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PMID: 6228716 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Allosteric regulatory properties of muscle phosphofructokinase.

Molecular and cellular biochemistry ·Vol. 57 ·No. 2 ·1983-00-00 ·Pages 147-54

Kemp RG, Foe LG

Abstract

We have reviewed the allosteric regulatory properties of skeletal muscle phosphofructokinase and recent results on the phosphorylation of this enzyme. The number and affinities of various ligand binding sites are described, and a simple three state model is presented to explain the kinetic and ligand-binding properties of the enzyme. Data describing a lack of fit to a concerted transition model are presented. The widespread occurrence of partial phosphorylation of phosphofructokinase at a specific site near the carboxyl terminus is documented, as well as the lack of significant kinetic consequences of such phosphorylation.

MeSH Terms
Adenosine Triphosphate/metabolism Allosteric Regulation Amino Acids/analysis Animals Hydrogen-Ion Concentration Kinetics Ligands Muscles/enzymology Phosphofructokinase-1/metabolism Phosphopeptides/analysis Phosphorylation Protein Kinases/metabolism
Chemicals
Amino Acids Ligands Phosphopeptides Adenosine Triphosphate Protein Kinases Phosphofructokinase-1
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kemp R G
Foe L G
References (44)
44 references, click to expand
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Article Info
Journal
Molecular and cellular biochemistry
Abbr.
Mol Cell Biochem
ISSN
0300-8177
DOI
10.1007/BF00849191
Published
1983-00-00
Pages
147-54
Language
English
Region
Netherlands
NLM ID
0364456
Subset
IM
Grants
NIADDK NIH HHS · AM19912 · United States
External Links
PubMed source DOI: 10.1007/BF00849191 View journal details
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