The Phosphoenolpyruvate : Methyl-alpha-d-glucoside Phosphotransferase System in Bacillus Subtilis Marburg : Kinetic Studies of Enzyme Ii and Evidence for a Phosphoryl Enzyme Ii Intermediate

Overview

Journal Biochimie

Specialty Biochemistry

Date 1978 Jan 1

PMID 111719

Citations 4

Authors

M Marquet

M C Creignou

R DEDONDER

Affiliations

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Abstract

The Enzyme II complex catalyzing the phosphoryl transfer from P-HPr to sugar in the inducible methyl-alpha-D-glucoside : phosphotransferase system in Bacillus subtilis acts according to a ping-pong mechanism, implying a phosphorylated Enzyme II intermediate. This result is supported by the demonstration of a specific transphosphorylation between [14C] alphaMG and glucose-6-phosphate in the presence of an induced Enzyme II preparation.

Citing Articles

The enzymology of the bacterial phosphoenolpyruvate-dependent sugar transport systems.

Robillard G Mol Cell Biochem. 1982; 46(1):3-24.

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Reizer J, Novotny M, Stuiver I, Saier Jr M J Bacteriol. 1984; 159(1):243-50.

PMID: 6429122 PMC: 215620. DOI: 10.1128/jb.159.1.243-250.1984.

Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria.

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Phosphoenolpyruvate:sugar phosphotransferase system of Bacillus subtilis: cloning of the region containing the ptsH and ptsI genes and evidence for a crr-like gene.

Steinmetz M J Bacteriol. 1987; 169(5):2287-90.

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