Cloning and overproduction of biodegradative threonine deaminase from Escherichia coli W strain.
We have cloned the structural gene (tdcB) of biodegradative threonine deaminase from Escherichia coli W strain by utilizing the polymerase chain reaction. The JM109/pUCTDA strain, which was obtained by transforming E. coli JM109 with a vector plasmid (pUCTDA) containing the cloned tdcB gene, produced a large amount of the enzyme corresponding to more than 5% of the total soluble protein. Amino acid sequence analysis of this recombinant enzyme showed that the amino acid sequence is identical to the nucleotide-deduced sequence of biodegradative threonine deaminase from E. coli K-12.
Hirose
K
K
Department of Chemistry, Faculty of Science, Kyoto University, Japan.
Fujita
M
M
Takeuchi
M
M
Yumoto
N
N
Tokushige
M
M
Kawata
Y
Y
D000595:Amino Acid Sequence; D001483:Base Sequence; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D013913:Threonine Dehydratase / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*
D013913:Threonine Dehydratase