| http://purl.uniprot.org/citations/20822141 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20822141 | http://www.w3.org/2000/01/rdf-schema#comment | "The K12G mutation at yeast triosephosphate isomerase (TIM) results in a 5.5 × 10(5)-fold decrease in k(cat)/K(m) for isomerization of glyceraldehyde 3-phosphate, and the activity of this mutant can be successfully "rescued" by NH(4)(+) and primary alkylammonium cations. The transition state for the K12G mutant TIM-catalyzed reaction is stabilized by 1.5 kcal/mol by interaction with NH(4)(+). The larger 3.9 kcal/mol stabilization by CH(3)CH(2)CH(2)CH(2)NH(3)(+) is due to hydrophobic interactions between the mutant enzyme and the butyl side chain of the cation activator. There is no significant transfer of a proton from alkylammonium cations to GAP at the transition state for the K12G mutant TIM-catalyzed reaction, because activation by a series of RNH(3)(+) shows little or no dependence on the pK(a) of RNH(3)(+). A comparison of k(cat)/K(m) = 6.6 × 10(6) M(-1) s(-1) for the wildtype TIM-catalyzed isomerization of GAP and the third-order rate constant of 150 M(-2) s(-1) for activation by NH(4)(+) of the K12G mutant TIM-catalyzed isomerization shows that stabilization of the bound transition state by the effectively intramolecular interaction of the cationic side chain of Lys-12 at wildtype TIM is 6.3 kcal/mol greater than that for the corresponding intermolecular interaction of NH(4)(+) at K12G mutant TIM."xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.org/dc/terms/identifier | "doi:10.1021/ja106104h"xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/author | "Go M.K."xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/author | "Richard J.P."xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/author | "Amyes T.L."xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/name | "J Am Chem Soc"xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/pages | "13525-13532"xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/title | "Rescue of K12G triosephosphate isomerase by ammonium cations: the reaction of an enzyme in pieces."xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://purl.uniprot.org/core/volume | "132"xsd:string |
| http://purl.uniprot.org/citations/20822141 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20822141 |
| http://purl.uniprot.org/citations/20822141 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20822141 |
| http://purl.uniprot.org/uniprot/#_P00942-mappedCitation-20822141 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20822141 |
| http://purl.uniprot.org/uniprot/P00942 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20822141 |