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
-
2.4.1.1
-
amp
-
glycogenolysis
-
hepatocytes
-
mcardle
-
glucagon
-
glucose-6-phosphatase
-
pyridoxal
-
hexokinase
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6-phosphate
-
creatine
-
epinephrine
-
myopathy
-
phosphorylases
-
phosphofructokinase
-
intolerance
-
gluconeogenesis
-
glucose-1-phosphate
-
phosphorolysis
-
bb
-
troponins
-
antidiabetic
-
sarcoplasm
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maltodextrins
-
amp-dependent
-
isoproterenol
-
vasopressin
-
gluconeogenic
-
phenylephrine
-
glucokinase
-
rhabdomyolysis
-
myoglobinuria
-
pp1
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beta-adrenergic
-
adrenaline
-
phosphatase-1
-
phosphocreatine
-
phosphoglucomutase
-
debranching
-
soleus
-
glucose-6-p
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adp-glucose
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g6pase
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glucagon-stimulated
-
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
-
biotechnology
-
amyloplasts
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medicine
-
heart-type
-
agriculture
-
analysis
-
synthesis
-
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
-
debranching
- soleus
-
glucose-6-p
- adp-glucose
- g6pase
-
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
results (
results (Inhibitors
Inhibitors on EC 2.4.1.1 - glycogen phosphorylase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(1S)-1,5-anhydro-D-glucitol-spiro[1.5]-3-(2-naphthyl)-1,4,2-oxathiazole
-
-
(1S)-1,5-anhydro-D-glucitol-spiro[1.5]-3-(4-methoxyphenyl)-1,4,2-oxathiazole
-
-
(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-1H-pyrrolo[2,3-c]pyridin-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-6-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-chloro-7-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2-[[(5-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
-
-
(2E,2'E)-N,N'-(oxydiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
-
(2E,2'E)-N,N'-(thiodiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
-
(2E,2'E)-N,N'-pentane-1,5-diylbis[3-(3,4-dichlorophenyl)acrylamide]
crystallization data
(2R)-2-cyclohexyl-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]propanoic acid
-
potent in vitro inhibition, reduced inhibition of CYP2C9 and good pharmacokinetic properties
(2R,3R,4S,5R,6R)-3,4,5,9-tetrahydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione
-
(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione
-
(2S)-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]heptanoic acid
-
(2S)-cyclohexyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
-
-
(2S)-cyclopentyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
-
-
(3beta)-28-[(2-[[2-(acetylamino)ethyl]amino]ethyl)amino]-28-oxoolean-12-en-3-yl acetate
-
-
(3beta)-28-[(3-aminopropyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
-
-
(3beta)-28-[(6-aminohexyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
-
-
(3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oic acid
-
-
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
-
-
(4aS,6aS,6bR,8aR,14aR,14bR,16bS)-2,2,6a,6b,9,9,14a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,14,14a,14b,15,16b-hexadecahydrochryseno[1,2-g]quinoxaline-4a(2H)-carboxylic acid
-
-
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(2-naphthyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
-
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(4-methoxyphenyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
-
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(4-toluyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
-
(5R,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dione
-
-
(5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(4-methoxyphenyl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane 2,2-dioxide
-
-
(5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(naphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(4-methoxyphenyl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-8,9,10-triol 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(5,6,7,8-tetrahydronaphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-8,9,10-triol 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(naphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-8,9,10-triol 2,2-dioxide
-
-
(5S,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-2-thioxo-6-oxa-1,3-diazaspiro[4.5]decan-4-one
-
-
(5S,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dione
-
-
(6aS,6bR,8aR,16aR,16bR,18bS)-2,2,6a,6b,9,9,16a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,16,16a,16b,17,18b-hexadecahydrochryseno[1,2-b]phenazine-4a(2H)-carboxylic acid
-
-
1,3,5-tris-4'-2''-[3'''-C-(beta-D-glucopyranosyl)-1''',2''',4'''-oxadiazol-5'''-yl]ethyl-1',2',3'-triazol-1'-ylmethylbenzene
-
trivalent inhibitor. The valency of the molecules influences slightly the inhibition of the enzyme whereas the presence of a spacer arm between the core and the pharmacophore moieties does not
1,3,5-tris[3'-C-(beta-D-glucopyranosyl)-1',2',4'-oxadiazol-5'-yl]-benzene
