The gdhA1 point mutation in Escherichia coli K12 CLR207 alters a key lysine residue of glutamate dehydrogenase.
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.
Jones
K M
KM
Department of Genetics, University of Leeds, UK.
McPherson
M J
MJ
Baron
A J
AJ
Mattaj
I W
IW
Riordan
C L
CL
Wootton
J C
JC
D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005798:Genes, Bacterial; D005969:Glutamate Dehydrogenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D008239:Lysine / Q000235:genetics*; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D011995:Recombination, Genetic; D015183:Restriction Mapping
D004269:DNA, Bacterial; D005969:Glutamate Dehydrogenase; D008239:Lysine