Triosephosphate isomerase

Details

Name
Triosephosphate isomerase
Synonyms
  • 5.3.1.1
  • TIM
  • Triose-phosphate isomerase
Gene Name
TPI
Organism
Plasmodium falciparum
Amino acid sequence
>lcl|BSEQ0019091|Triosephosphate isomerase
MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFS
TGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNN
LKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQ
AQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESF
VDIIKSAM
Number of residues
248
Molecular Weight
27934.505
Theoretical pI
6.37
GO Classification
Functions
identical protein binding / triose-phosphate isomerase activity
Processes
gluconeogenesis / glycolytic process / pentose-phosphate shunt
General Function
Triose-phosphate isomerase activity
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0002499|747 bp
ATGGCTAGAAAATATTTTGTCGCAGCAAACTGGAAATGTAATGGAACTTTAGAAAGTATT
AAATCTTTAACAAACAGTTTTAACAATTTGGATTTTGATCCAAGCAAATTAGACGTTGTT
GTTTTTCCTGTTTCCGTACATTATGATCATACAAGGAAATTACTTCAGAGTAAGTTTTCT
ACTGGTATTCAGAATGTATCAAAATTCGGAAATGGATCATACACAGGTGAAGTAAGTGCA
GAAATTGCCAAGGATTTAAATATTGAATATGTTATTATTGGTCATTTTGAAAGAAGAAAA
TATTTCCATGAAACCGATGAAGATGTTCGTGAAAAATTACAAGCTTCATTAAAAAATAAT
TTAAAAGCCGTTGTATGTTTTGGTGAATCTTTAGAACAAAGAGAACAAAATAAAACTATC
GAAGTTATTACAAAACAAGTTAAAGCATTTGTTGATTTAATTGATAATTTTGATAATGTT
ATTTTGGCTTATGAACCTTTATGGGCTATTGGTACTGGTAAAACAGCTACACCTGAACAA
GCTCAATTAGTACACAAAGAAATCAGAAAAATTGTAAAAGATACATGCGGAGAAAAACAA
GCTAACCAAATAAGAATATTATATGGAGGTAGTGTTAATACTGAAAACTGCTCTTCATTA
ATTCAACAAGAAGATATTGATGGTTTCTTAGTTGGAAATGCTTCCTTAAAAGAATCTTTT
GTTGATATAATAAAAAGTGCTATGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ07412
UniProtKB Entry NameTPIS_PLAFA
GenBank Protein ID160706
GenBank Gene IDL01654
General 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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed: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. [PubMed:15465054]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB017092-phospho-D-glyceric acidexperimentalunknownDetails
DB01779Glycerol-2-PhosphateexperimentalunknownDetails
DB025153-PhosphoglycerolexperimentalunknownDetails
DB027262-Phosphoglycolic AcidexperimentalunknownDetails
DB029513-Hydroxypyruvic AcidexperimentalunknownDetails
DB045103-phospho-D-glyceric acidexperimentalunknownDetails