-
trivalent inhibitor. The valency of the molecules influences slightly the inhibition of the enzyme whereas the presence of a spacer arm between the core and the pharmacophore moieties does not
1,4-dideoxy-1,4-imino-D-arabinitol
-
inhibits Pa-catalyzed As(V) reduction, inhibition of As(V) reduction is not influenced by glucose or AMP
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
1-(2-naphthyl)-3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
1-(beta-D-glucopyranosyl)-5-ethynyluracil
-
cytotoxic effect on Hep-G2 cells
1-methyl-3-([4-(2-thienylmethyl)phenyl]amino)quinoxalin-2(1H)-one
-
50% inhibition at 0.00011 mM in glycogenolysis assay, no bioavailability in vivo
1-phenyl-3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
1-[(2S)-2-([(5-chloro-1H-indol-2-yl)carbonyl]amino)-3-phenylpropanoyl]azetidine-3-carboxylic acid
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
1-[6-(acetyloxy)hexyl] 4-(7-[[(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy]heptyl) (2R)-2-hydroxybutanedioate
-
-
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclodecanecarboxylic acid
-
-
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclooctanecarboxylic acid
-
potent in vitro inhibition, reduced inhibition of CYP2C9 and good pharmacokinetic properties
2,2',2''-tris[(2E)-4-hydroxybut-2-en-1-yl] 1,1',1''-(3b,5x,9x,13x,18x)-lup-20(29)-ene-3,23,28-triyl triethanedioate
-
-
2,3,4,6-tetra-O-acetyl-1-O-[(2alpha,3beta)-2,3-dihydroxy-28-oxoolean-12-en-28-yl]-beta-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-({[(4-methylphenyl)sulfonyl]oxy}methyl)-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-({[2-(1H-indol-3-yl)ethyl]amino}methyl)-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(chlorooxy)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(hydroxyamino)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(naphthalen-2-ylamino)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-[(pyridin-2-ylamino)methyl]-alpha-D-glucopyranose
-
-
2,3,4,6-tetra-O-benzyl-1-C-{[(4-methoxyphenyl)amino]methyl}-alpha-D-glucopyranose
-
-
2,3-dichloro-N-(1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.002 microM
2,3-dichloro-N-(1-[3-hydroxy-2-(hydroxymethyl)propyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.038 microM
2,3-dichloro-N-[1-(2-hydroxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.007 microM
2,3-dihydroisooxazolyl oleanolic acid benzyl ester
-
50% inhibition at 0.0196 mM
2-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)-4-methoxybutanoic acid
-
-
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-4-fluoro-N-(4-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
simultaneous inhibition of glycogen phosphorylase and activation of glucokinase
2-chloro-N-((3R)-1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.040 microM
2-chloro-N-((3R)-1-[(2S)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.021 microM
2-chloro-N-((3S)-1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.027 microM
2-chloro-N-((3S)-1-[(2S)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.012 microM
2-chloro-N-(1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.029 microM
2-chloro-N-(1-[2-(methylsulfinyl)ethyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.048 microM
2-chloro-N-(2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.041 microM
2-chloro-N-[1-(2-hydroxybutyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.044 microM
2-chloro-N-[1-(2-hydroxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.026 microM
2-chloro-N-[1-(2-methoxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.05 microM
2-chloro-N-[1-(3-hydroxypropyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.021 microM
2-chloro-N-[1-(cyanomethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.028 microM
2-ethoxy-2-oxoethyl (2beta,3alpha,5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2,3-dihydroxyolean-12-en-28-oate
-
50% inhibition at 0.019 mM
2-ethylimidazole
weak inhibition of wild-type activity, inhibition of mutant enzyme H334G
2-hydroxymethenyl oleanonic acid benzyl ester
-
50% inhibition at 0.0063 mM
2-O-acetyl-3-oxomaslinic acid benzyl ester
-
50% inhibition at 0.029 mM
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl (1S,2R,4aS,6aS,6bR,8aR,10S,12aR,12bR,14bS)-10-(acetyloxy)-1,2,6a,6b,9,9,12a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicene-4a(2H)-carboxylate
-
-
2-[(2R)-3,4-dihydroxy-5-oxo-2,5-dihydrofuran-2-yl]-2-hydroxyethyl (4aS,6aS,6bR,8aR,10S,12aR,12bR,14bS)-10-(acetyloxy)-2,2,6a,6b,9,9,12a-heptamethyl-1,3,4,5,6,6a,6b,7,8,8a,9,10,11,12,12a,12b,13,14b-octadecahydropicene-4a(2H)-carboxylate
-
-
2-[3'-(benzylamino)-2'-oxopyridin-1'(2H)-yl]-N-(3'',4''-dichlorobenzyl)acetamide
-
-
3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
3-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)propanoic acid
-
-
3-(beta-D-glucopyranosyl)-1-(2-naphthyl)-1H-1,2,4-triazol-5(4H)-one
-
3-(beta-D-glucopyranosyl)-6-pentyl-2,3-dihydro-furano-[2,3-d]pyrimidin-2-one
-
-
3-(beta-D-glucopyranosyl)-6-propyl-2,3-dihydro-furano-[2,3-d]pyrimidin-2-one
-
-
