| http://purl.uniprot.org/citations/15158492 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15158492 | http://www.w3.org/2000/01/rdf-schema#comment | "The kinetics for the isomerization of fructose-6-phosphate to glucose-6-phosphate (F6P --> G6P) by baker's yeast phosphoglucose isomerase (PGI) with regard to k(cat) and K(m) were determined from analysis of differential stopped flow microcalorimeter measurements using the integrated form of the Michaelis-Menten rate equation. Values for K(m) (F6P --> G6P) that were determined at pH 8.0 and ionic strength 0.1M at 293.4, 298.4, 303.4, and 311.5K exhibited a linear dependence on the substrate concentration at each temperature because of the substrate-product equilibrium. The minimum values for K(m) ranged from 2.62+/-0.55 mM at 293.4K to 7.8+/-4.8mM at 311.5K and were the same as the minimum values for the reverse reaction (G6P --> F6P) at 293.4 K and 298.4 K. Minimum values for k(cat) increased with temperature, from 2.78+/-0.34s(-1) at 293.4K to 11.4+/-1.0s(-1) at 311.5K, and for the reverse reaction, G6P --> F6P, from 0.852+/-0.086 s(-1) at 293.4K to 1.46+/-0.06s(-1) at 298.4K. The enzyme efficiency at 311.5K is close to the collision rate for a diffusion-controlled process in solution. The [F6P]/[G6P] equilibrium constants were determined from comparison of the values of k(cat) in both directions and were 0.307+/-0.053 at 293.4K and 0.395+/-0.033 at 298.4K. The heats of reaction in the F6P --> G6P direction increased from -8.96+/-0.26 kJmol(-1) at 311.5K to -8.27+/-0.40 kJmol(-1) at 293.4K, a value in fair agreement with 7.01+/-0.32 kJmol(-1) in the opposite G6P --> F6P direction."xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.ab.2004.03.005"xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://purl.uniprot.org/core/author | "Schwarz F.P."xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://purl.uniprot.org/core/author | "Stodeman M."xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15158492 | http://purl.uniprot.org/core/name | "Anal Biochem"xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://purl.uniprot.org/core/pages | "307-315"xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://purl.uniprot.org/core/title | "Importance of product/reactant equilibration in the kinetics of the phosphoglucose isomerization reaction by differential stopped flow microcalorimetry."xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://purl.uniprot.org/core/volume | "329"xsd:string |
| http://purl.uniprot.org/citations/15158492 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15158492 |
| http://purl.uniprot.org/citations/15158492 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15158492 |
| http://purl.uniprot.org/uniprot/#_P12709-mappedCitation-15158492 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15158492 |
| http://purl.uniprot.org/uniprot/P12709 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15158492 |