Overproduction of the pyruvate dehydrogenase multienzyme complex of Escherichia coli and site-directed substitutions in the E1p and E2p subunits.

Russell, G C; Machado, R S; Guest, J R

Russell, G C; Machado, R S; Guest, J R.

Affiliation

Russell GC; Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, U.K.

Biochem J ; 287 ( Pt 2): 611-9, 1992 Oct 15.

Article in En | MEDLINE | ID: mdl-1445221

Subject(s)

Acetyltransferases/genetics; Bacterial Proteins/genetics; Escherichia coli/enzymology; Pyruvate Dehydrogenase Complex/genetics; Bacterial Proteins/biosynthesis; Bacterial Proteins/isolation & purification; Base Sequence; Dihydrolipoyllysine-Residue Acetyltransferase; Enzyme Induction; Escherichia coli/genetics; Gene Deletion; Gene Expression/genetics; Genes, Bacterial/genetics; Isopropyl Thiogalactoside/pharmacology; Macromolecular Substances; Molecular Sequence Data; Mutagenesis, Site-Directed; Plasmids/genetics; Pyruvate Dehydrogenase Complex/biosynthesis; Pyruvate Dehydrogenase Complex/isolation & purification

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Pyruvate Dehydrogenase Complex / Acetyltransferases / Bacterial Proteins / Escherichia coli Language: En Journal: Biochem J Year: 1992 Document type: Article Affiliation country: United kingdom Country of publication: United kingdom

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