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Information on EC 2.4.1.1 - glycogen phosphorylase and Organism(s) Oryctolagus cuniculus and UniProt Accession P00489
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2.4.1.1 glycogen phosphorylaseIUBMB Comments
This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.
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Word Map
- 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
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
glycogen phosphorylase, phosphorylase a, phosphorylase b, myophosphorylase, muscle phosphorylase, glycogen phosphorylase b, glycogen phosphorylase a, muscle glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycogen phosphorylase b
-
1,4-alpha-glucan phosphorylase
-
-
-
-
alpha-glucan phosphorylase
-
-
-
-
amylopectin phosphorylase
-
-
-
-
amylophosphorylase
-
-
-
-
glucan phosphorylase
-
-
-
-
glucosan phosphorylase
-
-
-
-
glycogen phosphorylase
glycogen phosphorylase b
-
-
granulose phosphorylase
-
-
-
-
maltodextrin phosphorylase
-
-
-
-
muscle phosphorylase
-
-
-
-
muscle phosphorylase a and b
-
-
-
-
myophosphorylase
-
-
-
-
phosphorylase a
phosphorylase, alpha-glucan
-
-
-
-
polyphosphorylase
-
-
-
-
potato phosphorylase
-
-
-
-
starch phosphorylase
-
-
-
-
additional information
-
enzyme belongs to the GT-B-fold glycosyltransferase superfamily
glycogen phosphorylase
-
-
-
-
phosphorylase a
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
catalytic site structure
[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
determination and analysis of rgulatory binding sites
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-glucan:phosphate alpha-D-glucosyltransferase
This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. Some of these enzymes catalyse the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. The accepted name of the enzyme should be modified for each specific instance by substituting "glycogen" with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.
CAS REGISTRY NUMBER
COMMENTARY
9035-74-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
polysaccharide substrate is glycogen
-
-
r
pyridylamino-maltohexaose + alpha-D-glucose 1-phosphate
pyridylamino-maltoheptaose + phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
alpha-D-glucan + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
-
r
glycogen + alpha-D-glucose 1-phosphate
glycogen + phosphate
-
-
-
-
?
maltoheptaose + glucose 1-phosphate
maltooctaose + phosphate
-
best substrate
-
r
maltohexaose + glucose 1-phosphate
maltoheptaose + phosphate
-
-
-
r
maltopentaose + glucose 1-phosphate
maltohexaose + phosphate
-
-
-
r
maltotetraose + glucose 1-phosphate
maltopentaose + phosphate
-
-
-
ir
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
glycogen + glucose 1-phosphate
glycogen + phosphate
-
-
-
?
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
bovine liver glycogen, effects of the C-terminal domain on enzyme binding to glycogen, overview
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is glycogen, first step in glycogen breakdown removing one glucose at a time
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is glycogen, phosphorolysis is the preferred reaction
-
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
minimum chain length requirement for efficient activity: 5 glucose units per maltodextrin molecule
-
r
(maltodextrin)n-1 + glucose 1-phosphate
(maltodextrin)n + phosphate
-
minimum chain length requirement for efficient activity: 4 glucose units per maltodextrin molecule
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
glycogen from oyster
-
r
glycogen + glucose 1-phosphate
glycogen + phosphate
-
yeast or rabbit enzyme
-
r
starch + glucose 1-phosphate
starch + phosphate
-
soluble starch
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
r
additional information
?
-
mastoparan binds to the enzyme to negatively regulate sarcoplasmic reticular Ca2+ release in skeletal muscle involving the ryanodine receptor, overview
-
-
?
additional information
?
-
-
mastoparan binds to the enzyme to negatively regulate sarcoplasmic reticular Ca2+ release in skeletal muscle involving the ryanodine receptor, overview
-
-
?
additional information
?
-
the enzyme specifically binds to mastoparan, a wasp venom toxin
-
-
?
additional information
?
-
-
the enzyme specifically binds to mastoparan, a wasp venom toxin
-
-
?
additional information
?
-
the assay of enzyme activity at micromolar concentration of maltooligosyl-substrate is about 100 times lower than that in conventional enzyme assays using glycogen
-
-
?
additional information
?
-
-
GPa reduces arsenate (As(V)) to the more toxic arsenite (As(III)) in a glutathione (GSH)-dependent fashion
-
-
?
additional information
?
-
-
a maltotetraosyl residue comprising the non-reducing-end of a pyridylaminated maltooligosaccharide is indispensable for the chain-lengthening action of phosphorylase
-
-
?
additional information
?
-
-
the catalytic site binds glucose 1-phosphate, glycogen, glucose, and glucose analogues
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
r
(1,4-alpha-D-glucosyl)n + phosphate
(1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate
-
polysaccharide substrate is glycogen, first step in glycogen breakdown removing one glucose at a time
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
-
-
-
r
additional information
?
-
mastoparan binds to the enzyme to negatively regulate sarcoplasmic reticular Ca2+ release in skeletal muscle involving the ryanodine receptor, overview
-
-
?
additional information
?