3-O-[1-(methyl 6-deoxy-alpha-D-glucopyranosid-6-yl)-1H-1,2,3-triazol-4-yl]methyl 3b-hydroxyolean-12-en-28-oate
inhibitor is predicted to bind at the T-state allosteric site exclusively. The binding position of the oleanolic acid moiety occupies the same location as the T-state allosteric site of asiatic acid in the crystal structure. The newly attached sugar moiety shields the carboxyl group of oleanolic acid from forming the salt bridge with Arg310, and consequently reverses the orientation of the oleanolic acid as well as propelled the sugar moiety to extend more deeply into the alloteric dimer interface. As a result, a new hydrogen-bonding network forms between the sugar hydroxyls and the carboxyl of Asp227 plus the guanidino of Arg193, respectively, enhancing their contribution to the stability of the complex
3-[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)amino]-3-oxopropanoic acid
-
-
3-[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]propanoic acid
-
-
3-[(4-isoxazolidin-3-ylphenyl)amino]-1-methylquinoxalin-2(1H)-one
-
50% inhibition at 0.00011 mM in glycogenolysis assay, no bioavailability in vivo
4-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)butanoic acid
-
-
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
4-nitrophenol
-
5 mM, 56% inhibition, enhances inhibition by glucose, glucose-6-phosphate and ATP
4-[(4-methyl-3-oxo-3,4-dihydroquinoxalin-2-yl)amino]-N-(2-thienylmethyl)benzamide
-
50% inhibition at 0.00014 mM in glycogenolysis assay, no bioavailability in vivo
4-[[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)methyl]sulfonyl]butanoic acid
-
-
5-chloro-N-(1,3,6,6-tetrafluoro-(R)-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
docking study. Hydrophobic residues, such as Phe53, Pro188, and Gly186, around the two aliphatic fluorine atoms suggest that the lipophilic contact among them is an important driver of activity increases. Hydrophobic residues Leu39 and Lys191 are close to one of the aromatic fluorine atoms
5-chloro-N-(1,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-(1-[(2R)-2,3-dihydroxypropyl]-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl)-1H-indole-2-carboxamide
-
50% inhibition at 0.044 microM
5-chloro-N-(3,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-(5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-(6,6-difluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
-
-
5-chloro-N-[1-(2-hydroxyethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-1H-indole-2-carboxamide
-
50% inhibition at 0.017 microM
5-chloro-N-[2-chloro-4-(1,2-dihydroxyethyl)-phenyl]-1H-indole-2-carboxamide
-
5-chloro-N-[4-(1,2-dihydroxyethyl)-3-(trifluoromethyl)phenyl]-1H-indole-2-carboxamide
-
5-chloro-N-[5-(1,2-dihydroxyethyl)pyrazin-2-yl]-1H-indole-2-carboxamide
-
5-chloro-N-[5-(1,2-dihydroxyethyl)pyridin-2-yl]-1H-indole-2-carboxamide
-
6-[(4-methylphenyl)amino]hexyl (3beta)-3-hydroxyolean-12-en-28-oate
-
-
6-[4-(methyl 2,3,4-tri-O-benzyl-alpha-D-glucopyranosiduronylmethyl)-1H-1,2,3-triazol-1-yl]hexyl 3beta-hydroxyolean-12-en-28-oate
-
acetate
weak inhibition of wild-type activity, no effect on the activity of the H334G mutant
alpha-cyclodextrin
-
mixed-type competitive inhibition, inhibitor is not bound into the enzyme crystal
alpha-D-Glucopyranose-1,2-cyclic phosphate
-
competitive vs. glucose 1-phosphate
baicalein
-
50% inhibition of phosphorylated, active enzyme at 0.0112 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0102 mM
BAY U6751
-
inhibits Pa-catalyzed As(V) reduction, glucose enhances inhibitory effect of the inhibitor on As(V) reduction, AMP at high concentration alleviates the inhibition
benzyl (2beta,5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2-hydroxy-3-oxoolean-12-en-28-oate
-
50% inhibition at 0.029 mM
benzyl (2Z,5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2-[[(2,4-dichlorobenzyl)oxy]imino]-3-oxoolean-12-en-28-oate
-
50% inhibition at 0.008 mM
benzyl (3beta)-3-[(pyridinium-1-ylacetyl)oxy]olean-12-en-28-oate chloride
-
-
benzyl (3beta)-3-[([4-[(4-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-methoxy-3-oxopropyl]phenoxy)methyl]-1H-1,2,3-triazol-1-yl]acetyl)oxy]olean-12-en-28-oate
-
-
benzyl (3beta)-3-[([4-[(dodecanoyloxy)methyl]-1H-1,2,3-triazol-1-yl]acetyl)oxy]olean-12-en-28-oate
-
-
benzyl (3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oate
-
-
benzyl (5xi,8alpha,9xi,10alpha,14beta,17alpha,18alpha)-2-hydroxy-3-oxooleana-1,12-dien-28-oate
-
50% inhibition at 0.030 mM
benzyl 1'-[(ethoxycarbonyl)methyl]pyrazolo[4,3-b]olean-12-en-28-oate
-
-
beta-cyclodextrin
-
mixed-type competitive inhibition, the inhibitor can be accomodated in the glycogen storage site of T-state enzyme, subsite specificity
beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide
-
competitive
beta-D-glucopyranosyl bismethoxyphosphoramidate
weak competitive inhibitor, binds at the catalytic site and induces conformational changes in the vicinity of the site, inhibition mechanism, overview
bis(6-([(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy)hexyl) (2R)-2-hydroxybutanedioate
-
-
cyanidin
-
50% inhibition of phosphorylated, active enzyme at 0.003 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.009 mM
