The lid domain is important, but not essential, for catalysis of Escherichia coli pyruvate kinase.

Sugrue, Elena; Coombes, David; Wood, David; Zhu, Tong; Donovan, Katherine A; Dobson, Renwick C J

Sugrue, Elena; Coombes, David; Wood, David; Zhu, Tong; Donovan, Katherine A; Dobson, Renwick C J.

Afiliación

Sugrue E; Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Coombes D; MRC-University of Glasgow Centre for Virus Research, Glasgow, G61 1QH, UK.
Wood D; Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Zhu T; Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Donovan KA; Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Dobson RCJ; Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.

Eur Biophys J ; 49(8): 761-772, 2020 Dec.

Article en En | MEDLINE | ID: mdl-32978636

Asunto(s)

Biocatálisis; Escherichia coli/enzimología; Piruvato Quinasa/química; Piruvato Quinasa/metabolismo; Cinética; Modelos Moleculares; Dominios Proteicos; Ingeniería de Proteínas; Piruvato Quinasa/genética

Palabras clave

Analytical ultracentrifugation; Enzyme evolution; Enzyme kinetics; Glycolysis; Protein engineering; Pyruvate kinase

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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Piruvato Quinasa / Escherichia coli / Biocatálisis Idioma: En Revista: Eur Biophys J Asunto de la revista: BIOFISICA Año: 2020 Tipo del documento: Article País de afiliación: Nueva Zelanda

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