Cloning, expression, and nucleotide sequence of a mutant glgC gene from Escherichia coli B
Open Access
- 1 July 1992
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 174 (13) , 4509-4512
- https://doi.org/10.1128/jb.174.13.4509-4512.1992
Abstract
A mutant glgC gene contained in a 10.9-kb PstI fragment was cloned from the Escherichia coli B strain SG5 via colony hybridization by using a wild-type glgC probe. The altered allosteric properties of the expressed ADPglucose synthetase were found to result from the conversion of proline to serine at amino acid residue 295.Keywords
This publication has 24 references indexed in Scilit:
- Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sourcesJournal of Molecular Evolution, 1992
- Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzymeArchives of Biochemistry and Biophysics, 1990
- Physiology, Biochemistry and Genetics of Bacterial Glycogen SynthesisPublished by Elsevier ,1990
- Biosynthesis of Starch and Its RegulationPublished by Elsevier ,1988
- [1] Production of single-stranded plasmid DNAPublished by Elsevier ,1987
- BACTERIAL GLYCOGEN SYNTHESIS AND ITS REGULATIONAnnual Review of Microbiology, 1984
- A technique for radiolabeling DNA restriction endonuclease fragments to high specific activityAnalytical Biochemistry, 1983
- [2] New M13 vectors for cloningPublished by Elsevier ,1983
- Modification of the allosteric activator site of Escherichia coli ADP-glucose synthetase by trinitrobenzenesulfonateBiochemistry, 1981
- Substrate and metal ion interactions in the NAD+ malic enzyme from cauliflowerArchives of Biochemistry and Biophysics, 1980