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Inducible xylitol dehydrogenases in enteric bacteria
Journal of Bacteriology
|May 1, 1985
Summary
Four bacterial strains, including Morganella morganii and Serratia marcescens, produce xylitol dehydrogenase enzymes. These enzymes vary in their ability to convert xylitol into D-xylulose or L-xylulose, impacting biochemical pathways.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- Xylitol metabolism is crucial in various biological systems.
- The enzyme xylitol dehydrogenase plays a key role in xylitol catabolism.
- Understanding bacterial xylitol dehydrogenase diversity is important for biotechnological applications.
Purpose of the Study:
- To investigate the induction and characteristics of xylitol dehydrogenase in selected bacterial strains.
- To compare the substrate specificity and kinetic properties of xylitol dehydrogenases from different bacterial species.
Main Methods:
- Bacterial cultivation on xylitol-containing media.
- Partial purification of induced xylitol dehydrogenase enzymes.
- Enzymatic assays to determine substrate oxidation and product formation.
- Determination of kinetic parameters (Km) and molecular weights.
Main Results:
- Morganella morganii, Providencia stuartii, and Serratia marcescens induced xylitol dehydrogenase that oxidizes xylitol to D-xylulose.
- These three enzymes exhibited Km values between 7.1-16.4 mM and molecular weights of 130,000-155,000 Da.
- Erwinia sp. strain 4D2P produced a distinct xylitol dehydrogenase oxidizing xylitol to L-xylulose, with a Km of 72 mM and a molecular weight of 102,000 Da.
Conclusions:
- Bacterial xylitol dehydrogenases exhibit significant diversity in substrate oxidation and kinetic properties.
- The findings highlight enzymatic differences in xylitol metabolism among bacterial species.
- This research provides insights into bacterial enzyme diversity relevant to carbohydrate metabolism.