Triosephosphate isomerase

NameTriosephosphate isomerase
Synonyms
  • 5.3.1.1
  • TIM
  • Triose-phosphate isomerase
Gene NameTPI
OrganismPlasmodium falciparum
Amino acid sequence
>lcl|BSEQ0019091|Triosephosphate isomerase
MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFS
TGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNN
LKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQ
AQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESF
VDIIKSAM
Number of residuesNone
Molecular Weight27934.505
Theoretical pI6.37
GO Classification
Functions
  • triose-phosphate isomerase activity
  • identical protein binding
Processes
  • pentose-phosphate shunt
  • gluconeogenesis
  • glycolytic process
Components
General FunctionTriose-phosphate isomerase activity
Specific FunctionNone
Transmembrane Regions
GenBank Protein ID
UniProtKB IDQ07412
UniProtKB Entry Name
Cellular LocationNone
Gene sequence
>lcl|BSEQ0002499|747 bp
ATGGCTAGAAAATATTTTGTCGCAGCAAACTGGAAATGTAATGGAACTTTAGAAAGTATT
AAATCTTTAACAAACAGTTTTAACAATTTGGATTTTGATCCAAGCAAATTAGACGTTGTT
GTTTTTCCTGTTTCCGTACATTATGATCATACAAGGAAATTACTTCAGAGTAAGTTTTCT
ACTGGTATTCAGAATGTATCAAAATTCGGAAATGGATCATACACAGGTGAAGTAAGTGCA
GAAATTGCCAAGGATTTAAATATTGAATATGTTATTATTGGTCATTTTGAAAGAAGAAAA
TATTTCCATGAAACCGATGAAGATGTTCGTGAAAAATTACAAGCTTCATTAAAAAATAAT
TTAAAAGCCGTTGTATGTTTTGGTGAATCTTTAGAACAAAGAGAACAAAATAAAACTATC
GAAGTTATTACAAAACAAGTTAAAGCATTTGTTGATTTAATTGATAATTTTGATAATGTT
ATTTTGGCTTATGAACCTTTATGGGCTATTGGTACTGGTAAAACAGCTACACCTGAACAA
GCTCAATTAGTACACAAAGAAATCAGAAAAATTGTAAAAGATACATGCGGAGAAAAACAA
GCTAACCAAATAAGAATATTATATGGAGGTAGTGTTAATACTGAAAACTGCTCTTCATTA
ATTCAACAAGAAGATATTGATGGTTTCTTAGTTGGAAATGCTTCCTTAAAAGAATCTTTT
GTTGATATAATAAAAAGTGCTATGTAA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Ranie J, Kumar VP, Balaram H: Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli. Mol Biochem Parasitol. 1993 Oct;61(2):159-69. [7903426 ]
  2. Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR: Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. Structure. 1997 Jun 15;5(6):751-61. [9261072 ]
  3. Parthasarathy S, Balaram H, Balaram P, Murthy MR: Structures of Plasmodium falciparum triosephosphate isomerase complexed to substrate analogues: observation of the catalytic loop in the open conformation in the ligand-bound state. Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):1992-2000. Epub 2002 Nov 23. [12454456 ]
  4. Parthasarathy S, Ravindra G, Balaram H, Balaram P, Murthy MR: Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state. Biochemistry. 2002 Nov 5;41(44):13178-88. [12403619 ]
  5. Parthasarathy S, Eaazhisai K, Balaram H, Balaram P, Murthy MR: Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution. J Biol Chem. 2003 Dec 26;278(52):52461-70. Epub 2003 Oct 16. [14563846 ]
  6. Eaazhisai K, Balaram H, Balaram P, Murthy MR: Structures of unliganded and inhibitor complexes of W168F, a Loop6 hinge mutant of Plasmodium falciparum triosephosphate isomerase: observation of an intermediate position of loop6. J Mol Biol. 2004 Oct 22;343(3):671-84. [15465054 ]

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