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.

Library of Congress Subject Headings

Dehydrogenases; Serratia marcescens; Enzyme inhibitors; Enzymes

Publication Date

12-1-1998

Document Type

Thesis

Department, Program, or Center

School of Chemistry and Materials Science (COS)

Advisor

Craig, Paul

Comments

Note: imported from RIT’s Digital Media Library running on DSpace to RIT Scholar Works. Physical copy available through RIT's The Wallace Library at: QP603.D4 W48 1998

Campus

RIT – Main Campus

Download

Share

COinS