Mechanism of proton abstraction in biotin-dependent carboxylation reactions
| Autor: | Irwin A. Rose, Donald J. Kuo |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
Reaction mechanism Stereochemistry Propionyl-CoA carboxylase General Chemistry complex mixtures Biochemistry Catalysis Solvent chemistry.chemical_compound Colloid and Surface Chemistry Enzyme Biotin chemistry Carboxylation Methylmalonyl-CoA lipids (amino acids peptides and proteins) Propionyl-CoA |
| Zdroj: | Journal of the American Chemical Society. 115:387-390 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja00055a003 |
| Popis: | Transcarboxylase (E-biotin) in T water is diluted into methylmalonyl CoA (MMCoA) in normal water to determine by isotope capture whether enzyme or solvent provides the proton required to form the product, propionyl CoA. The half-reaction E-biotin-methylmalonyl CoA... E-biotin-CO 2 .-propionyl CoA is followed, in the presence of pyruvate, by formation of oxalacetic acid and free propionyl CoA with regeneration of E-biotin, the three events required for another cycle of reaction with MMCoA |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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