-
-
mastoparan binds to the enzyme to negatively regulate sarcoplasmic reticular Ca2+ release in skeletal muscle involving the ryanodine receptor, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
-
(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
-
1-(2-naphthyl)-3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
1-phenyl-3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
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
3-(2',3',4',6'-tetra-O-benzoyl-beta-D-glucopyranosyl)-1H-1,2,4-triazol-5(4H)-one
-
3-(beta-D-glucopyranosyl)-1-(2-naphthyl)-1H-1,2,4-triazol-5(4H)-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
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
-
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
CH3Hg+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA
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
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
gallic acid
competitive inhibitor with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP
Hg2+
irreversible inhibition, partial reactivation of the enzyme by GSH, but not by EDTA
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)-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-[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-[[([1,1'-biphenyl]-4-yl)oxy]acetyl]-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
-
(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
-
-
(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,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-(beta-D-glucopyranosyl)-5-ethynyluracil
-
cytotoxic effect on Hep-G2 cells
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
-
-
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-dihydroisooxazolyl oleanolic acid benzyl ester
-
50% inhibition at 0.0196 mM
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-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-(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
-
-
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
6-[(4-methylphenyl)amino]hexyl (3beta)-3-hydroxyolean-12-en-28-oate
-
-
alpha-cyclodextrin
-
mixed-type competitive inhibition, inhibitor is not bound into the enzyme crystal
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
bis(6-([(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy)hexyl) (2R)-2-hydroxybutanedioate
-
-
chrysin
-
50% inhibition of phosphorylated, active enzyme above 0.0275 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0153 mM
cyanidin
-
50% inhibition of phosphorylated, active enzyme at 0.003 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.009 mM
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
delphinidin
-
50% inhibition of phosphorylated, active enzyme at 0.0031 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0107 mM
ellagic acid
-
50% inhibition of phosphorylated, active enzyme at 0.0032 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0121 mM
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
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
-
-
luteolin
-
50% inhibition of phosphorylated, active enzyme at 0.0156 mM, 50% inhibition of unphosphorylated, adenosine monophosphate-activated enzyme at 0.0288 mM
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
-
-
N-([(2E)-2-[4-(trifluoromethyl)benzylidene]hydrazinyl]carbonothioyl)-beta-D-glucopyranosylamine
-
-
N-([4-[(benzyloxy)carbonyl]benzoyl]carbamoyl)-beta-D-glucopyranosylamine
-
-
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-[[(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-[[4-(methoxycarbonyl)benzoyl]carbamoyl]-beta-D-glucopyranosylamine
-
-
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
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
-
-
[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
-
-
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
alpha-D-glucopyranosyl fluoride
-
strong inhibition of phosphorylase b, kinetics
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
-
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
additional information
pentacyclic triterpenes may exert hypoglycemic effects, at least in part, through glycogen phosphorylase inhibition
-
additional information
-
pentacyclic triterpenes may exert hypoglycemic effects, at least in part, through glycogen phosphorylase inhibition
-
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
-
additional information
molecular and kinetic mechanisms of enzyme inhibition by mercury, overview
-
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
-
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
-
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
-
additional information
synthesis of possible isomers of C-(2-deoxy-d-arabino-hex-1-enopyranosyl)-oxadiazoles and evaluation as glycogen phosphorylase inhibitors, overview
-
additional information
-
synthesis of possible isomers of C-(2-deoxy-d-arabino-hex-1-enopyranosyl)-oxadiazoles and evaluation as glycogen phosphorylase inhibitors, overview
-
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
-
additional information
-
binding and inhibition mechanism, no inhibition by (2,3,6-tri-O-methyl)-gamma-cyclodextrin
-
additional information
-
preference for hydrophobic group at C-28 of maslinic acid for enzyme inhibition
-
additional information
-
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
-
additional information
-
inhibitor screening, native ligand docking of inhibitor tautomers supplemented by QM/MM calculations, modeling of free state ligands and bound ligands, detailed overview
-
additional information
-
