PMID: 7916624Jul 10, 1993

Comparative analysis of species-independent, isozyme-specific amino-acid substitutions in mammalian muscle, brain and liver glycogen phosphorylases

Biochimica Et Biophysica Acta
J W HudsonM M Crerar

Abstract

Mammalian glycogen phosphorylases exist as three isozymes, muscle, brain and liver, that exhibit different responses to activation by phosphorylation and AMP, regardless of species. To identify species-independent, amino-acid substitutions that may be important determinants in differential isozyme control, we have sequenced cDNAs containing the entire protein coding regions of rat muscle and brain phosphorylases. Nucleotide sequence comparisons with rat liver, rabbit muscle, and human muscle, brain and liver phosphorylase genes, indicate that muscle and brain isozymes are more related to each other than to the liver isozyme. Unlike the human isozymes, there is little difference in GC content of codons in the rat isozymes. In relation to the rabbit muscle isozyme three-dimensional structure, amino-acid sequence comparisons indicate that very few nonconservative isozyme-specific substitutions occur in buried and dimer contact residues. There is strict conservation of active site, pyridoxal-phosphate-binding site and nucleoside inhibitor site residues, as well as CAP loop and helix-2 residues that comprise the phosphorylation activation and part of the AMP binding sites. In contrast, five liver isozyme-specific substitutions occur...Continue Reading

References

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Mar 28, 2006·The Journal of Biological Chemistry·Geetha BabuShao-Cong Sun

Citations

May 23, 2012·Neurochemical Research·Mauro DinuzzoFederico Giove
Nov 1, 2015·Molecular Aspects of Medicine·Loranne Agius
Sep 13, 1996·The Journal of Biological Chemistry·J L Buchbinder, R J Fletterick
Sep 24, 2015·Physiological Genomics·Fleur C GartonAlejandro Lucia

Related Concepts

Brain
DNA, Double-Stranded
Phosphorylases
Alloenzymes
Liver
Muscle

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