearrangement.". Somat. Cell Mol. Genet. 14 (3): 293-303. PMID 2835825.
- Fujimori S, Hidaka Y, Davidson BL, et al. (1988). "Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor).". Hum. Genet. 79 (1): 39-43. PMID 2896620.
- Davidson BL, Pashmforoush M, Kelley WN, Palella TD (1989). "Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville).". J. Biol. Chem. 264 (1): 520-5. PMID 2909537.
- Fujimori S, Davidson BL, Kelley WN, Palella TD (1989). "Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome.". J. Clin. Invest. 83 (1): 11-3. PMID 2910902.
外部リンク
- Purine metabolism at genome.jp
- MeSH Hypoxanthine+phosphoribosyltransferase
[Wiki en表示]
| HPRT1 |
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| Available structures |
| PDB |
Ortholog search: PDBe RCSB |
| List of PDB id codes |
|
1BZY, 1D6N, 1HMP, 1Z7G, 3GEP, 3GGC, 3GGJ, 2VFA, 4IJQ, 4KN6, 4RAB, 4RAC, 4RAD, 4RAN, 4RAO, 4RAQ, 5BSK, 5BRN
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| Identifiers |
| Aliases |
HPRT1, HGPRT, HPRT, hypoxanthine phosphoribosyltransferase 1 |
| External IDs |
OMIM: 308000 MGI: 96217 HomoloGene: 56590 GeneCards: 3251 |
| Gene ontology |
| Molecular function |
• transferase activity
• nucleotide binding
• protein homodimerization activity
• transferase activity, transferring glycosyl groups
• hypoxanthine phosphoribosyltransferase activity
• guanine phosphoribosyltransferase activity
• metal ion binding
• protein binding
• identical protein binding
• magnesium ion binding
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| Cellular component |
• cytoplasm
• cytosol
• extracellular exosome
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| Biological process |
• purine nucleotide biosynthetic process
• grooming behavior
• cytolysis
• purine ribonucleoside salvage
• GMP catabolic process
• adenine salvage
• locomotory behavior
• dendrite morphogenesis
• hypoxanthine metabolic process
• guanine salvage
• response to amphetamine
• purine-containing compound salvage
• nucleoside metabolic process
• dopamine metabolic process
• central nervous system neuron development
• lymphocyte proliferation
• cerebral cortex neuron differentiation
• IMP metabolic process
• GMP salvage
• IMP salvage
• protein homotetramerization
• striatum development
• hypoxanthine salvage
• adenine metabolic process
• positive regulation of dopamine 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 |
| Entrez |
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| Ensembl |
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| UniProt |
|
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| RefSeq (mRNA) |
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| RefSeq (protein) |
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| Location (UCSC) |
Chr X: 134.46 – 134.52 Mb |
Chr X: 52.99 – 53.02 Mb |
| PubMed search |
[1] |
[2] |
| Wikidata |
| View/Edit Human |
View/Edit Mouse |
Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is an enzyme encoded in humans by the HPRT1 gene.[3][4]
HGPRT is a transferase that catalyzes conversion of hypoxanthine to inosine monophosphate and guanine to guanosine monophosphate. This reaction transfers the 5-phosphoribosyl group from 5-phosphoribosyl 1-pyrophosphate (PRPP) to the purine. HGPRT plays a central role in the generation of purine nucleotides through the purine salvage pathway.
Contents
- 1 Function
- 2 Substrates and inhibitors
- 3 Role in disease
- 4 Creation of hybridomas
- 5 See also
- 6 References
- 7 Further reading
- 8 External links
Function
| hypoxanthine phosphoribosyltransferase |
| Identifiers |
| EC number |
2.4.2.8 |
| CAS number |
9016-12-0 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
HGPRT catalyzes the following reactions:
| Substrate |
Product |
Notes |
| hypoxanthine |
inosine monophosphate |
— |
| guanine |
guanosine monophosphate |
Often called HGPRT. Performs this function only in some species. |
| xanthine |
xanthosine monophosphate |
Only certain HPRTs. |
HGPRTase functions primarily to salvage purines from degraded DNA to reintroduce into purine synthetic pathways. In this role, it catalyzes the reaction between guanine and phosphoribosyl pyrophosphate (PRPP) to form GMP, or between hypoxanthine and phosphoribosyl pyrophosphate (PRPP) to form inosine monophosphate.
