Threonine dehydrogenase has been purified from Serretia marcescens 450 fold to obtain 1300 micrograms of enzyme from 15 grams of cells. The amino-terminus has been sequenced and places it in a class with medium chain alcohol dehydrogenases from both Z.mobilus and E.coli. The native enzyme is a dimer of 35.6 kD sub-units containing approximately 324 amino acids. The gene structure of the enzyme is dissimilar from that of the E.coli TDH and may represent a mutation of an alcohol dehydrogenase with possible preference to propanol.
Library of Congress Subject Headings
Dehydrogenases; Serratia marcescens; Enzyme inhibitors; Enzymes
Department, Program, or Center
School of Chemistry and Materials Science (COS)
Wetherell, Michael, "Molecular & physical characterization of threonine dehydrogenase from Serratia marcescens" (1998). Thesis. Rochester Institute of Technology. Accessed from
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