D-glucono-delta-lactone
-
0.05 mM, 90% inhibition of glucan phosphorolysis
delphinidin
-
50% inhibition of phosphorylated, active enzyme at 0.0031 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0107 mM
EGTA
-
i.e. ethylene glycol bis(beta-aminoethylether)-N,N'-tetraacetic acid, 1 mM, 53% inhibition
epicatechin gallate
-
50% inhibition of phosphorylated, active enzyme at 0.0125 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.050 mM
epigallocatechin-3-gallate
-
50% inhibition of phosphorylated, active enzyme at 0.0077 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0339 mM
formate
5fold reduction of wild-type activity, no effect on the activity of the H334G mutant
FR258900
the inhibitor binds at the allosteric activator site, where the physiological activator AMP binds. The contacts from FR258900 to glycogen phosphorylase are dominated by nonpolar van der Waals interactions with Gln71, Gln72, Phe196, and Val459 (from the symmetry-related subunit), and also by ionic interactions from the carboxylate groups to the three arginine residues (Arg242, Arg309, and Arg310) that form the allosteric phosphate-recognition subsite. The binding of FR258900 to the protein promotes conformational changes that stabilize an inactive T-state quaternary conformation of the enzyme
gamma-cyclodextrin
-
mixed-type competitive inhibition, the inhibitor can be accomodated in the glycogen storage site of T-state enzyme, subsite specificity
glucopyranosylidene spirohydantoin
-
most effective glucose analogue inhibitor for glycogen phosphorylase b
glucopyranosylidene spirothiohydantoin
-
muscle and liver phosphorylase b, strong competitive inhibition vs. phosphate and glycogen
guanidine hydrochloride
-
study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation
hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyl) (3beta,3'beta)-bis(3-hydroxyolean-12-en-28-oate)
-
-
iminobis[ethane-2,1-diylimino(3beta)-28-oxoolean-12-ene-28,3-diyl]diacetate
-
-
maslinic acid-(2-piperidin-1-yl)ethyl ester
-
50% inhibition at 0.031 mM
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](4-hydroxyphenyl)ethanoate
-
-
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](phenyl)ethanoate
-
-
methyl 6-deoxy-6-[4-([[(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy]methyl)-1H-1,2,3-triazol-1-yl]-alpha-D-glucopyranoside
-
-
methyl [3-([(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino)-2-oxo-3,4-dihydroquinolin-1(2H)-yl]acetate
-
50% inhibition at 0.084 microM
N-(1-phenyl-1H-1,2,3-triazole-4-carbonyl)-beta-D-glucopyranosylamine
-
N-(3-cyano-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
N-(3-fluoro-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
-
N-(3-phenyl-1,2-oxazole-5-carbonyl)-beta-D-glucopyranosylamine
-
N-(beta-D-glucopyranosyl)-3-(napht-1-yl)-1,2,4-oxadiazol-5-carboxamide
-
N-(beta-D-glucopyranosyl)-3-phenyl-1,2,4-oxadiazol-5-carboxamide
-
N-(beta-D-glucopyranosyl)-5-(napht-1-yl)-1,3,4-oxadiazole-2-carboxamide
-
N-(beta-D-glucopyranosyl)-5-(naphth-1-yl)-1,2,4-oxadiazol-3-carboxamide
-
N-(beta-D-glucopyranosyl)-5-(naphth-2-yl)-1,3,4-oxadiazole-2-carboxamide
-
N-(beta-D-glucopyranosyl)-5-phenyl-1,2,4-oxadiazol-3-carboxamide
-
N-(beta-D-glucopyranosyl)-5-phenyl-1,3,4-oxadiazole-2-carboxamide
-
N-([(2E)-2-[4-(trifluoromethyl)benzylidene]hydrazinyl]carbonothioyl)-beta-D-glucopyranosylamine
-
-
N-([4-[(benzyloxy)carbonyl]benzoyl]carbamoyl)-beta-D-glucopyranosylamine
-
-
N-[(2E)-3-(5,6,7,8-tetrahydronaphthalen-2-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2E)-3-(naphthalen-2-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2E)-3-([1,1'-biphenyl]-4-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2E)-3-[4-(propan-2-yl)phenyl]prop-2-enoyl]-beta-D-glucopyranosylamine
-
N-[(2R)-2-methyl-3-[4-(propan-2-yl)phenyl]propanoyl]-beta-D-glucopyranosylamine
-
N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-norleucine
potent in vitro inhibition, low potential for P450 inhibition, and good pharmacokinetic properties
N-[1-(2-amino-2-oxoethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-2-methyl-6H-thieno[2,3-b]pyrrole-5-carboxamide
N-[1-(naphthalen-1-yl)-1H-1,2,3-triazole-4-carbonyl]-beta-D-glucopyranosylamine
-
N-[3-(naphthalen-1-yl)-1,2-oxazole-5-carbonyl]-beta-D-glucopyranosylamine
-
N-[[(2E)-2-(2-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(2-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(2-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(3-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(3-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(3-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-fluorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-methoxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-methylbenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(4-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[(2E)-2-(pyridin-4-ylmethylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
-
-
N-[[([1,1'-biphenyl]-4-yl)oxy]acetyl]-beta-D-glucopyranosylamine
-
N-[[4-(methoxycarbonyl)benzoyl]carbamoyl]-beta-D-glucopyranosylamine
-
-
