RGD Reference Report - Glycogen phosphorylase: control by phosphorylation and allosteric effectors. - Rat Genome Database

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Glycogen phosphorylase: control by phosphorylation and allosteric effectors.

Authors: Johnson, LN 
Citation: Johnson LN FASEB J. 1992 Mar;6(6):2274-82.
RGD ID: 2304109
Pubmed: PMID:1544539   (View Abstract at PubMed)

Structural studies of muscle glycogen phosphorylase during the last two decades have provided a detailed mechanism for the molecular basis of the control by phosphorylation and by allosteric effectors and the catalytic mechanism. Control by phosphorylation is effected by a disorder to order transition of the NH2-terminal residues that promotes localized changes in the structure of the protein at the region of subunit-subunit contacts and larger changes in the quaternary structure. The covalently attached phosphate group acts like an allosteric effector but the full manifestation of the response is also dependent on the NH2-terminal tail residues. The noncovalently bound allosteric effectors produce similar shifts in the structural states although these are bound at sites that are remote from the serine-phosphate site. The communication from these sites to the catalytic site is through long-range interactions that result in activation of the enzyme through opening access to the buried catalytic site and through creation of the substrate phosphate recognition site by an interchange of an acidic group with a basic group. Recent advances in expression systems have opened the way to a study of properties both for the muscle and other isozymes and other species that should illuminate the different regulatory roles of the enzyme in different tissues and organisms. The allosteric mechanism of activation of phosphorylase by phosphorylation may be relevant to other enzymes although it is now known that other mechanisms such as electrostatic steric blocking mechanisms also exist.



Molecular Pathway Annotations    Click to see Annotation Detail View

RGD Manual Annotations


  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PYGBHumanglycogen degradation pathway   TAS  RGD 
PYGLHumanglycogen degradation pathway   TAS  RGD 
PYGMHumanglycogen degradation pathway   TAS  RGD 
PygbRatglycogen degradation pathway   ISORGD:736182 RGD 
PygbMouseglycogen degradation pathway   ISORGD:736182 RGD 
PyglRatglycogen degradation pathway   ISORGD:731803 RGD 
PyglMouseglycogen degradation pathway   ISORGD:731803 RGD 
PygmRatglycogen degradation pathway   ISORGD:737329 RGD 
PygmMouseglycogen degradation pathway   ISORGD:737329 RGD 
Objects Annotated

Genes (Rattus norvegicus)
Pygb  (glycogen phosphorylase B)
Pygl  (glycogen phosphorylase L)
Pygm  (glycogen phosphorylase, muscle associated)

Genes (Mus musculus)
Pygb  (brain glycogen phosphorylase)
Pygl  (liver glycogen phosphorylase)
Pygm  (muscle glycogen phosphorylase)

Genes (Homo sapiens)
PYGB  (glycogen phosphorylase B)
PYGL  (glycogen phosphorylase L)
PYGM  (glycogen phosphorylase, muscle associated)


Additional Information