inhibitory efficiency and inhibition kinetics of beta-D-glucopyranosyl-thiosemicarbazone derivatives as glycogen phosphorylase inhibitors, binding analysis, overview
-
additional information
-
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
-
additional information
-
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
-
additional information
-
synthesis of glucopyranonucleosides in the 5-alkynyl- and 6-alkylfurano[2,3-d]pyrimidine series, overview
-
additional information
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sulfate
-
activates the wild-type but not the N-terminally truncated mutant
5'-AMP
-
phosphorylase Ia, half-maximal activity at 0.25 mM, phosphorylase IIIa, half-maximal activity at 6 mM
AMP
-
quantification of the allosteric effect and the thermodynamic effect of AMP on phosphorylase b, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
when maltohexaose is used as the substrate, typical Michaelis-Menten curves ar obtained
-
additional information
additional information
-
comparison of muscle phosphorylases of various animals
-
additional information
additional information
-
allosteric kinetics, overview
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0393
(2R,3R,4S,5R,6R)-3,4,5,9-tetrahydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione
-
0.0031
(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione
pH 6.8, 30°C
0.00063
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(2-naphthyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
pH 6.8
0.0066
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(4-methoxyphenyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
pH 6.8
0.0079
(5R,7R,8R,9S,10R)-7-(hydroxymethyl)-3-(4-toluyl)-1,6-dioxa-2-azaspiro[4,5]dec-2-ene-8,9,10-triol
pH 6.8
0.191
3-(beta-D-glucopyranosyl)-1-phenyl-1H-1,2,4-triazol-5(4H)-one
pH and temperature not specified in the publication
5.9
beta-D-glucopyranosyl bismethoxyphosphoramidate
pH 6.8, 30°C, versus alpha-D-glucose 1-phosphate, synthesis reaction
1.7
D-glucose
pH and temperature not specified in the publication
0.04868
N-[(2E)-3-(5,6,7,8-tetrahydronaphthalen-2-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
pH and temperature not specified in the publication
0.0035
N-[(2E)-3-(naphthalen-2-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
pH and temperature not specified in the publication
0.00514
N-[(2E)-3-([1,1'-biphenyl]-4-yl)prop-2-enoyl]-beta-D-glucopyranosylamine
pH and temperature not specified in the publication
0.00498
N-[(2E)-3-[4-(propan-2-yl)phenyl]prop-2-enoyl]-beta-D-glucopyranosylamine
pH and temperature not specified in the publication
0.07529
N-[(2R)-2-methyl-3-[4-(propan-2-yl)phenyl]propanoyl]-beta-D-glucopyranosylamine
pH and temperature not specified in the publication
0.3769
N-[(3S)-3-(4-ethylphenyl)butanoyl]-beta-D-glucopyranosylamine
pH and temperature not specified in the publication
0.00825
N-[[([1,1'-biphenyl]-4-yl)oxy]acetyl]-beta-D-glucopyranosylamine
pH and temperature not specified in the publication
0.00016
(1S)-1,5-anhydro-D-glucitol-spiro[1.5]-3-(2-naphthyl)-1,4,2-oxathiazole
-
-
0.0082
(1S)-1,5-anhydro-D-glucitol-spiro[1.5]-3-(4-methoxyphenyl)-1,4,2-oxathiazole
-
-
0.32
(5R,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dione
-
pH and temperature not specified in the publication
0.015
(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
-
pH and temperature not specified in the publication
0.0051
(5S,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-2-thioxo-6-oxa-1,3-diazaspiro[4.5]decan-4-one
-
pH and temperature not specified in the publication
0.0031
(5S,7R,8S,9S,10R)-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dione
-
pH and temperature not specified in the publication
0.48
1,3,5-tris-4'-2''-[3'''-C-(beta-D-glucopyranosyl)-1''',2''',4'''-oxadiazol-5'''-yl]ethyl-1',2',3'-triazol-1'-ylmethylbenzene
-
-
0.535
1,3,5-tris[3'-C-(beta-D-glucopyranosyl)-1',2',4'-oxadiazol-5'-yl]-benzene
-
-
3.204
1-(beta-D-glucopyranosyl)-5-(hept-1-yn-1-yl)uracil
-
pH 6.8, 30°C
0.303
1-(beta-D-glucopyranosyl)-5-(pent-1-yn-1-yl)uracil
-
pH 6.8, 30°C
0.0334
3-(beta-D-glucopyranosyl)-6-pentyl-2,3-dihydro-furano-[2,3-d]pyrimidin-2-one
-
pH 6.8, 30°C
0.0324
3-(beta-D-glucopyranosyl)-6-propyl-2,3-dihydro-furano-[2,3-d]pyrimidin-2-one
-
pH 6.8, 30°C
0.0088
5-(beta-D-glucopyranosyl)-3-(4-methylphenyl)-1,2,4-oxadiazole
-
-
0.02
N-(3-carboxypropanoyl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.37
N-(acetylcarbamoyl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.049
N-(azidoacetyl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.0046
N-(benzoylcarbamoyl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
5.9
N-(dimethoxyphosphoryl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.01
N-(naphthalen-2-ylcarbonyl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.075
N-(trifluoroacetyl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.15
N-([4-[(benzyloxy)carbonyl]benzoyl]carbamoyl)-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.032
N-acetyl-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.14
N-carbamoyl-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.081
N-phenyl-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.006
N-[(4-aminobenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.085
N-[(4-carboxybenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.0044
N-[(4-chlorobenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.0063
N-[(4-hydroxybenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.0032
N-[(4-methoxybenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.0023
N-[(4-methylbenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.0033
N-[(4-nitrobenzoyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.0037