N1-(2,4-dinitrophenyl)-C-(2,3,4,6-tetra-O-benzoyl-beta-D-glucopyranosyl)formamidrazone
-
N1-carbamoyl-C-(2,3,4,6-tetra-O-benzoyl-beta-D-glucopyranosyl)formamidrazone
-
N1-ethoxycarbonyl-C-(2,3,4,6-tetra-O-benzoyl-beta-D-glucopyranosyl)formamidrazone
-
N1-phenyl-N4-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosylcarbonyl)semicarbazide
-
NADPH
-
also oxidized form, less effective than nucleotide sugars, not NAD(H)
O-(1-methylcyclopentyl)-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
-
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
potent in vitro inhibition, low potential for P450 inhibition, and good pharmacokinetic properties
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-serine
potent in vitro inhibition, low potential for P450 inhibition, and good pharmacokinetic properties
oleanolic acid 3-O-[(2E)-3-(4-chlorophenyl)acrylic acid] ester
-
50% inhibition at 0.0033 mM
oleanolic acid 3-O-[(2E)-3-(4-methoxyphenyl)acrylic acid] ester
-
50% inhibition at 0.0169 mM
p-chloromercuribenzene sulfonate
-
inhibits GPa-catalyzed As(V) reduction
pelargonidin
-
50% inhibition of phosphorylated, active enzyme at 0.0436 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0062 mM
peonidin
-
50% inhibition of phosphorylated, active enzyme at 0.0251 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0176 mM
proline
-
concentrations of 0.1 M have a slight accelerating effect on thermal aggregation of glycogen phosphorylase b. The suppression aggregation at high proline concentrations is mainly due to the protective action of proline on the stage of unfolding of the molecule
pyridoxal 5'-phosphate
-
74 and 76% inhibition of phosphorylase II and I respectively
resorcinol
-
1 mM, 50% inhibition of phosphorylase A and B, 23% inhibition of phosphorylase C
Tannic acid
-
0.005 mg, complete inhibition of phosphorylase B, 63% and 50% inhibition of phosphorylase A and C respectively
tert-butyl (5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(4-methoxyphenyl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-1-carboxylate 2,2-dioxide
-
-
tert-butyl (5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-3-(naphthalen-2-yl)-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-1-carboxylate 2,2-dioxide
-
-
tert-butyl (5S,7R,8R,9S,10R)-8,9,10-tris(benzyloxy)-7-[(benzyloxy)methyl]-6-oxa-2-thia-1,3-diazaspiro[4.5]decane-1-carboxylate 2,2-dioxide
-
-
[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]acetic acid
-
-
[1-(6-[4-[(acetyloxy)methyl]-1H-1,2,3-triazol-1-yl]hexyl)-1H-1,2,3-triazol-4-yl]methyl (3b)-3-hydroxyolean-12-en-28-oate
-
-
[[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)methyl]sulfanyl]acetic acid
-
-
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
i.e. AVE9423. Inhibitor fully exploits the volume of the binding pocket and show pronounced binding entropy
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
-
-
1-[(2S)-2-([(5-chloro-1H-indol-2-yl)carbonyl]amino)-3-phenylpropanoyl]azetidine-3-carboxylic acid
-
i.e. CP-403700, 50% inhibition at 0.1 microM in presence of 1 mM phosphate. In presence of 1 mM phosphate plus 8 mM glucose, 50% inhibition at 0.05 microM. Presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
1-[(2S)-2-([(5-chloro-1H-indol-2-yl)carbonyl]amino)-3-phenylpropanoyl]azetidine-3-carboxylic acid
-
i.e. CP-403700, indole-site inhibitor, suppression of hepatic glycogenolysis
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
i.e. AVE2865. Inhibitor fully exploits the volume of the binding pocket and show pronounced binding entropy
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
-
-
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
i.e. AVE5688, binding to enzyme is exclusively enthalpic
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
-
-
5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
crystallization data
5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
-
inhibitor shows oral hypoglycemic activity in diabetic db/db mice
ADP
-
1.6 mM, 50% inhibition of starch phosphorolysis, 0.23 mM, 50% inhibition of starch synthesis, allosteric inhibition, kinetics
ADP-glucose
maximal inhibition achieved is 70%; maximal inhibition achieved is 95%
ADPglucose
-
1.3 mM, 50% inhibition of phosphorylase II, glucan phosphorolysis; strong inhibition of phosphorolysis, isozyme I
alpha-cyclodextrin dialdehyde I
-
0.4 mM, 50% inhibition after 15 min, 1.6 mM, 50% inhibition after 4.7 min
-
alpha-D-glucopyranosyl fluoride
-
strong inhibition of phosphorylase b, kinetics; weak inhibition
alpha-D-glucose-1-methylenephosphonate
-
competitive vs. glucose 1-phosphate
alpha-D-glucose-1-methylenephosphonate
-
competitive vs. glucose 1-phosphate
ATP
-
2.9 mM, 50% inhibition of starch phosphorolysis, 1.4 mM, 50% inhibition of starch synthesis
ATP
-
1 mM, 20% inhibition of phosphorylase B, 5 mM, 90% inhibition; phosphorylase A or C are not inhibited
ATP
-
1 mM, 50% inhibition, at non-saturating levels of glucose 1-phosphate; additive inhibition together with tyrosine
Caffeine
-
5 mM, complete inhibition of phosphorylase b, strong inhibition of phosphorylases ab and a
Caffeine
-
