Isolation and Characterization of a Mutation That Alters the Substrate Specificity of the Escherichia Coli Glucose Permease

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1996 Feb 1

PMID 8550539

Citations 8

Authors

G S Begley

K A Warner

J C Arents

P W Postma

G R Jacobson

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

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Mannitol-1-phosphate dehydrogenase (MtlD) is required for mannitol and glucitol assimilation in Bacillus subtilis: possible cooperation of mtl and gut operons.

Watanabe S, Hamano M, Kakeshita H, Bunai K, Tojo S, Yamaguchi H J Bacteriol. 2003; 185(16):4816-24.

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Genetic control of manno(fructo)kinase activity in Escherichia coli.

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Glucose transporter mutants of Escherichia coli K-12 with changes in substrate recognition of IICB(Glc) and induction behavior of the ptsG gene.

Zeppenfeld T, Larisch C, Lengeler J, Jahreis K J Bacteriol. 2000; 182(16):4443-52.

PMID: 10913077 PMC: 94615. DOI: 10.1128/JB.182.16.4443-4452.2000.

Substrate specificity and signal transduction pathways in the glucose-specific enzyme II (EII(Glc)) component of the Escherichia coli phosphotransferase system.

Notley-McRobb L, Ferenci T J Bacteriol. 2000; 182(16):4437-42.

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