N-[(biphenyl-4-ylcarbonyl)carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.21
N-[methoxy(oxo)acetyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.004
N-[[4-(methoxycarbonyl)benzoyl]carbamoyl]-beta-D-glucopyranosylamine
-
pH and temperature not specified in the publication
0.44
alpha-D-glucopyranosyl fluoride
-
phosphorylase b, at 1 mM vs. glucose 1-phosphate
0.71
alpha-D-glucopyranosyl fluoride
-
phosphorylase b, at 1 mM vs. phosphate
0.0023
glucopyranosylidene spirothiohydantoin
-
muscle phosphorylase b, vs. phosphate
0.0028
glucopyranosylidene spirothiohydantoin
-
muscle phosphorylase b, vs. glycogen
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00895
2-amino-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-N-(3-trifluoromethyl-phenyl)-benzamide
Oryctolagus cuniculus
-
0.0309
2-amino-4-fluoro-N-(3-fluoro-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.0239
2-amino-4-fluoro-N-(4-methoxy-phenyl)-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.00268
2-amino-N-(3-amino-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.00987
2-amino-N-(3-cyano-phenyl)-4-fluoro-5-(1-methyl-1H-imidazol-2-ylsulfanyl)-benzamide
Oryctolagus cuniculus
-
0.08
3-(beta-D-glucopyranosyl)-1-(2-naphthyl)-1H-1,2,4-triazol-5(4H)-one
Oryctolagus cuniculus
pH and temperature not specified in the publication
0.35
3-(beta-D-glucopyranosyl)-1-phenyl-1H-1,2,4-triazol-5(4H)-one
Oryctolagus cuniculus
pH and temperature not specified in the publication
0.00114
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
Oryctolagus cuniculus
pH 6.0, 37°C
0.0116
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
Oryctolagus cuniculus
pH 6.0, 37°C
0.0265
benzyl 3-O-propargyl-3beta-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
pH 6.0, 37°C
0.0125
N-(3-cyano-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
Oryctolagus cuniculus
-
0.0187
N-(3-fluoro-phenyl)-2-[4-(2-fluoro-phenyl)-piperazin-1-yl]-acetamide
Oryctolagus cuniculus
-
0.0133
(2alpha,3beta)-2,3-bis(acetyloxy)olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0252
(2alpha,3beta)-2,3-bis(butanoyloxy)olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0105
(2alpha,3beta)-2,3-bis(propanoyloxy)olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00625
(2beta,3alpha)-2,3-dihydroxyolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0011
(2beta,3alpha)-2,3-dihydroxyurs-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00325
(3beta)-28-[(2-[[2-(acetylamino)ethyl]amino]ethyl)amino]-28-oxoolean-12-en-3-yl acetate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0152
(3beta)-28-[(3-aminopropyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
Oryctolagus cuniculus
-
-
0.0035
(3beta)-28-[(6-aminohexyl)amino]-28-oxolup-20(29)-ene-3,23-diyl diacetate
Oryctolagus cuniculus
-
-
0.0309
(3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0102
(3beta)-N-(6-aminohexyl)-3,23-dihydroxylup-20(29)-en-28-amide
Oryctolagus cuniculus
-
-
0.0031
(3beta,12alpha,13xi)-3,12-dihydroxyoleanan-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00259 - 0.0026
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
0.0251
(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
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.014
(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
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0493
1'-(methylsulfonyl)pyrazolo[4,3-b]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0372
1'-propanoylpyrazolo[4,3-b]olean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000044 - 0.000059
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
0.000014 - 0.000024
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
0.0123
1-[6-(acetyloxy)hexyl] 4-(7-[[(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy]heptyl) (2R)-2-hydroxybutanedioate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0191
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
Oryctolagus cuniculus
-
-
0.0186
2,3,4,6-tetra-O-acetyl-1-O-[(2alpha,3beta)-2,3-dihydroxy-28-oxoolean-12-en-28-yl]-beta-D-glucopyranose
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0256
2-(phenylamino)ethyl (3beta)-3-hydroxyurs-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0254
2-bromoethyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0225
2-ethoxy-2-oxoethyl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00153
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
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00223
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
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0063
2-[3'-(benzylamino)-2'-oxopyridin-1'(2H)-yl]-N-(3'',4''-dichlorobenzyl)acetamide
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00043 - 0.000915
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
0.0247
4-oxo-4-[(pyrazolo[4,3-b]olean-12-en-28-yl)oxy]butanoic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0126
6-(butylamino)hexyl (3beta)-3-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0141
6-aminohexyl (3beta)-3-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0281
6-[(4-methylphenyl)amino]hexyl (3beta)-3-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00669
benzyl (2beta,3alpha)-2,3-dihydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00125
benzyl (2beta,3alpha)-2,3-dihydroxyurs-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00539
benzyl (3beta)-3-[(pyridinium-1-ylacetyl)oxy]olean-12-en-28-oate chloride
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0175
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
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0078
