The primary structure of Escherichia coli L-threonine dehydrogenase.
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.
Aronson
B D
BD
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
Somerville
R L
RL
Epperly
B R
BR
Dekker
E E
EE
D000143:Acids; D000429:Alcohol Oxidoreductases / Q000235:genetics / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification*; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005796:Genes; D005798:Genes, Bacterial; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D000143:Acids; D001426:Bacterial Proteins; D010446:Peptide Fragments; D000429:Alcohol Oxidoreductases; C023159:L-threonine 3-dehydrogenase