PMID:8355660

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Citation

Jones, KM, McPherson, MJ, Baron, AJ, Mattaj, IW, Riordan, CL and Wootton, JC (1993) The gdhA1 point mutation in Escherichia coli K12 CLR207 alters a key lysine residue of glutamate dehydrogenase. Mol. Gen. Genet. 240:286-9

Abstract

gdhA1 is a spontaneous mutant of Escherichia coli that causes complete loss of activity of the NADP-specific glutamate dehydrogenase (GDH) encoded by the gdhA gene. The gdhA1 mutational site has been identified by recombinational mapping, polymerase chain reaction (PCR) amplification and DNA sequencing, as an A to G transition at nucleotide 274 of the gdhA coding sequence, resulting in an amino acid change of lysine 92 to glutamic acid. The mutant enzyme forms hybrid hexamers with a wild-type GDH, providing a useful system for analysis of conformational integrity of mutational variants.

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PubMed

Keywords

Base Sequence; Cloning, Molecular; DNA, Bacterial; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Glutamate Dehydrogenase/chemistry; Glutamate Dehydrogenase/genetics; Glutamate Dehydrogenase/metabolism; Lysine/genetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Polymerase Chain Reaction; Protein Conformation; Recombination, Genetic; Restriction Mapping

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