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Showing Protein Triosephosphate isomerase (HMDBP13064)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP13064
Secondary Accession Numbers None
Name Triosephosphate isomerase
Synonyms
  1. TIM
  2. Methylglyoxal synthase
  3. Triose-phosphate isomerase
Gene Name TPI1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids.
Pathways
  • Biosynthesis of amino acids
  • Carbon metabolism
  • Fructose and mannose metabolism
  • gluconeogenesis
  • glycolysis
  • Glycolysis / Gluconeogenesis
  • Inositol phosphate metabolism
Reactions Not Available
GO Classification
Biological Process
gluconeogenesis
multicellular organismal development
glycolysis
methylglyoxal biosynthetic process
glyceraldehyde-3-phosphate biosynthetic process
Cellular Component
cytoplasm
Molecular Function
protein homodimerization activity
triose-phosphate isomerase activity
ubiquitin protein ligase binding
methylglyoxal synthase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 249
Molecular Weight 26756.45
Theoretical pI 7.331
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P00939
UniProtKB/Swiss-Prot Entry Name TPIS_RABIT
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Lindblad-Toh K, Garber M, Zuk O, Lin MF, Parker BJ, Washietl S, Kheradpour P, Ernst J, Jordan G, Mauceli E, Ward LD, Lowe CB, Holloway AK, Clamp M, Gnerre S, Alfoldi J, Beal K, Chang J, Clawson H, Cuff J, Di Palma F, Fitzgerald S, Flicek P, Guttman M, Hubisz MJ, Jaffe DB, Jungreis I, Kent WJ, Kostka D, Lara M, Martins AL, Massingham T, Moltke I, Raney BJ, Rasmussen MD, Robinson J, Stark A, Vilella AJ, Wen J, Xie X, Zody MC, Baldwin J, Bloom T, Chin CW, Heiman D, Nicol R, Nusbaum C, Young S, Wilkinson J, Worley KC, Kovar CL, Muzny DM, Gibbs RA, Cree A, Dihn HH, Fowler G, Jhangiani S, Joshi V, Lee S, Lewis LR, Nazareth LV, Okwuonu G, Santibanez J, Warren WC, Mardis ER, Weinstock GM, Wilson RK, Delehaunty K, Dooling D, Fronik C, Fulton L, Fulton B, Graves T, Minx P, Sodergren E, Birney E, Margulies EH, Herrero J, Green ED, Haussler D, Siepel A, Goldman N, Pollard KS, Pedersen JS, Lander ES, Kellis M: A high-resolution map of human evolutionary constraint using 29 mammals. Nature. 2011 Oct 12;478(7370):476-82. doi: 10.1038/nature10530. [PubMed:21993624 ]
  2. Corran PH, Waley SG: The amino acid sequence of rabbit muscle triose phosphate isomerase. Biochem J. 1975 Feb;145(2):335-44. doi: 10.1042/bj1450335. [PubMed:1171682 ]
  3. Putney SD, Herlihy WC, Schimmel P: A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing. Nature. 1983 Apr 21;302(5910):718-21. doi: 10.1038/302718a0. [PubMed:6687628 ]
  4. Hartman FC: Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomerase. Biochemistry. 1971 Jan 5;10(1):146-54. doi: 10.1021/bi00777a021. [PubMed:4922541 ]
  5. Sun AQ, Yuksel KU, Gracy RW: Terminal marking of triosephosphate isomerase: consequences of deamidation. Arch Biochem Biophys. 1995 Oct 1;322(2):361-8. doi: 10.1006/abbi.1995.1476. [PubMed:7574709 ]
  6. Aparicio R, Ferreira ST, Polikarpov I: Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. J Mol Biol. 2003 Dec 12;334(5):1023-41. doi: 10.1016/j.jmb.2003.10.022. [PubMed:14643664 ]