PMID:2647748
| Citation |
Aronson, BD, Somerville, RL, Epperly, BR and Dekker, EE (1989) The primary structure of Escherichia coli L-threonine dehydrogenase. J. Biol. Chem. 264:5226-32 |
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| Abstract |
The complete primary structures of Escherichia coli L-threonine dehydrogenase has been deduced by sequencing the cloned tdh gene. The primary structure so determined agrees with results obtained independently for the amino acid composition, the N-terminal amino acid sequence (20 residues), and a short sequence at the end of an internal peptide of the purified enzyme. The presence of a predicted Asp-Pro bond at residues 148 and 149 was confirmed by treatment of purified threonine dehydrogenase with dilute acid and subsequent analysis of the resulting cleavage products. The primary structure of L-threonine dehydrogenase from E. coli has been examined for possible homology to other NAD+-dependent dehydrogenases; indications are that this enzyme is a member of the zinc-containing long-chain alcohol/polyol dehydrogenase family. |
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| Keywords |
Acids; Alcohol Oxidoreductases/genetics; Alcohol Oxidoreductases/isolation & purification; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Base Sequence; Escherichia coli/enzymology; Escherichia coli/genetics; Genes; Genes, Bacterial; Hydrolysis; Molecular Sequence Data; Peptide Fragments/isolation & purification; Sequence Homology, Nucleic Acid |
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