Sequence of TPIS_PLAFA
EC Number:5.3.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
D-Glyceraldehyde 3-phosphate = glycerone phosphate
Other sequences found for EC No. 5.3.1.1
General information:
Sequence
0 MARKYFVAAN WKCNGTLESI KSLTNSFNNL DFDPSKLDVV VFPVSVHYDH TRKLLQSKFS
60 TGIQNVSKFG NGSYTGEVSA EIAKDLNIEY VIIGHFERRK YFHETDEDVR EKLQASLKNN
120 LKAVVCFGES LEQREQNKTI EVITKQVKAF VDLIDNFDNV ILAYEPLWAI GTGKTATPEQ
180 AQLVHKEIRK IVKDTCGEKQ ANQIRILYGG SVNTENCSSL IQQEDIDGFL VGNASLKESF
240 VDIIKSAM
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
494224
Ranie J.,Kumar V.P.,Balaram H.
Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli.
Mol. Biochem. Parasitol.
61
159-169
1993
494225
Velanker S.S.,Ray S.S.,Gokhale R.S.,Suma S.,Balaram H.,Balaram P.,Murthy M.R.N.
Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design.
Structure
5
751-761
1997
494226
Parthasarathy S.,Balaram H.,Balaram P.,Murthy M.R.N.
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
58
1992-2000
2002
494227
Parthasarathy S.,Ravindra G.,Balaram H.,Balaram P.,Murthy M.R.N.
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
41
13178-13188
2002
494228
Parthasarathy S.,Eaazhisai K.,Balaram H.,Balaram P.,Murthy M.R.N.
Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution.
J. Biol. Chem.
278
52461-52470
2003
494229
Eaazhisai K.,Balaram H.,Balaram P.,Murthy M.R.N.
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.
343
671-684
2004
494230
Gayathri P.,Banerjee M.,Vijayalakshmi A.,Balaram H.,Balaram P.,Murthy M.R.
Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.
Acta Crystallogr. D
65
847-857
2009
494231
Pareek V.,Samanta M.,Joshi N.V.,Balaram H.,Murthy M.R.,Balaram P.
Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme.
ChemBioChem
17
620-629
2016
