Properties of Malic Enzyme from the Aerobic Methanotroph Methylosinus trichosporium
| Autor: | Olga N. Rozova, Ildar I. Mustakhimov, Valentina N. Khmelenina, S. Y. But, Yu. A. Trotsenko |
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| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
biology Chemistry Decarboxylation Malic enzyme General Medicine Biochemistry Methylosinus trichosporium Recombinant Proteins Cofactor Kinetics Enzyme Carboxylation Malate Dehydrogenase Pyruvic Acid Biocatalysis biology.protein Enzyme kinetics Heterologous expression NADP Oxidative decarboxylation |
| Zdroj: | Biochemistry (Moscow). 84:390-397 |
| ISSN: | 1608-3040 0006-2979 |
| DOI: | 10.1134/s0006297919040060 |
| Popis: | Recombinant malic enzyme from the aerobic methanotroph Methylosinus trichosporium was obtained by heterologous expression in Escherichia coli and purified by affinity metal-chelating chromatography. The homohexameric enzyme of 6×80 kDa catalyzed the reversible reaction of oxidative decarboxylation of malate to pyruvate in the presence of mono- and divalent cations and NADP+ as a cofactor. The kcat/Km ratio indicated much higher catalytic efficiency of the malate decarboxylation reaction as compared with the pyruvate carboxylation reaction. Analysis of the protein sequence revealed that the C-region of the enzyme contains a large domain homologous to phosphoacetyltransferase, but no phosphoacetyl-transferase activity was detected either for a full chimeric malic enzyme or for the C-end fragment obtained as a separate protein. This C-end domain promoted activity of the malic enzyme. |
| Databáze: | OpenAIRE |
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