Substrates and inhibitors
Comparative homology modelling of this enzyme in L. donovani suggest that among all of the computationally screened compounds, pentamidine, 1,3-dinitroadamantane, acyclovir and analogs of acyclovir had higher binding affinities than the real substrate (guanosine monophosphate).[5] The in silico and in-vitro correlation of these compounds were test in Leishmania HGPRT and validates the result.[6]
Role in disease
Mutations in the gene lead to hyperuricemia:
- Some men have partial (up to 20% less activity of the enzyme) HGPRT deficiency that causes high levels of uric acid in the blood, which leads to the development of gouty arthritis and the formation of uric acid stones in the urinary tract. This condition has been named the Kelley-Seegmiller syndrome.[7]
- Lesch-Nyhan syndrome is due to deficiency of HGPRT caused by HPRT1 mutation [8]
- Some mutations have been linked to gout, the risk of which is increased in hypoxanthine-guanine phosphoribosyltransferase deficiency.
- HPRT expression on the mRNA and protein level is induced by hypoxia inducible factor 1 (HIF1A). HIF-1 is a transcription factor that directs an array of cellular responses that are used for adaptation during oxygen deprivation. This finding implies that HPRT is a critical pathway that helps preserve the cell's purine nucleotide resources under hypoxic conditions as found in pathology such as myocardial ischemia.[9]
Creation of hybridomas
Hybridomas are immortal (immune to cellular senescence), HGPRT+ cells that result from fusion of mortal, HGPRT+ plasma cells and immortal, HGPRT− myeloma cells. They are created to produce monoclonal antibodies in biotechnology. HAT medium inhibits de novo synthesis of nucleic acids, killing myeloma cells that cannot switch over to the salvage pathway, due to lack of HRPT1. The plasma cells in the culture eventually die from senesence, leaving pure hybridoma cells.
See also
References
- ^ "Human PubMed Reference:".
- ^ "Mouse PubMed Reference:".
- ^ "Entrez Gene: hypoxanthine phosphoribosyltransferase 1 (Lesch-Nyhan syndrome)".
- ^ Finette BA, Kendall H, Vacek PM (Aug 2002). "Mutational spectral analysis at the HPRT locus in healthy children". Mutation Research. 505 (1-2): 27–41. doi:10.1016/S0027-5107(02)00119-7. PMID 12175903.
- ^ Ansari MY, Dikhit MR, Sahoo GC, Das P (Apr 2012). "Comparative modeling of HGPRT enzyme of L. donovani and binding affinities of different analogs of GMP". International Journal of Biological Macromolecules. 50 (3): 637–49. doi:10.1016/j.ijbiomac.2012.01.010. PMID 22327112.
- ^ Ansari MY, Equbal A, Dikhit MR, Mansuri R, Rana S, Ali V, Sahoo GC, Das P (Nov 2015). "Establishment of Correlation between In-Silico &In-Vitro Test Analysis against Leishmania HGPRT to inhibitors". International Journal of Biological Macromolecules. 83: 78–96. doi:10.1016/j.ijbiomac.2015.11.051. PMID 26616453.
- ^ Khattak FH, Morris IM, Harris K (May 1998). "Kelley-Seegmiller syndrome: a case report and review of the literature". British Journal of Rheumatology. 37 (5): 580–1. doi:10.1093/rheumatology/37.5.580c. PMID 9651092.
- ^ Hladnik U, Nyhan WL, Bertelli M (Sep 2008). "Variable expression of HPRT deficiency in 5 members of a family with the same mutation". Archives of Neurology. 65 (9): 1240–3. doi:10.1001/archneur.65.9.1240. PMID 18779430.
- ^ Wu J, Bond C, Chen P, Chen M, Li Y, Shohet RV, Wright G (Feb 2015). "HIF-1α in the heart: Remodeling nucleotide metabolism". Journal of Molecular and Cellular Cardiology. 82: 194–200. doi:10.1016/j.yjmcc.2015.01.014. PMID 25681585.
