In vivo effect of GroESL on the folding of glutamate racemase of Escherichia coli.
The overexpression of the murI (glr) gene, which encodes the glutamate racemase of Escherichia coli, resulted in the formation of inclusion bodies of the enzyme, and little activity was found in the soluble fraction of the transformant cells. The coexpression of the groESL gene with murI caused an in vivo solubilization of glutamate racemase in an active form. We isolated the active enzyme and purified it effectively.
Ashiuchi
M
M
Institute for Chemical Research, Kyoto University.
Yoshimura
T
T
Kitamura
T
T
Kawata
Y
Y
Nagai
J
J
Gorlatov
S
S
Esaki
N
N
Soda
K
K
D000591:Amino Acid Isomerases / Q000235:genetics*; D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology*; D005798:Genes, Bacterial; D005822:Genetic Vectors; D008969:Molecular Sequence Data; D017510:Protein Folding; D012995:Solubility
D000591:Amino Acid Isomerases; C062292:glutamate racemase