Triosephosphate isomerase, glycosomal


NameTriosephosphate isomerase, glycosomal
Synonyms
  • 5.3.1.1
  • TIM
Gene NameNone
OrganismTrypanosoma brucei brucei
Amino acid sequence
>lcl|BSEQ0017682|Triosephosphate isomerase, glycosomal
MSKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMTKERLSHPKF
VIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAYYGETNEIVADKVAAAVASG
FMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADWAKVVIAYEPVWAIGTGKVATP
QQAQEAHALIRSWVSSKIGADVAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKP
EFVDIIKATQ
Number of residues250
Molecular Weight26834.665
Theoretical pINone
GO Classification
Functions
  • triose-phosphate isomerase activity
Processes
  • pentose-phosphate shunt
  • gluconeogenesis
  • glycolytic process
Components
  • glycosome
General FunctionTriose-phosphate isomerase activity
Specific FunctionNone
Transmembrane Regions
GenBank Protein ID
UniProtKB IDP04789
UniProtKB Entry NameTPIS_TRYBB
Cellular LocationGlycosome
Gene sequence
None
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Swinkels BW, Gibson WC, Osinga KA, Kramer R, Veeneman GH, van Boom JH, Borst P: Characterization of the gene for the microbody (glycosomal) triosephosphate isomerase of Trypanosoma brucei. EMBO J. 1986 Jun;5(6):1291-8.[3015595 ]
  2. Borst P: How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes). Biochim Biophys Acta. 1986 May 5;866(4):179-203.[3516224 ]
  3. Wierenga RK, Kalk KH, Hol WG: Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution. J Mol Biol. 1987 Nov 5;198(1):109-21.[3430602 ]
  4. Wierenga RK, Noble ME, Vriend G, Nauche S, Hol WG: Refined 1.83 A structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex. J Mol Biol. 1991 Aug 20;220(4):995-1015.[1880808 ]
  5. Noble ME, Wierenga RK, Lambeir AM, Opperdoes FR, Thunnissen AM, Kalk KH, Groendijk H, Hol WG: The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes. Proteins. 1991;10(1):50-69.[2062828 ]
  6. Wierenga RK, Noble ME, Davenport RC: Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J Mol Biol. 1992 Apr 20;224(4):1115-26.[1569570 ]
  7. Borchert TV, Pratt K, Zeelen JP, Callens M, Noble ME, Opperdoes FR, Michels PA, Wierenga RK: Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant. Eur J Biochem. 1993 Feb 1;211(3):703-10.[8436128 ]
  8. Borchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK: Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8. Structure. 1995 Jul 15;3(7):669-79.[8591044 ]
  9. Kursula I, Partanen S, Lambeir AM, Wierenga RK: The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis. FEBS Lett. 2002 May 8;518(1-3):39-42.[11997014 ]

From www.t3db.ca