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Cloning and overproduction of biodegradative threonine deaminase from Escherichia coli W strain.“
Author(s) -
Hirose K.,
Fujita M.,
Takeuchi M.,
Yumoto N.,
Tokushige M.,
Kawata Y.
Publication year - 1992
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1992.tb00201.x
Subject(s) - escherichia coli , threonine , strain (injury) , biochemistry , peptide sequence , plasmid , nucleic acid sequence , biology , gene , amino acid , enzyme , chemistry , microbiology and biotechnology , serine , anatomy
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.