The gdhA1 point mutation in Escherichia coli K12 CLR207 alters a key lysine residue of glutamate dehydrogenase |
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Authors: | Kerrie M Jones Michael J McPherson Andrew J Baron Iain W Mattaj Claudia L Riordan John C Wootton |
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Institution: | 1. Department of Genetics, University of Leeds, LS29JT, Leeds, UK 2. Department of Biochemistry and Molecular Biology, University of Leeds, LS29JT, Leeds, UK
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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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