5 mM, 95% inhibition of heart phosphorylase Ib in the presence of 1 mM AMP, 30% inhibition of heart phosphorylase IIb
CH3Hg+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA, about 80% inhibition at 0.03 mM
CH3Hg+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA
chrysin
-
50% inhibition of phosphorylated, active enzyme above 0.0275 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0153 mM
CP-316819
-
indole-site inhibitor, presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
CP-316819
-
indole-site inhibitor, oral administration to diabetic ob/ob mice results in lowering of plasma glucose concentration by 40% at 50 mg per kg. Measured drug concentration in the liver is about 100fold higher than the in vitro IC50 values
CP-320626
-
indole-site inhibitor, presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
CP-380867
-
indole-site inhibitor, presence of endogenous inhibitors such as D-glucose, ADP, ATP, D-fructose 1-phosphate, D-glucose 6-phosphate, UDP-glucose markedly reduces the inhibitory effect
CP320626
-
hypoglycaemic drug, potent inhibitor of liver and muscle glycogen phosphorylase a
CP320626
-
inhibits Pa-catalyzed As(V) reduction, glucose enhances inhibitory effect of the inhibitor on As(V) reduction, AMP at high concentration alleviated the inhibition
cyclodextrin
-
i.e. structure analogue of alpha-1,4-linked starch molecule; weak inhibition
-
cyclodextrin
-
alpha- or beta-, not gamma-cyclodextrin; i.e. structure analogue of alpha-1,4-linked starch molecule
-
cyclodextrin
-
i.e. structure analogue of alpha-1,4-linked starch molecule; weak inhibition
-
cyclodextrin
-
i.e. structure analogue of alpha-1,4-linked starch molecule; strong inhibition
-
D-glucose
-
5 mM and 8.5 mM, 50% inhibition of phosphorylase ab at 8 mM and 16 mM glucose 1-phosphate, 23 mM and 40 mM, 50% inhibition of phosphorylase a
ellagic acid
-
50% inhibition of phosphorylated, active enzyme at 0.0032 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0121 mM
ellagic acid
competitive inhibitor with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. Ellagic acid functions with glucose in a strongly synergistic mode. Determination of crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes, overview
gallic acid
competitive inhibitor with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP
GDPglucose
-
0.05 mM, 50% inhibition, competitive inhibition of phosphorolysis
glucose 6-phosphate
inhibits the phosphorylated and unphosphorylated enzyme forms. Binding of glucose 6-phosphate to the muscle isozyme is competitive with binding of AMP, but it also stabilizes a conformation that is more tense than the native T-state enzyme. Inhibition of muscle GPa enzyme activity by G6P is additive with inhibition by glucose
Hg2+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA, about 90% inhibition at 0.0125 mM Hg2+, 80% at 0.01 mM
Hg2+
-
0.05 mM, 21% inhibition of phosphorylase A, 73% inhibition of phosphorylase
Hg2+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA
luteolin
-
50% inhibition of phosphorylated, active enzyme at 0.0156 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0288 mM
monohydroxyphenols
-
10 mM, 50, 40 and 65% inhibition of phosphorylases A, B and C
-
N-[1-(2-amino-2-oxoethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-2-methyl-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
50% inhibition at 0.135 microM
N-[1-(2-amino-2-oxoethyl)-2-oxo-1,2,3,4-tetrahydroquinolin-3-yl]-2-methyl-6H-thieno[2,3-b]pyrrole-5-carboxamide
-
-
p-chloromercuribenzoate
-
0.5 mM, 60% inhibition, reversible by 10 mM 2-mercaptoethanol
peroxynitrite
-
the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613, a key amino acid of the allosteric inhibitor site of the enzyme. Glycogen phosphorylase functions may be regulated by tyrosine nitration
peroxynitrite
the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613, a key amino acid of the allosteric inhibitor site of the enzyme. Glycogen phosphorylase functions may be regulated by tyrosine nitration
peroxynitrite
1 mM, almost complete inactivation. After the exposure to 1 mM peroxynitrite, the molar content of Cys residues decreases from 8.63 to 3.43 and 4.24 in the absence and in the presence of bicarbonate, respectively. The addition of 1 mM DTT in 10 min after peroxynitrite treatment does not significantly reverse loss of either activity or molar content of DTNB-reactive Cys residues. No involvement of Tyr613 nitration in the control of enzymatic function. The enzymatic activity does not directly correlate with the protein nitration levels
phosphate
Pho1 activity is strongly competitively inhibited by product phosphate in the synthesis reaction when amylopectin is the primer substrate, but this inhibition is less pronounced when short alpha-glucan chains are used as primers
quercetin
-
50% inhibition of phosphorylated, active enzyme at 0.0048 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0209 mM
quercetin
-
inhibits Pa-catalyzed As(V) reduction, inhibition of As(V) reduction is not influenced by glucose or AMP
UDP
-
at high glucose 1-phosphate concentration, glycogen synthesis, not phosphorolysis
UDPglucose
