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Resolution of the Phosphoenolpyruvate: Fructose Phosphotransferase System of Escherichia Coli into Two Components: Enzyme IIfructose and Fructose-induced HPr-like Protein (FPr)

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Journal Can J Biochem
Specialty Biochemistry
Date 1980 Oct 1
PMID 7006754
Citations 7
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Abstract

A protein that substitutes for histidine-containing protein (HPr) in the phosphoenolpyruvate, fructose phosphotransferase system has been found in Escherichia coli grown on fructose. The impure preparation of the fructose-induced HPr-like protein (FPr) appears to be an extrinsic membrane protein which differs from HPr on the basis of its apparent molecular weight (45 000 vs. 9600, respectively), its affinity for DEAE-cellulose and its ability to promote sugar phosphorylation which is specific for fructose, rather than for glucose.

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

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

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Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria.

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