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
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phosphofructokinase
- intolerance
-
gluconeogenesis
- glucose-1-phosphate
-
phosphorolysis
- bb
- troponins
-
antidiabetic
- sarcoplasm
- maltodextrins
-
amp-dependent
- isoproterenol
- vasopressin
-
gluconeogenic
- phenylephrine
- glucokinase
- rhabdomyolysis
- myoglobinuria
- pp1
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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
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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
results (
results (Temperature Stability
Temperature Stability on EC 2.4.1.1 - glycogen phosphorylase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
0
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heart isozyme Ib or IIIb: t1/2: 2.4-2.9 min, heart isozyme Ia: stable in the presence of 2-mercaptoethanol
30
40
43
45
48
50
55
60
70
75 - 85
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stGP retains more than 80% of the full activity after incubation at 75°C and 85°C for 8 h
80
additional information
40
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purified recombinant enzyme, loss of 10% activity within 120 min, stable
45
half-life 2.6 min for wild-type, 0.8 min for mutant T28A, 5.3 min for mutant K31A, 2.8 min for mutant S174A, 2.9 min for mutant R141A. In presence of 10 mM phosphate, half-life 280 min for wild-type, 2.2 min for mutant T28A, 170 min for mutant K31A, 33 min for mutant S174A, 7.5 min for mutant R141A. In presence of 100 mM phosphate, half-life 3500 min for wild-type, 330 min for mutant T28A, 3500 min for mutant K31A, 990 min for mutant S174A, 1400 min for mutant R141A
48
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kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle is studied by dynamic light scattering. The aggregation process proceeds in the regime of diffusion-limited cluster-cluster aggregation. In the presence of alpha-crystallin, a protein possessing the chaperone-like activity, the process of protein aggregation switches to the regime of reactionlimited clustercluster aggregation. The addition of alpha-crystallin raises the rate of thermal inactivation of Phb
48
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half-life about 50 min. In presence of 1.5 M proline, half-life above 150 min. Suppression of thermal aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the molecule
50
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half-life without additives is about 2 h, and is extended by 45fold to 90 h through a combined addition of 0.1 mM Mg2+, 5 mM DTT, 1% NaCl, 0.1% Triton X-100, and 1 mg/mL BSA
55
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loss of approx. 90% activity after 10 min in 500 mM potassium phosphate pH 7.3
55
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unprimed phosphorylase II, 80% loss of activity after 10 min, albumin protects
60
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wild-type, complete loss of activity within 20 min. Mutants F39L, N135S and T706I retain about 50% of activity after 20 min at 60°C. Mutant F39L/N135S/T706I retains more than 95% of its activity after 60 min at 60°C
70
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purified recombinant enzyme, half-ife is about 40 min, inactivation after 120 min
80
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purified recombinant enzyme, loss of over 90% activity within 10 min, inactivation after 60 min
80
retains its complete activity after 24 h at 80°C in Tris-HCl buffer
additional information
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phosphate protects against thermal inactivation
additional information
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heating enhances sensitivity to tyrosine inhibition
additional information
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the proposed scheme of thermal denaturation and aggregation of Phb includes the stage of reversible dissociation of dimers of Phb into monomers, the stage of the formation of the starting aggregates from the denatured monomers of Phb, and the stage of the sticking of the starting aggregates and higher order aggregates
