A distinct holoenzyme organization for two-subunit pyruvate carboxylase
Pyruvate carboxylases are homotetrameric enzymes in eukaryotes and most bacteria. Here, the authors report the structure of an unusual two-subunit form of the enzyme from the Gram-negative bacterium Methylobacillus flagellates, revealing an unexpected α2β4stoichiometry.
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Autores principales: | , , , , , , |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2016
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Materias: | |
Acceso en línea: | https://doaj.org/article/e289b0f367274707a7bceab080bc093b |
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Sumario: | Pyruvate carboxylases are homotetrameric enzymes in eukaryotes and most bacteria. Here, the authors report the structure of an unusual two-subunit form of the enzyme from the Gram-negative bacterium Methylobacillus flagellates, revealing an unexpected α2β4stoichiometry. |
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