Purification and properties of malyl-coenzyme A lyase from Pseudomonas AM1
| Autor: | J. R. Quayle, A. J. Hacking |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Stereochemistry
Malates Glyoxylate cycle Cleavage (embryo) Biochemistry Chromatography DEAE-Cellulose Bivalent (genetics) Pseudomonas Centrifugation Density Gradient Coenzyme A Magnesium Molecular Biology Equilibrium constant chemistry.chemical_classification biology Chemistry Oxo-Acid-Lyases Cobalt Cell Biology Hydrogen-Ion Concentration biology.organism_classification Lyase Molecular Weight Kinetics Electrophoresis Enzyme Enzymology Electrophoresis Polyacrylamide Gel Ultracentrifugation |
| Zdroj: | Biochemical Journal. 139:399-405 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj1390399 |
| Popis: | 1. Malyl-CoA lyase was purified 20-fold from extracts of methanol-grown Pseudomonas AM1. 2. Preparations of the enzyme were essentially homogeneous by electrophoretic and ultracentrifugal criteria. 3. Malyl-CoA lyase has a molecular weight of 190000 determined from sedimentation-equilibrium data. 4. Within the range of compounds tested, malyl-CoA lyase is specific for (2S)-4-malyl-CoA or glyoxylate and acetyl-CoA or propionyl-CoA. 5. A bivalent cation is essential for activity, Mg2+ or Co2+ being most effective. 6. Malyl-CoA lyase is inhibited by (2R)-4-malyl-CoA and by some buffers, but thiol-group inhibitors are without effect. 7. Optimal activity was recorded at pH7.8. 8. An equilibrium constant of 4.7×10−4m was determined for the malyl-CoA cleavage reaction. 9. The Michaelis constants for the enzyme are: 4-malyl-CoA, 6.6×10−5m; acetyl-CoA, 1.5×10−5m; glyoxylate, 1.7×10−3m; Mg2+, 1.2×10−3m. |
| Databáze: | OpenAIRE |
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