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PMID: 7006754 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Resolution of the phosphoenolpyruvate: fructose phosphotransferase system of Escherichia coli into two components: enzyme IIfructose and fructose-induced HPr-like protein (FPr).

Canadian journal of biochemistry ·Vol. 58 ·No. 10 ·1980-10-00 ·Pages 1144-6

Waygood EB

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.

MeSH Terms
Bacterial Proteins Carrier Proteins/isolation & purification,metabolism Enzyme Induction Escherichia coli/enzymology Escherichia coli Proteins Fructose/pharmacology Intracellular Signaling Peptides and Proteins Kinetics Mutation Phenotype Phosphoenolpyruvate Sugar Phosphotransferase System/isolation & purification,metabolism Phosphorylation Protein Kinases Substrate Specificity Sugar Phosphates/biosynthesis
Chemicals
Bacterial Proteins Carrier Proteins Escherichia coli Proteins Intracellular Signaling Peptides and Proteins Sugar Phosphates fructose-induced HPr-like protein, bacteria Fructose Protein Kinases fruB protein, E coli Phosphoenolpyruvate Sugar Phosphotransferase System
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Waygood E B
Article Info
Journal
Canadian journal of biochemistry
Abbr.
Can J Biochem
ISSN
0008-4018
Published
1980-10-00
Pages
1144-6
Language
English
Region
Canada
NLM ID
0421034
Subset
IM
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