| http://purl.uniprot.org/citations/26762569 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26762569 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26762569 | http://www.w3.org/2000/01/rdf-schema#comment | "Despite extensive research into triosephosphate isomerases (TIMs), there exists a gap in understanding of the remarkable conjunction between catalytic loop-6 (residues 166-176) movement and the conformational flip of Glu165 (catalytic base) upon substrate binding that primes the active site for efficient catalysis. The overwhelming occurrence of serine at position 96 (98% of the 6277 unique TIM sequences), spatially proximal to E165 and the loop-6 residues, raises questions about its role in catalysis. Notably, Plasmodium falciparum TIM has an extremely rare residue--phenylalanine--at this position whereas, curiously, the mutant F96S was catalytically defective. We have obtained insights into the influence of residue 96 on the loop-6 conformational flip and E165 positioning by combining kinetic and structural studies on the PfTIM F96 mutants F96Y, F96A, F96S/S73A, and F96S/L167V with sequence conservation analysis and comparative analysis of the available apo and holo structures of the enzyme from diverse organisms."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.org/dc/terms/identifier | "doi:10.1002/cbic.201500532"xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.org/dc/terms/identifier | "doi:10.1002/cbic.201500532"xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Samanta M."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Samanta M."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Murthy M.R."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Murthy M.R."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Balaram H."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Balaram H."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Balaram P."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Balaram P."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Joshi N.V."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Joshi N.V."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Pareek V."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/author | "Pareek V."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/name | "ChemBioChem"xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/name | "ChemBioChem"xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/pages | "620-629"xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/pages | "620-629"xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/title | "Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme."xsd:string |
| http://purl.uniprot.org/citations/26762569 | http://purl.uniprot.org/core/title | "Connecting Active-Site Loop Conformations and Catalysis in Triosephosphate Isomerase: Insights from a Rare Variation at Residue 96 in the Plasmodial Enzyme."xsd:string |