-
competitive to glucose 1-phosphate, non-competitive to phosphate
UDPglucose
-
1 mM, 43, 27 and 18% inhibition of phosphorylases A, B and C respectively
UDPglucose
-
10 mM, 44% inhibition at non-saturating levels of glucose 1-phosphate
UDPglucose
-
competitive to glucose 1-phosphate, non-competitive to phosphate
[(alpha-D-glucopyranosyloxy)methyl]phosphonic acid
-
competitive vs. glucose 1-phosphate
[(alpha-D-glucopyranosyloxy)methyl]phosphonic acid
-
competitive vs. glucose 1-phosphate
additional information
-
not inhibited by GMP; not inhibited by TMP; not inhibited by UMP, CMP, CTP
-
additional information
-
not inhibited by maltose, maltotriose, maltotetraose
-
additional information
-
not inhibited by 3-phosphoglycerate; not inhibited by acetate, acetylphosphate, butyrylphosphate, 6-phosphogluconate; not inhibited by fructose 6-phosphate
-
additional information
-
maltohexaose causes negligible substrate inhibition with Ki of 360 mM
-
additional information
-
the more active phosphorylated form of the enzyme, glycogen phosphorylase a, is a homodimer having an inhibitory allosteric binding site at the dimer interface for which synthetic ligands
-
additional information
molecular and kinetic mechanisms of enzyme inhibition by mercury, overview
-
additional information
-
not inhibited by 2-mercaptoethanol; not inhibited by non-aromatic amino acids; not inhibited by p-coumaric acid, caffeic acid or cinnamic acid
-
additional information
-
not inhibited by 3-phosphoglycerate; not inhibited by adenosine, cytosine; not inhibited by F-, ClO4-; not inhibited by fructose 6-phosphate; not inhibited by GMP; not inhibited by non-aromatic amino acids; not inhibited by succinate, 2-oxoglutarate, malate
-
additional information
-
binding and inhibition mechanism, no inhibition by (2,3,6-tri-O-methyl)-gamma-cyclodextrin
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additional information
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preference for hydrophobic group at C-28 of maslinic acid for enzyme inhibition
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additional information
pentacyclic triterpenes may exert hypoglycemic effects, at least in part, through glycogen phosphorylase inhibition
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additional information
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pentacyclic triterpenes may exert hypoglycemic effects, at least in part, through glycogen phosphorylase inhibition
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additional information
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inhibitor screening, native ligand docking of inhibitor tautomers supplemented by QM/MM calculations, modeling of free state ligands and bound ligands, detailed overview
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additional information
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inhibitory efficiency and inhibition kinetics of beta-D-glucopyranosyl-thiosemicarbazone derivatives as glycogen phosphorylase inhibitors, binding analysis, overview
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additional information
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N-(4-substituted-benzoyl)-N'-(beta-D-glucopyranosyl)ureas as inhibitors of glycogen phosphorylase, synthesis and evaluation by kinetic and crystallographic data, NMR structure analysis, molecular docking and modelling, overview. N-(trifluoroacetyl)-alpha-D-glucopyranosylamine and N-(trifluoroacetyl)-alpha-D-glucopyranosylamine are not inhibitory
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additional information
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the purine inhibitory site binds purine derivatives as well as pentacyclic triterpenes. Synthesis and inhibitory potencies of triazole-linked oleanolic acid dimers as enzyme inhibitors, overview. No inhibition by hexane-1,6-diyl(3beta,3'beta)-bis(3-hydroxyolean-12-en-28-oate) and dibenzyl (3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oate
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additional information
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evaluation of pentacyclic triterpenes as a class of inhibitors against glycogen phosphorylase, by receptor-based comparative molecular field analysis, and comparative molecular similarity analysis to investigate the quantitative structure-activity relationships of 106 compounds, detailed overview
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additional information
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synthesis of glucopyranonucleosides in the 5-alkynyl- and 6-alkylfurano[2,3-d]pyrimidine series, overview
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additional information
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synthesis of C-glucosylated spiro-sulfamide enzyme inhibitors via nucleophilic displacement of 1-O-tosyl or 1-deoxy-1-iodo-alpha-D-gluco-hept-2-ulopyranose tetra-O-benzylated derivative using aryl amines, followed by the formation of the corresponding cyclic sulfamide, overview