Further reading
- Sculley DG, Dawson PA, Emmerson BT, Gordon RB (Nov 1992). "A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency". Human Genetics. 90 (3): 195–207. doi:10.1007/bf00220062. PMID 1487231.
- Ansari MY, Dikhit MR, Sahoo GC, Das P (Apr 2012). "Comparative modeling of HGPRT enzyme of L. donovani and binding affinities of different analogs of GMP". International Journal of Biological Macromolecules. 50 (3): 637–49. doi:10.1016/j.ijbiomac.2012.01.010. PMID 22327112.
- Davidson BL, Tarlé SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD (May 1991). "Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency". American Journal of Human Genetics. 48 (5): 951–8. PMC 1683055. PMID 2018042.
- Stout JT, Caskey CT (1986). "HPRT: gene structure, expression, and mutation". Annual Review of Genetics. 19: 127–48. doi:10.1146/annurev.ge.19.120185.001015. PMID 3909940.
- Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL (Sep 1992). "Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency". Human Molecular Genetics. 1 (6): 427–32. doi:10.1093/hmg/1.6.427. PMID 1301916.
- Lightfoot T, Joshi R, Nuki G, Snyder FF (Mar 1992). "The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction". Human Genetics. 88 (6): 695–6. doi:10.1007/BF02265300. PMID 1551676.
- Yamada Y, Goto H, Ogasawara N (1992). "Identification of two independent Japanese mutant HPRT genes using the PCR technique". Advances in Experimental Medicine and Biology. Advances in Experimental Medicine and Biology. 309B: 121–4. doi:10.1007/978-1-4615-7703-4_27. ISBN 978-1-4615-7705-8. PMID 1840476.
- Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB (Oct 1991). "Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification". Human Genetics. 87 (6): 688–92. doi:10.1007/BF00201727. PMID 1937471.
- Tarlé SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD (Jun 1991). "Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects". Genomics. 10 (2): 499–501. doi:10.1016/0888-7543(91)90341-B. PMID 2071157.
- Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT (1991). "Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE)". Journal of Inherited Metabolic Disease. 13 (5): 692–700. doi:10.1007/BF01799570. PMID 2246854.
- Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W (Apr 1990). "Automated DNA sequencing of the human HPRT locus". Genomics. 6 (4): 593–608. doi:10.1016/0888-7543(90)90493-E. PMID 2341149.
- Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT (Jun 1990). "Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families". Genomics. 7 (2): 235–44. doi:10.1016/0888-7543(90)90545-6. PMID 2347587.
- Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ (Jun 1990). "Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures". Human Genetics. 85 (1): 111–6. doi:10.1007/BF00276334. PMID 2358296.
- Davidson BL, Tarlé SA, Palella TD, Kelley WN (Jul 1989). "Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts". The Journal of Clinical Investigation. 84 (1): 342–6. doi:10.1172/JCI114160. PMC 303988. PMID 2738157.
- Ogasawara N, Stout JT, Goto H, Sonta S, Matsumoto A, Caskey CT (Sep 1989). "Molecular analysis of a female Lesch-Nyhan patient". The Journal of Clinical Investigation. 84 (3): 1024–7. doi:10.1172/JCI114224. PMC 329751. PMID 2760209.
- Yang TP, Stout JT, Konecki DS, Patel PI, Alford RL, Caskey CT (May 1988). "Spontaneous reversion of novel Lesch-Nyhan mutation by HPRT gene rearrangement". Somatic Cell and Molecular Genetics. 14 (3): 293–303. doi:10.1007/BF01534590. PMID 2835825.
- Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN (May 1988). "Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor)". Human Genetics. 79 (1): 39–43. doi:10.1007/BF00291707. PMID 2896620.
- Davidson BL, Pashmforoush M, Kelley WN, Palella TD (Jan 1989). "Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville)". The Journal of Biological Chemistry. 264 (1): 520–5. PMID 2909537.
- Fujimori S, Davidson BL, Kelley WN, Palella TD (Jan 1989). "Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome". The Journal of Clinical Investigation. 83 (1): 11–3. doi:10.1172/JCI113846. PMC 303636. PMID 2910902.