benzyl (3beta)-3-[([4-[(dodecanoyloxy)methyl]-1H-1,2,3-triazol-1-yl]acetyl)oxy]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0277
benzyl (3beta)-3-[[(4-[[(phenylacetyl)oxy]methyl]-1H-1,2,3-triazol-1-yl)acetyl]oxy]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0065
benzyl (3beta,12alpha,13xi)-3,12-dihydroxyoleanan-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00535
benzyl (3beta,12beta,13xi)-3,12-dihydroxyoleanan-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.132
benzyl 1'-(2,4-dichlorobenzyl)pyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.057
benzyl 1'-(carboxymethyl)pyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.063
benzyl 1'-benzylpyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0999
benzyl 1'-methylpyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.111
benzyl 1'-[(ethoxycarbonyl)methyl]pyrazolo[4,3-b]olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0201
benzyl 3beta-(2-(diethylamino)acetoxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0126
benzyl 3beta-(2-chloroacetoxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00213
benzyl 3beta-(4-aminobenzoyloxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0161
benzyl 3beta-(4-nitrobenzoyloxy)olean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0123
bis(6-([(3beta)-3-hydroxy-28-oxoolean-12-en-28-yl]oxy)hexyl) (2R)-2-hydroxybutanedioate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0207
hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyl) (3beta,3'beta)-bis(3-hydroxyolean-12-en-28-oate)
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00325
iminobis[ethane-2,1-diylimino(3beta)-28-oxoolean-12-ene-28,3-diyl]diacetate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0112
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](4-hydroxyphenyl)ethanoate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0239
methyl (2S)-[[(2alpha,3beta)-2,3-bis(acetyloxy)-28-oxours-12-en-28-yl]amino](phenyl)ethanoate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.00114
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
Oryctolagus cuniculus
-
pH 7.2, 22°C
524.3
N-([(2E)-2-[4-(trifluoromethyl)benzylidene]hydrazinyl]carbonothioyl)-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
0.0342
N-benzyl-2-[3'-(benzylamino)-2'-oxopyridin-1'(2H)-yl]acetamide
Oryctolagus cuniculus
-
pH 7.2, 22°C
370
N-[[(2E)-2-(2-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
26.6
N-[[(2E)-2-(2-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
484.2
N-[[(2E)-2-(2-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
50.4
N-[[(2E)-2-(3-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
23.2
N-[[(2E)-2-(3-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
180
N-[[(2E)-2-(3-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
93.2
N-[[(2E)-2-(4-bromobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
28.3
N-[[(2E)-2-(4-chlorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
5.7
N-[[(2E)-2-(4-fluorobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
340.5
N-[[(2E)-2-(4-hydroxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
406.5
N-[[(2E)-2-(4-methoxybenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
192.4
N-[[(2E)-2-(4-methylbenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
25.7
N-[[(2E)-2-(4-nitrobenzylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
200
N-[[(2E)-2-(pyridin-4-ylmethylidene)hydrazinyl]carbonothioyl]-beta-D-glucopyranosylamine
Oryctolagus cuniculus
-
pH 6.8, temperature not specified in the publication
0.0231
prop-2-en-1-yl (2beta)-2-hydroxyolean-12-en-28-oate
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0207
[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
Oryctolagus cuniculus
-
pH 7.2, 22°C
additional information
additional information
Oryctolagus cuniculus
-
kinetics of inhibition of the forward reaction
-
0.00259
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.0026
(3beta,3'beta)-3,3'-[hexane-1,6-diylbis(1H-1,2,3-triazole-1,4-diylmethanediyloxy)]bisolean-12-en-28-oic acid
Oryctolagus cuniculus
-
pH 7.2, 22°C
0.000044
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase a, pH 7.4, 25°C
0.000059
1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase b, pH 7.4, 25°C
0.000014
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase a, pH 7.4, 25°C
0.000024
1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid
Oryctolagus cuniculus
-
phosphorylase b, pH 7.4, 25°C
0.00043
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
Oryctolagus cuniculus
-
phosphorylase a, pH 7.4, 25°C
0.000915
4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid
Oryctolagus cuniculus
-
phosphorylase b, pH 7.4, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
purified muscle enzyme, pH and temperature not specified in the publication
70
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
mastoparan dissociates the enzyme from the heavy fraction of the sarcoplasmic reticulum, i.e. HSR
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
mutations that impair glycogen phosphorylase activity leads to McArdle's disease which is characterized by exercise intolerance, muscle fatigue, and cramps. The irreversible inhibition of the enzyme might represent one of the mechanisms that contribute to mercury-dependent muscle toxicity
metabolism
muscle glycogen phosphorylase is the rate-limiting enzyme of glycogen breakdown in skeletal muscle
physiological function
-
