Gel electrophoretic analysis of Zymomonas mobilis glycolytic and fermentative enzymes: Identification of alcohol dehydrogenase II as a stress protein
- Univ. of Florida, Gainesville (United States)
- La Trobe Univ., Victoria (Australia)
The 13 major enzymes which compose the glycolytic and fermentative pathways in Zymomonas mobilis are particularly abundant and represent one-half of the soluble protein in exponential-phase cells. One- and two-dimensional polyacrylamide gel electrophoresis maps were developed for 12 of these enzymes. Assignments were made by comigration with purified proteins, comparison with overexpressed genes in recombinant strains, and Western blots (immunoblots). Although most glycolytic enzymes appeared resistant to turnover and accumulated in stationary-phase cells, the protein levels of pyruvate kinase, alcohol dehydrogenase I, and glucokinase declined. Alcohol dehydrogenase II was identified as a major stress protein and was induced both by exposure to ethanol and by elevated temperature (45C). This enzyme, encoded by the adhB gene, is expressed from tandem promoters which share partial sequence identity with Escherichia coli consensus sequence for heat shock proteins.
- OSTI ID:
- 5865549
- Journal Information:
- Journal of Bacteriology; (United States), Vol. 173:19; ISSN 0021-9193
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
ALCOHOL DEHYDROGENASE
BIOCHEMICAL REACTION KINETICS
ZYMOMONAS MOBILIS
ENZYME ACTIVITY
BIOLOGICAL PATHWAYS
BIOLOGICAL STRESS
ETHANOL
GENES
TEMPERATURE EFFECTS
ALCOHOLS
BACTERIA
ENZYMES
HEMIACETAL DEHYDROGENASES
HYDROXY COMPOUNDS
KINETICS
MICROORGANISMS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PROTEINS
REACTION KINETICS
550200* - Biochemistry
560300 - Chemicals Metabolism & Toxicology
560200 - Thermal Effects