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additional information
synthesis, enzyme kinetics and computational evaluation of N-(beta-D-glucopyranosyl) oxadiazolecarboxamides as glycogen phosphorylase inhibitors, overview. The compounds have promising oral drug-like properties without any toxicity. No inhibition by N-(beta-D-glucopyranosyl)-5-(naphth-2-yl)-1,2,4-oxadiazol-3-carboxamide, N-(beta-D-glucopyranosyl)-3-(napht-2-yl)-1,2,4-oxadiazol-5-carboxamide, N-[3-(naphthalen-2-yl)-1,2-oxazole-5-carbonyl]-beta-D-glucopyranosylamine, and N-[1-(naphthalen-2-yl)-1H-1,2,3-triazole-4-carbonyl]-beta-D-glucopyranosylamine
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additional information
structure-based inhibitor design targeting glycogen phosphorylase b, virtual screening, synthesis, biochemical and biological assessment of N-acyl-beta-D-glucopyranosylamines, overview. In silico screening of 1888 N-acyl-beta-D-glucopyranosylamines putative enzyme inhibitors differing only in their R groups. Docking study for ligand binding affinities of the active sites and selection of six compounds and analysis of the inhibitory potency both in vitro and ex vivo
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additional information
synthesis of possible isomers of C-(2-deoxy-d-arabino-hex-1-enopyranosyl)-oxadiazoles and evaluation as glycogen phosphorylase inhibitors, overview
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additional information
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synthesis of possible isomers of C-(2-deoxy-d-arabino-hex-1-enopyranosyl)-oxadiazoles and evaluation as glycogen phosphorylase inhibitors, overview
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additional information
synthesis and evolution of C-glucopyranosyl-1,2,4-triazol-5-ones as inhibitors of glycogen phosphorylase, overview. No inhibition by 3-(beta-D-glucopyranosyl)-1-tosyl-1H-1,2,4-triazol-5(4H)-one and N1-(tert-butoxycarbonyl)-N2-phenyl-N4-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosylcarbonyl)semicarbazide
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additional information
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synthesis and evolution of C-glucopyranosyl-1,2,4-triazol-5-ones as inhibitors of glycogen phosphorylase, overview. No inhibition by 3-(beta-D-glucopyranosyl)-1-tosyl-1H-1,2,4-triazol-5(4H)-one and N1-(tert-butoxycarbonyl)-N2-phenyl-N4-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosylcarbonyl)semicarbazide
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additional information
molecular and kinetic mechanisms of enzyme inhibition by mercury, overview
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additional information
computationally motivated synthesis, using N-(2,3,4,6-tetra-O-acetyl-beta-D-glucopyranosyl)-tetrazole-5-carboxamide as starting material, and enzyme kinetic evaluation of N-(beta-D-glucopyranosyl)-1,2,4-triazolecarboxamides as glycogen phosphorylase inhibitors, overview. No inhibition by 3b and 4b. Ki values are calculated from the IC50 values by the ChengPrusoff equation: Ki = IC50/(1 + [S]/Km). Comparison of the relative energies of different tautomers and conformations of the 1,2,4-triazole for models of the N-(beta-D-glucopyranosyl)-1,2,4-triazolecarboxamides, quantum mechanics/molecular mechanics calculations and modeling. No inhibition by 3b and 4b
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additional information
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no or poor inhibition by ribose 5-phosphate, glucose 6-phosphate, fructose-1,6-bisphosphate, ADP and UDP
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additional information
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not inhibited by fructose 6-phosphate; not inhibited by fructose, sucrose, dihydroxyacetone phosphate, 6-phosphogluconate, 2-phosphoglycollate, 2-phosphoglycerate, pyruvate
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additional information
structure-based inhibitor design targeting glycogen phosphorylase b, virtual screening, synthesis, biochemical and biological assessment of N-acyl-beta-D-glucopyranosylamines, overview. Determination of the effects of the enzyme inhibitors on conversion of glycogen phosphorylase a to b
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additional information
slight inhibition by azobenzene glucosides. After irradiation and subsequent conversion to the (Z)-form, the inhibitory potency of the azobenzene glucoside does not significantly change for the rat muscle enzyme form. The anomeric ratio of alpha:beta form is approximately 1:4
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additional information
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not inhibited by 2-mercaptoethanol; not inhibited by agarose; not inhibited by gibberellic acid, indolyl-3-acetic acid; not inhibited by Ni2+
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additional information
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not inhibited by 2-mercaptoethanol; not inhibited by Sr2+
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