molecular crowding by 1 M trimethylamine N-oxide stimulates phosphorylase b and phosphorylase kinase combined binding on glycogen particles. Phosphorylase kinase binding to glycogen particles containing adsorbed phosphorylase shows a two-stage character. At the initial stage, limited size particles with hydrodynamic radius of about 220 nm are formed, whereas the second stage is accompanied by linear growth of hydrodynamic radius. Flavin adenine dinucleotide selectively inhibits phosphorylase kinase binding at the second stage, while its binding in the second stage does not involve phosphorylase b
additional information
additional information
modeling of the glycogen phosphorylase b GPb receptor structure using the 2.15 A resolution GPb-N-4-phenylbenzoyl-2-N'-beta-D-glycopyrglycopyranosyl urea crystal complex, PDB ID 2QLN
additional information
the enzyme activity consists of two activities: (i) binding to the glycogen molecule and (ii) phosphorolysis of the non-reducing-end glucose residues. Activity (i) is mainly due to the activities of the two storage sites, which depend on the ionic strength of the medium and are directly inhibited by cyclodextrins. Activity (ii), the total activity of the two catalytic sites, exhibit relatively little ionic strength dependence. Because the combined activity of (i) and (ii) is deduced using glycogen as an assay substrate, the sole activity of (ii) must be measured using small maltooligosyl-substrates
additional information
-
phosphorylase a is produced and isolated utilizing purified phosphorylase b and commercially available phosphorylase kinase
additional information
-
structural analysis of molecular elements that govern molecular recognition by the catalytic site of the enzyme with emphasis in the beta-pocket environment, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PYGM_RABIT
843
0
97289
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
97000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
biologically active form, each subunit has two distinct maltooligosaccharide binding sites: a storage site and a catalytic site
additional information
additional information
proteolytic digestion pattern, amino acid sequence determination
additional information
-
proteolytic digestion pattern, amino acid sequence determination
additional information
-
phosphorylase a dissociates into active dimers in the presence of high salt concentration, glucose or glycogen, human enzyme at 5 mg/ml protein concentration, the rabbit enzyme remains a tetramer even at 1 mg/ml
additional information
-
enzyme has 2 distinct Rossmann domains separated by a large cleft that permits important flexibility, crystal structure, 1A8I, comparison with the glycogen synthase and amino acid sequence alignment
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
each subunit has two distinct maltooligosaccharide binding sites: a storage site and a catalytic site
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the cocrystallized rabbit muscle glycogen phosphorylase bFR258900 complex, 2.2 A resolution
determination of crystal structures of the glycogen phosphorylase b-gallic acid and glycogen phosphorylase b-ellagic acid complexes, overview
enzyme complexed with inhibitor beta-D-glucopyranosyl bismethoxyphosphoramidate by soaking of native enzyme crystals in 150 mM inhibitor 7.5 h prior to diffraction data collection, X-ray diffraction structure determination and analysis at 1.83 A resolution, modeling
in complex with inhibitors (2R,3R,4S,5R,6R)-3,4,5-trihydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione, (2R,3R,4S,5R,6R)-3,4,5,9-tetrahydroxy-2-hydroxymethyl-7,9-diaza-1-oxa-spiro[4,5]decane-8,10-dione, 1-deoxy-1-methoxycarbonylamino-beta-D-glucopyranose. Inhibitors bind at the active site of the enzyme and induce minor movements of the side chains of D283 and N284 that block access of the substrate glycogen to the catalytic site
purified native muscle enzyme, soaking of crystals in a 5 mM inhibitor solution in 10 mM sodium N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonate, pH 6.7, containing 0.1 mM EDTA, and 0.02% w/v sodium azide at room temperature for 2 h prior to data collection, X-ray diffraction structure determination and analysis at 1.85-2.15 A resolution
crystal structure of glycogen phosphorylase beta-glucopyranosylidene spirothiohydantoin complex at 2.26 A resolution
-
crystal structure of muscle glycogen phosphorylase a in complex with glucose and in complex with both glucose and CP320626 at 2.0 A resolution
-
enzyme in complex with different inhibitory N-(4-substituted-benzoyl)-N'-(beta-D-glucopyranosyl)urea compounds, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular modelling
-
in comlex with inhibitor 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, localization of two inhibitor molecules at the enzyme dimer interface
-
in complex with inhibitors beta-D-glucopyranosyl 1-oxalylamide, beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide, beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide. Inhibitors accomodate at the catalytic site at approximately the position of alpha-D-glucose and stabilize the T-state conformation
-
native enzyme crystals are soaked in 150 mM gamma-cyclodextrin, or 15 mM beta-cyclodextrin, respectively, and 70 mM maltopentaose or maltoheptaose in fesh solutions of mother liquor containing 10 mM MES, pH 6.7, 0.1 mM EDTA, at least 2 h at room temperature, X-ray diffraction structure determination and analysis of enzyme-inhibitor complexes at 2.3 A and 1.94 A resolution, respectively
-
purified enzyme bound to different inhibitors, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution, structure modeling
-
purified enzyme bound to diverse inhibitor molecules, X-ray diffraction structure determination and analysis, modeling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D238A
