Molecular & physical characterization of threonine dehydrogenase from Serratia marcescens

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Title: Molecular & physical characterization of threonine dehydrogenase from Serratia marcescens
Author: Wetherell, Michael
Abstract: 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.
Record URI: http://hdl.handle.net/1850/13823
Date: 1998-12

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