Phosphorylation of D-glucose in Escherichia Coli Mutants Defective in Glucosephosphotransferase, Mannosephosphotransferase, and Glucokinase

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1975 Jun 1

PMID 1097393

Citations 118

Authors

S J Curtis

W Epstein

Affiliations

Soon will be listed here.

Abstract

Genetic studies show that Escherichia coli has three enzymes capable of phosphorylating glucose: soluble adenosine 5'-triphosphate-dependent glucokinase, which plays only a minor role in glucose metabolism; an enzyme II, called glucosephosphotransferase, with high specificity for the D-glucose configuration; and another enzyme II, called mannosephosphotransferase, with broader specificity. The former enzyme II is active on glucose and methyl-alpha-glucopyranoside, whereas the latter is active on D-glucose, D-mannose, 2-deoxy-D-glucose, D-glucosamine, and D-mannosamine. Mutations leading to loss of glucosephosphotransferase activity and designated by the symbol gpt are between the purB and pyrC markers in a locus previously called cat. The locus of mutations to loss of mannosephosphotransferase, mpt, is between the eda and fadD genes. Mutations to loss of glucokinase, glk, are between the ptsI and dsd genes.

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