Purification and Characterization of the 2-Oxoglutarate Dehydrogenase Complex from Dictyostelium discoideum
| Autor: | Barbara E. Wright, Jacqueline M. Reimers, Leslie L. Heckert, Kathy R. Albe, Margaret Husta Butler |
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| Rok vydání: | 1989 |
| Předmět: |
chemistry.chemical_classification
biology Nucleotides fungi Kinetics Ketone Oxidoreductases Mycetozoa biology.organism_classification Microbiology Dictyostelium discoideum Enzyme assay Citric acid cycle Enzyme chemistry Biochemistry biology.protein Dictyostelium Ketoglutarate Dehydrogenase Complex NAD+ kinase Oxoglutarate dehydrogenase complex |
| Zdroj: | Microbiology. 135:155-161 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/00221287-135-1-155 |
| Popis: | The 2-oxoglutarate dehydrogenase complex was isolated from the cellular slime mould, Dictyostelium discoideum, and purified 113-fold. The enzyme exhibited Michaelis-Menten kinetics and the Km values for 2-oxoglutarate, CoA, and NAD were 1.0 mM, 0.002 mM, and 0.07 mM, respectively. The Ki value for succinyl-CoA was determined to be 0.004 mM and the Ki for NADH was 0.018 mM. AMP had positive effects whereas ATP had negative effects on the enzyme activity. The kinetic constants determined in this study and the reaction mechanism suggested can now be incorporated into a transition model of the tricarboxylic acid cycle during differentiation of D. discoideum. |
| Databáze: | OpenAIRE |
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