-
15fold decrease in Vmax, 10fold decrease in Km for glucose 1-phosphate, 10fold increase in Ka for AMP, 10-20fold increase in Ki for glucose
D238N
-
15fold decrease in Vmax, 10fold decrease in Km for glucose 1-phosphate, 10fold increase in Ka for AMP, 10-20fold increase in Ki for glucose
F285L
-
2fold decrease in Vmax, 10fold decrease in affinity for caffeine, 3fold increase in Ka for AMP
additional information
-
construction of an N-terminal truncated mutant DELTA2-17
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0
-
heart isozyme Ib or IIIb: t1/2: 2.4-2.9 min, heart isozyme Ia: stable in the presence of 2-mercaptoethanol
48
additional information
-
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
48
-
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
-
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from muscle, to homogeneity by several chromatographic steps and preparative SDS-PAGE
native glycogen phosphorylase b from skeletal muscle, glycogen phosphorylase a is prepared from glycogen phosphorylase b by phosphorylation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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. Test system for the study of the effects of macromolecular crowding induced by osmolytes on aggregation of proteins
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is an important target for is a validated target for the development of type 2 diabetes treatments and the discovery of hypoglycaemic agents, both synthetic and natural
analysis
-
a highly sensitive and convenient assay for glycogen phosphorylase activity by analysing its chainlengthening action on a fluorogenic maltooligosaccharide derivative in a glucose-1-phosphate-rich medium. A maltotetraosyl residue comprising the non-reducing-end of a pyridylaminated maltooligosaccharide is indispensable for the chain-lengthening action of phosphorylase, and pyridylaminated maltohexaose is the most suitable substrate. Pyridylaminated maltoheptaose produced by the chain elongation reaction can be isolated and quantified at 10 fmol. Method has about 1000 times greater sensitivity than the spectrophotometric phosphate assay
biotechnology
-
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. Test system for the study of the effects of macromolecular crowding induced by osmolytes on aggregation of proteins
drug development
additional information
-
the enzyme is a target for development of inhibitors to prevent unwanted hepatic glycogenolysis under high glucose conditions in treatment of diabetes type 2 in humans
drug development
-
glycogen phosphorylase is an active target of research in search of inhibitors for the treatment of type II diabetes
drug development
-
pentacyclic triterpenes, as inhibitors of glycogen phosphorylase, hold promise for the treatment of type-2 diabetes and other diseases with disorders in glycogen metabolism
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JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Madsen, N.
The inhibition of glycogen phosphorylase by uridine diphosphate glucose
Biochem. Biophys. Res. Commun.
6
310-313
1961
Agrobacterium tumefaciens, Oryctolagus cuniculus
Tanabe, S.; Kobayashi, M.; Matsuda, K.
Yeast glycogen phosphorylase: kinetic properties compared with muscle and potato enzymes
Agric. Biol. Chem.
52
757-764
1988
Saccharomyces cerevisiae, Oryctolagus cuniculus, Solanum tuberosum
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Kobayashi, M.; Takagi, S.; Matsuda, K.; Ichishima, E.
Inhibiton of alpha-amylase and phosphorylase by cyclodextrin-dialdehyde
Agric. Biol. Chem.
52
2703-2708
1988
Saccharomyces cerevisiae, Oryctolagus cuniculus, Solanum tuberosum
-
Kamogawa, A.; Fukui, T.
Inhibition of -glucan phosphorylase by bisulfite competition at the phosphate binding site
Biochim. Biophys. Acta
302
158-166
1973
Oryctolagus cuniculus, Solanum tuberosum
Assaf, S.A.; Yunis, A.A.
Physicochemical and catalytic properties of crystallized human muscle glycogen phosphorylase
Ann. N. Y. Acad. Sci.
210
139-152
1973
Carcharhinus falciformis, Oryctolagus cuniculus, Homarus americanus, Homo sapiens
Schliselfeld, L.H.
Comparative studies of phosphorylase isozymes from the rabbit
Ann. N. Y. Acad. Sci.
210
181-191
1973
Oryctolagus cuniculus, Sus scrofa
Soman, G.; Philip, G.
Aromatic compounds as allosteric inhibitors of glycogen phosphorylase b
Biochim. Biophys. Acta
358
359-362
1974
Oryctolagus cuniculus
-
Ariki, M.; Fukui, T.
Inhibition of alpha-glucan phosphorylase by alpha-D-glucopyranosyl fluoride
J. Biochem.
78
1191-1199
1975
Oryctolagus cuniculus, Solanum tuberosum
Khandelwal, R.L.
Some properties of purified phosphoprotein phosphatases from rabbit liver
Biochim. Biophys. Acta
485
379-390
1977
Oryctolagus cuniculus
Vereb, G.; Fodor, A.; Bot, G.
Kinetic characterization of rabbit skeletal muscle phosphorylase ab hybrid
Biochim. Biophys. Acta
915
19-27
1987
Oryctolagus cuniculus
Klinov, S.V.; Kurganov, B.I.
Kinetic mechanism of activation of muscle glycogen phosphorylase b by adenosine 5'-monophosphate
Arch. Biochem. Biophys.
312
14-21
1994
Oryctolagus cuniculus
Buchbinder, J.L.; Fletterick, R.J.
Role of the active site gate of glycogen phosphorylase in allosteric inhibition and substrate binding
J. Biol. Chem.
271
22305-22309
1996
Oryctolagus cuniculus
Oikonomakos, N.G.; Kosmopoulou, M.; Zographos, S.E.; Leonidas, D.D.; Chrysina, E.D.; Somsak, L.; Nagy, V.; Praly, J.P.; Docsa, T.; Toth, B.; Gergely, P.
Binding of N-acetyl-N'-beta-D-glucopyranosyl urea and N-benzoyl-N'-beta-D-glucopyranosyl urea to glycogen phosphorylase b: kinetic and crystallographic studies
Eur. J. Biochem.