External links
- Hypoxanthine phosphoribosyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
- Purine metabolism at genome.jp
- GeneReviews/NCBI/NIH/UW entry on Lesch-Nyhan Syndrome
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PDB gallery
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1bzy: HUMAN HGPRTASE WITH TRANSITION STATE INHIBITOR
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1d6n: TERNARY COMPLEX STRUCTURE OF HUMAN HGPRTASE, PRPP, MG2+, AND THE INHIBITOR HPP REVEALS THE INVOLVEMENT OF THE FLEXIBLE LOOP IN SUBSTRATE BINDING
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1hmp: THE CRYSTAL STRUCTURE OF HUMAN HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE WITH BOUND GMP
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| Purine metabolism |
| Anabolism |
| R5P→IMP: |
- Ribose-phosphate diphosphokinase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase
- AIR synthetase (FGAM cyclase)
- Phosphoribosylaminoimidazole carboxylase
- Phosphoribosylaminoimidazolesuccinocarboxamide synthase
- IMP synthase
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| IMP→AMP: |
- Adenylosuccinate synthase
- Adenylosuccinate lyase
- reverse
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| IMP→GMP: |
- IMP dehydrogenase
- GMP synthase
- reverse
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| Nucleotide salvage |
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenine phosphoribosyltransferase
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| Catabolism |
- Adenosine deaminase
- Purine nucleoside phosphorylase
- Guanine deaminase
- Xanthine oxidase
- Urate oxidase
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| Pyrimidine metabolism |
| Anabolism |
- CAD
- Carbamoyl phosphate synthase II
- Aspartate carbamoyltransferase
- Dihydroorotase
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- Dihydroorotate dehydrogenase
- Orotidine 5'-phosphate decarboxylase/Uridine monophosphate synthetase
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| Catabolism |
- 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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Transferases: glycosyltransferases (EC 2.4)
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2.4.1: Hexosyl-
transferases |
| Glucosyl- |
- Phosphorylase
- Glycogen synthase
- Debranching enzyme
- Branching enzyme
- 1,3-Beta-glucan synthase
- Ceramide glucosyltransferase
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| Galactosyl- |
- Lactose synthase
- B-N-acetylglucosaminyl-glycopeptide b-1,4-galactosyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase (C1GALT1)
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| Glucuronosyl- |
- 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- |
- POFUT1
- POFUT2
- FUT1
- FUT2
- FUT3
- FUT4
- FUT5
- FUT6
- FUT7
- FUT8
- FUT9
- FUT10
- FUT11
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| Mannosyl- |
- Dolichyl-phosphate-mannose-protein mannosyltransferase
- DPM1
- DPM3
- ALG1
- ALG2
- ALG3
- ALG6
- ALG8
- ALG9
- ALG12
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2.4.2: Pentosyl-
transferases |
| Ribose |
| ADP-ribosyltransferase |
- NAD+:diphthamide ADP-ribosyltransferase
- NAD(P)+:arginine ADP-ribosyltransferase
- Pertussis toxin
- Cholera toxin
- Poly ADP ribose polymerase
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| Phosphoribosyltransferase |
- Adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Uracil phosphoribosyltransferase
- Amidophosphoribosyltransferase
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| Other |
- Purine nucleoside phosphorylase: Thymidine phosphorylase
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| Other |
- 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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Enzymes
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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English Journal
- Human HPRT1 Gene and the Lesch-Nyhan Disease: Substitution of Alanine for Glycine and Inversely in the HGprt Enzyme Protein.
- Nguyen KV1,2, Naviaux RK1,2,3, Nyhan WL2.
- Nucleosides, nucleotides & nucleic acids.Nucleosides Nucleotides Nucleic Acids.2017 Jan 3:1-7. doi: 10.1080/15257770.2016.1231319. [Epub ahead of print]
- Lesch-Nyhan disease (LND) is a rare X-linked inherited neurogenetic disorder of purine metabolism in which the enzyme, hypoxanthine-guanine phosphoribosyltransferase (HGprt) is defective. The authors report three novel independent mutations in the coding region of the HPRT1 gene from genomic DNA of
- PMID 28045594
- Novel mutation in HPRT1 causing a splicing error with multiple variations.
