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
- Functionsidentical protein binding / triose-phosphate isomerase activityProcessesgluconeogenesis / glycolytic process / pentose-phosphate shunt
- General Function
- Triose-phosphate isomerase activity
- Specific Function
- Not Available
- Pfam Domain Function
- TIM (PF00121)
- 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
Resource Link UniProtKB ID Q07412 UniProtKB Entry Name TPIS_PLAFA GenBank Protein ID 160706 GenBank Gene ID L01654 - General References
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01709 2-phospho-D-glyceric acid experimental unknown Details DB01779 Glycerol 2-phosphate experimental unknown Details DB02515 sn-glycerol 3-phosphate experimental unknown Details DB02726 2-Phosphoglycolic Acid experimental unknown Details DB02951 3-Hydroxypyruvic Acid experimental unknown Details DB04510 3-phospho-D-glyceric acid experimental unknown Details