TPI1
From Wikipedia, the free encyclopedia
| Triosephosphate isomerase 1 | |||||||||||||
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 PDB rendering based on 1hti. | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | TPI1; TIM; TPI | ||||||||||||
| External IDs | OMIM: 190450 MGI: 98797 HomoloGene: 128432 ChEMBL: 4880 GeneCards: TPI1 Gene | ||||||||||||
| EC number | 5.3.1.1 | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 7167 | 21991 | |||||||||||
| Ensembl | ENSG00000111669 | ENSMUSG00000023456 | |||||||||||
| UniProt | P60174 | P17751 | |||||||||||
| RefSeq (mRNA) | NM_000365 | NM_009415 | |||||||||||
| RefSeq (protein) | NP_000356 | NP_033441 | |||||||||||
| Location (UCSC) | Chr 12: 6.98 – 6.98 Mb | Chr 6: 124.81 – 124.81 Mb | |||||||||||
| PubMed search | |||||||||||||
Triosephosphate isomerase is an enzyme that in humans is encoded by the TPI1 gene.[1]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
Glycolysis and Gluconeogenesis edit
- ↑ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Abnormal |
| Recessive lethal study | Abnormal |
| Fertility | Normal |
| Body weight | Normal |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Plasma immunoglobulins | Normal |
| Haematology | Normal |
| Peripheral blood lymphocytes | Normal |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Skin Histopathology | Normal |
| Brain histopathology | Normal |
| Salmonella infection | Abnormal[2] |
| Citrobacter infection | Normal[3] |
| All tests and analysis from[4] [5] |
Model organisms have been used in the study of TPI1 function. A conditional knockout mouse line, called Tpi1tm1a(EUCOMM)Wtsi[6][7] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[8][9][10]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty six tests were carried out on mutant mice and three significant abnormalities were observed.[4] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and an increased susceptibility to bacterial infection was observed in male animals.[4]
See also
References
- ↑ "Entrez Gene: TPI1 triosephosphate isomerase 1".
- ↑ "Salmonella infection data for Tpi1". Wellcome Trust Sanger Institute.
- ↑ "Citrobacter infection data for Tpi1". Wellcome Trust Sanger Institute.
- ↑ 4.0 4.1 4.2 4.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ↑ "International Knockout Mouse Consortium".
- ↑ "Mouse Genome Informatics".
- ↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
Further reading
- Ationu A, Humphries A (1999). "The feasibility of replacement therapy for inherited disorder of glycolysis: triosephosphate isomerase deficiency (review).". Int. J. Mol. Med. 2 (6): 701–4. PMID 9850739.
- Oláh J, Orosz F, Keserü GM, et al. (2002). "Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease.". Biochem. Soc. Trans. 30 (2): 30–8. doi:10.1042/BST0300030. PMID 12023819.
- Rethoré MO, Kaplan JC, Junien C, Lejeune J (1977). "12pter to 12p12.2: possible assignment of human triose phosphate isomerase.". Hum. Genet. 36 (2): 235–7. doi:10.1007/BF00273263. PMID 858628.
- Perry BA, Mohrenweiser HW (1992). "Human triosephosphate isomerase: substitution of Arg for Gly at position 122 in a thermolabile electromorph variant, TPI-Manchester.". Hum. Genet. 88 (6): 634–8. doi:10.1007/BF02265287. PMID 1339398.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- Boyer TG, Maquat LE (1990). "Minimal sequence and factor requirements for the initiation of transcription from an atypical, TATATAA box-containing housekeeping promoter.". J. Biol. Chem. 265 (33): 20524–32. PMID 2243103.
- Maquat LE, Chilcote R, Ryan PM (1985). "Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man.". J. Biol. Chem. 260 (6): 3748–53. PMID 2579079.
- Daar IO, Artymiuk PJ, Phillips DC, Maquat LE (1986). "Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme.". Proc. Natl. Acad. Sci. U.S.A. 83 (20): 7903–7. doi:10.1073/pnas.83.20.7903. PMC 386831. PMID 2876430.
- Boyer TG, Krug JR, Maquat LE (1989). "Transcriptional regulatory sequences of the housekeeping gene for human triosephosphate isomerase.". J. Biol. Chem. 264 (9): 5177–87. PMID 2925688.
- Brown JR, Daar IO, Krug JR, Maquat LE (1985). "Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family.". Mol. Cell. Biol. 5 (7): 1694–706. PMC 367288. PMID 4022011.
- Lu HS, Yuan PM, Gracy RW (1984). "Primary structure of human triosephosphate isomerase.". J. Biol. Chem. 259 (19): 11958–68. PMID 6434534.
- Mande SC, Mainfroid V, Kalk KH, et al. (1994). "Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme.". Protein Sci. 3 (5): 810–21. doi:10.1002/pro.5560030510. PMC 2142725. PMID 8061610.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Chang ML, Artymiuk PJ, Wu X, et al. (1993). "Human triosephosphate isomerase deficiency resulting from mutation of Phe-240.". Am. J. Hum. Genet. 52 (6): 1260–9. PMC 1682273. PMID 8503454.
- Watanabe M, Zingg BC, Mohrenweiser HW (1996). "Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus.". Am. J. Hum. Genet. 58 (2): 308–16. PMC 1914533. PMID 8571957.
- Mainfroid V, Terpstra P, Beauregard M, et al. (1996). "Three hTIM mutants that provide new insights on why TIM is a dimer.". J. Mol. Biol. 257 (2): 441–56. doi:10.1006/jmbi.1996.0174. PMID 8609635.
- Ansari-Lari MA, Muzny DM, Lu J, et al. (1996). "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13.". Genome Res. 6 (4): 314–26. doi:10.1101/gr.6.4.314. PMID 8723724.
- Ansari-Lari MA, Shen Y, Muzny DM, et al. (1997). "Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination.". Genome Res. 7 (3): 268–80. doi:10.1101/gr.7.3.268. PMID 9074930.
- Rasmussen RK, Ji H, Eddes JS, et al. (1997). "Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2.". Electrophoresis 18 (3-4): 588–98. doi:10.1002/elps.1150180342. PMID 9150946.
- Ji H, Reid GE, Moritz RL, et al. (1997). "A two-dimensional gel database of human colon carcinoma proteins.". Electrophoresis 18 (3-4): 605–13. doi:10.1002/elps.1150180344. PMID 9150948.
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