- Baba S1, Saito T1, Yamada Y2, Takeshita E1, Nomura N2, Yamada K2, Wakamatsu N2, Sasaki M1.
- Nucleosides, nucleotides & nucleic acids.Nucleosides Nucleotides Nucleic Acids.2017 Jan 2;36(1):1-6. doi: 10.1080/15257770.2016.1163381. Epub 2016 Oct 18.
- Lesch-Nyhan disease (LND) is a rare X-linked recessive disorder caused by deficiency of the purine salvage enzyme hypoxanthine-guanine phosphoribosyltransferase (HPRT), encoded by the HPRT1. To date, nearly all types of mutations have been reported in the whole gene; however, duplication mutations a
- PMID 27754763
- Colonic microbiota can promote rapid local improvement of murine colitis by thioguanine independently of T lymphocytes and host metabolism.
- Oancea I1,2, Movva R1,2,3, Das I1, Aguirre de Cárcer D4, Schreiber V1,2, Yang Y1,5, Purdon A1,2, Harrington B1,2, Proctor M1,2, Wang R1,2, Sheng Y1,2, Lobb M6, Lourie R1,2, Ó Cuív P2,7, Duley JA4,6, Begun J1,2,8, Florin TH1,2,8.
- Gut.Gut.2017 Jan;66(1):59-69. doi: 10.1136/gutjnl-2015-310874. Epub 2016 Jul 13.
- OBJECTIVE: Mercaptopurine (MP) and pro-drug azathioprine are 'first-line' oral therapies for maintaining remission in IBD. It is believed that their pharmacodynamic action is due to a slow cumulative decrease in activated lymphocytes homing to inflamed gut. We examined the role of host metabolism, l
- PMID 27411368
Japanese Journal
- Genotoxicity of Acrylamide and Glycidamide : A Review of the Studies by HPRT Gene and TK Gene Mutation Assays
- AO Lin,CAO Jia
- Genes and environment : the official journal of the Japanese Environmental Mutagen Society 34(1), 1-8, 2012-02-20
- NAID 10030121669
- Urate nephropathy associated with impaired kinetic properties of hypoxanthine phosphoribosyl transferase in a 45-day-old infant
- SINGAL Rashi,KRISHNAMURTHY Sriram,NARAYANAN Parameswaran,RAJESH Nachiappa Ganesh,CHOUDHARY Bharat,JACOMELLI Gabriella,MICHELI Vanna
- Clinical and experimental nephrology 16(1), 164-167, 2012-02-01
- NAID 10030343288
Related Links
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- LightCycler® h-HPRT Housekeeping Gene Set ライトサイクラーインスツルメントでのh-HPRT mRNAの検出と定量的比較用のプライマー ... ヒポキサンチン-ホスフォリボシル-トランスフェラーゼ(HPRT) HPRT遺伝子は，本質的な発現 ...
Related Pictures
★リンクテーブル★
[★]
- 英
- hypoxanthine-guanine phosphoribosyltransferase HGPRT
- 同
- ヒポキサンチングアニンホスホリボシルトランスフェラーゼ,ヒポキサンチン-グアニンホスホリボシルトランスフェラーゼ
- ヒポキサンチンホスホリボシルトランスフェラーゼ hypoxanthine phosphoribosyltransferase, HPRT
- 関
- アデニンホスホリボシルトランスフェラーゼ APRT
- プリンヌクレオチド合成系路におけるサルベージ経路で機能する ⇔ de novo経路(リボース5-リン酸から始まるプリン合成系路)
- 以下の反応を触媒。
- ヒポキサンチン ＋ PRPP ←(HGPRT)→ IMP ＋ PPi
- グアニン ＋ PRPP ←(HGPRT)→ GMP ＋ PPi
- アデニン ＋ PRPP ←(APRT)→ AMP ＋ PPi
臨床関連
[★]
- 同
- hypoxanthine-guanine phosphoribosyltransferase
[★]