Isolation and characterization of a mutation that alters the substrate-specificity of the Escherichia coli glucose permease
| Autor: | J C Arents, Gary R. Jacobson, K A Warner, Gail S. Begley, P.W. Postma |
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| Přispěvatelé: | Molecular Microbial Physiology (SILS, FNWI) |
| Rok vydání: | 1996 |
| Předmět: |
Molecular Sequence Data
Mutant Biology medicine.disease_cause Microbiology Substrate Specificity Structure-Activity Relationship 03 medical and health sciences Escherichia coli medicine Structure–activity relationship Mannitol Amino Acid Sequence Phosphorylation Phosphoenolpyruvate Sugar Phosphotransferase System Molecular Biology Peptide sequence 030304 developmental biology 0303 health sciences Mutation Strain (chemistry) 030306 microbiology Chromosome Mapping Molecular biology Kinetics Transmembrane domain Biochemistry Research Article |
| Zdroj: | Journal of Bacteriology, 178, 940-942. American Society for Microbiology |
| ISSN: | 0021-9193 |
| Popis: | We isolated 10 mannitol-positive mutants from a mannitol-negative Escherichia coli strain. These mutations mapped within ptsG, encoding the glucose permease (EIIGlc), and resulted in a G-320-to-V substitution that allows EIIGlc to transport mannitol. Gly-320 lies within a putative transmembrane helix of EIIGlc that may be involved in substrate recognition. |
| Databáze: | OpenAIRE |
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