The gdhA1 point mutation in Escherichia coli K12 CLR207 alters a key lysine residue of glutamate dehydrogenase

Mol Gen Genet. 1993 Aug;240(2):286-9. doi: 10.1007/BF00277068.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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

Substances

  • DNA, Bacterial
  • Glutamate Dehydrogenase
  • Lysine