Pyruvate Carboxylase: Mechanisms of the Partial Reactions
| Autor: | Nelson F. B. Phillips, D. Bruce Keech, Mark A. Snoswell, Gregory J. Goodall, Paul V. Attwood, John C. Wallace |
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| Rok vydání: | 1985 |
| Předmět: |
Pyruvate decarboxylation
Pyruvate dehydrogenase kinase Stereochemistry Biotin Pyruvate dehydrogenase phosphatase General Biochemistry Genetics and Molecular Biology Adenosine Triphosphate History and Philosophy of Science Acetyl Coenzyme A Pyruvic Acid Animals Magnesium Binding site Dihydrolipoyl transacetylase Pyruvates Pyruvate Carboxylase Binding Sites Sheep Chemistry General Neuroscience Pyruvate dehydrogenase complex Pyruvate carboxylase Adenosine Diphosphate Kinetics Models Chemical Phosphoenolpyruvate carboxylase |
| Zdroj: | Annals of the New York Academy of Sciences. 447:169-188 |
| ISSN: | 1749-6632 0077-8923 |
| DOI: | 10.1111/j.1749-6632.1985.tb18436.x |
| Popis: | Data from isotopic exchange studies and from experiments with 32P- and 14C-labeled enzyme-bound intermediates support the following description of the first partial reaction: (Formula: see text). From studies of the transfer of the carboxyl-group from ENZ-biotin-CO2- to pyruvate or its analogues we propose that binding of the acceptor substrate induces the translation of carboxybiotin from the first to the second partial reaction site. The studies on the translocation of carboxybiotin can be summarized in the following reaction scheme: (Formula: see text). Where k+3 less than k+1, k-1, k+2 and k-2. Thus, the rate-limited step is governed by k+3 which represents the movement of carboxybiotin from the first subsite to the second. |
| Databáze: | OpenAIRE |
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