2.4.1.1: glycogen phosphorylase
This is an abbreviated version!
For detailed information about glycogen phosphorylase, go to the full flat file.
Word Map on EC 2.4.1.1
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2.4.1.1
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amp
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glycogenolysis
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hepatocytes
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mcardle
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glucagon
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glucose-6-phosphatase
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pyridoxal
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hexokinase
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6-phosphate
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creatine
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epinephrine
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myopathy
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phosphorylases
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phosphofructokinase
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intolerance
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gluconeogenesis
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glucose-1-phosphate
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phosphorolysis
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bb
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troponins
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antidiabetic
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sarcoplasm
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maltodextrins
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amp-dependent
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isoproterenol
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vasopressin
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gluconeogenic
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phenylephrine
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glucokinase
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rhabdomyolysis
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myoglobinuria
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pp1
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beta-adrenergic
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adrenaline
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phosphatase-1
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phosphocreatine
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phosphoglucomutase
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debranching
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soleus
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glucose-6-p
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adp-glucose
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g6pase
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glucagon-stimulated
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inhibitor-2
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2,6-bisphosphate
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glycogenesis
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t-state
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amylose
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biotechnology
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amyloplasts
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medicine
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heart-type
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agriculture
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analysis
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synthesis
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drug development
- 2.4.1.1
- amp
-
glycogenolysis
- hepatocytes
- mcardle
- glucagon
- glucose-6-phosphatase
- pyridoxal
- hexokinase
- 6-phosphate
- creatine
- epinephrine
- myopathy
- phosphorylases
-
phosphofructokinase
- intolerance
-
gluconeogenesis
- glucose-1-phosphate
-
phosphorolysis
- bb
- troponins
-
antidiabetic
- sarcoplasm
- maltodextrins
-
amp-dependent
- isoproterenol
- vasopressin
-
gluconeogenic
- phenylephrine
- glucokinase
- rhabdomyolysis
- myoglobinuria
- pp1
-
beta-adrenergic
- adrenaline
- phosphatase-1
- phosphocreatine
- phosphoglucomutase
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debranching
- soleus
-
glucose-6-p
- adp-glucose
- g6pase
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glucagon-stimulated
- inhibitor-2
-
2,6-bisphosphate
-
glycogenesis
-
t-state
- amylose
- biotechnology
- amyloplasts
- medicine
-
heart-type
- agriculture
- analysis
- synthesis
- drug development
Reaction
Synonyms
1,4-alpha-glucan phosphorylase, alpha-1,4 glucan phosphorylase, alpha-1,4-glycan phosphorylase, alpha-glucan phosphorylase, alpha-glucan phosphorylase H, alpha-glucan/maltodextrin phosphorylase, alphaGP, amylopectin phosphorylase, amylophosphorylase, CcStP, cyosolic phosphorylase, GlgP, glucan phosphorylase, glucosan phosphorylase, glycogen phosphorylase, glycogen phosphorylase a, glycogen phosphorylase b, glycogen phosphorylase-a, GP, GP b, GPA, GPase, GPase a, GPb, GPBB, GPH, granulose phosphorylase, MalP, maltodextrin phosphorylase, More, muscle glycogen phosphorylase, muscle phosphorylase, muscle phosphorylase a and b, myophosphorylase, PF1535, Phb, PHO, Pho 2, Pho1, phosphorylase a, phosphorylase b, phosphorylase, alpha-glucan, plastidial phosphorylase, polyphosphorylase, potato phosphorylase, RMGPa, rmGPb, SP, starch phosphorylase, starch phosphorylase H, stGP, StP, tGPGG, type L alpha-glucan phosphorylase
ECTree
2.4.1.1 glycogen phosphorylaseAdvanced search results
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Posttranslational Modification on EC 2.4.1.1 - glycogen phosphorylase
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycoprotein
each subunit has two distinct maltooligosaccharide binding sites: a storage site and a catalytic site
phosphoprotein
proteolytic modification
side-chain modification
phosphoprotein
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the glycogen phosphorylase dimer can exist in either in unphosphorylated glycogen phosphorylase b or phosphorylated glycogen phosphorylase a form depending on hormonal activation of kinase/phosphatase reactions
phosphoprotein
the muscle isoform of phosphorylase is activated by phosphorylation (GPb to GPa conversion)
phosphoprotein
glycogen phosphorylase a is prepared from glycogen phosphorylase b by phosphorylation through a truncated form of the catalytic subunit of rabbit skeletal muscle phosphorylase kinase
phosphoprotein
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phosphorylation and dephosphorylation of the enzyme regulates its activity and is catalyzed by a phosphorylase phosphatase
phosphoprotein
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phosphorylation and dephosphorylation of the enzyme regulates its activity and is catalyzed by a phosphorylase phosphatase and protein kinase A
phosphoprotein
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cyclin-dependent protein kinase Pho85p controls the phosphorylation state of phosphorylase and thus its activity
proteolytic modification
cleavage of a 55 amino acid transit peptide
side-chain modification
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activation by rabbit muscle calcium-activated phosphorylase kinase in the presence of ATP and Mg2+
side-chain modification
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phosphorylation converts inactive phosphorylase b into active phosphorylase a
side-chain modification
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in vitro phosphorylation of phosphorylase b with phosphorylase kinase from rabbit muscle
side-chain modification
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incorporation of approx. 1 mol phosphate/mol of subunit
side-chain modification
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phosphorylation converts inactive phosphorylase b into active phosphorylase a
side-chain modification
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activation of enzyme by phosphorylase kinase, inactivation by phosphorylase phosphatase is due to phosphorylation of a single threonine residue in the N-terminus of the large subunit
side-chain modification
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phosphate-content correlates with activity
side-chain modification
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0.1-0.74 mol covalently bound phosphate per mol subunit
side-chain modification
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activation by phosphorylation
side-chain modification
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phosphorylation site: a single Thr-residue in the N-terminal region
side-chain modification
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yeast and mammalian enzymes are activated by covalent phosphorylation, phosphorylase kinase
side-chain modification
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phosphorylation site: a single Thr-residue in the N-terminal region
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side-chain modification
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yeast and mammalian enzymes are activated by covalent phosphorylation, phosphorylase kinase
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