269
1684-1696
2002
Oryctolagus cuniculus
Oikonomakos, N.G.; Chrysina, E.D.; Kosmopoulou, M.N.; Leonidas, D.D.
Crystal structure of rabbit muscle glycogen phosphorylase a in complex with a potential hypoglycaemic drug at 2.0 A resolution
Biochim. Biophys. Acta
1647
325-332
2003
Oryctolagus cuniculus
Hirata, Y.; Atsumi, M.; Ohizumi, Y.; Nakahata, N.
Mastoparan binds to glycogen phosphorylase to regulate sarcoplasmic reticular Ca2+ release in skeletal muscle
Biochem. J.
371
81-88
2003
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Chrysina, E.D.; Kosmopoulou, M.N.; Kardakaris, R.; Bischler, N.; Leonidas, D.D.; Kannan, T.; Loganathan, D.; Oikonomakos, N.G.
Binding of beta-D-glucopyranosyl bismethoxyphosphoramidate to glycogen phosphorylase b: kinetic and crystallographic studies
Bioorg. Med. Chem.
13
765-772
2005
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Buschiazzo, A.; Ugalde, J.E.; Guerin, M.E.; Shepard, W.; Ugalde, R.A.; Alzari, P.M.
Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation
EMBO J.
23
3196-3205
2004
Oryctolagus cuniculus
Pinotsis, N.; Leonidas, D.D.; Chrysina, E.D.; Oikonomakos, N.G.; Mavridis, I.M.
The binding of beta- and gamma-cyclodextrins to glycogen phosphorylase b: kinetic and crystallographic studies
Protein Sci.
12
1914-1924
2003
Oryctolagus cuniculus
Eronina, T.B.; Chebotareva, N.A.; Kurganov, B.I.
Influence of osmolytes on inactivation and aggregation of muscle glycogen phosphorylase b by guanidine hydrochloride. Stimulation of protein aggregation under crowding conditions
Biochemistry (Moscow)
70
1020-1026
2005
Oryctolagus cuniculus
Hadjiloi, T.; Tiraidis, C.; Chrysina, E.D.; Leonidas, D.D.; Oikonomakos, N.G.; Tsipos, P.; Gimisis, T.
Binding of oxalyl derivatives of beta-d-glucopyranosylamine to muscle glycogen phosphorylase b
Bioorg. Med. Chem.
14
3872-3882
2006
Oryctolagus cuniculus
Chen, J.; Liu, J.; Zhang, L.; Wu, G.; Hua, W.; Wu, X.; Sun, H.
Pentacyclic triterpenes. Part 3: Synthesis and biological evaluation of oleanolic acid derivatives as novel inhibitors of glycogen phosphorylase
Bioorg. Med. Chem. Lett.
16
2915-2919
2006
Oryctolagus cuniculus
Wen, X.; Zhang, P.; Liu, J.; Zhang, L.; Wu, X.; Ni, P.; Sun, H.
Pentacyclic triterpenes. Part 2: Synthesis and biological evaluation of maslinic acid derivatives as glycogen phosphorylase inhibitors
Bioorg. Med. Chem. Lett.
16
722-726
2006
Oryctolagus cuniculus
Birch, A.M.; Kenny, P.W.; Oikonomakos, N.G.; Otterbein, L.; Schofield, P.; Whittamore, P.R.; Whalley, D.P.
Development of potent, orally active 1-substituted-3,4-dihydro-2-quinolone glycogen phosphorylase inhibitors
Bioorg. Med. Chem. Lett.
17
394-399
2007
Oryctolagus cuniculus, Homo sapiens
Jakobs, S.; Fridrich, D.; Hofem, S.; Pahlke, G.; Eisenbrand, G.
Natural flavonoids are potent inhibitors of glycogen phosphorylase
Mol. Nutr. Food Res.
50
52-57
2006
Oryctolagus cuniculus
Watson, K.A.; Chrysina, E.D.; Tsitsanou, K.E.; Zographos, S.E.; Archontis, G.; Fleet, G.W.; Oikonomakos, N.G.
Kinetic and crystallographic studies of glucopyranose spirohydantoin and glucopyranosylamine analogs inhibitors of glycogen phosphorylase
Proteins
61
966-983
2005
Oryctolagus cuniculus (P00489)
Meremyanin, A.V.; Eronina, T.B.; Chebotareva, N.A.; Kleimenov, S.Y.; Yudin, I.K.; Muranov, K.O.; Ostrovsky, M.A.; Kurganov, B.I.
Effect of alpha-crystallin on thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle
Biochemistry (Moscow)
72
518-528
2007
Oryctolagus cuniculus
Chen, L.; Li, H.; Liu, J.; Zhang, L.; Liu, H.; Jiang, H.
Discovering benzamide derivatives as glycogen phosphorylase inhibitors and their binding site at the enzyme
Bioorg. Med. Chem.
15
6763-6774
2007
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Loughlin, W.A.; Pierens, G.K.; Petersson, M.J.; Henderson, L.C.; Healy, P.C.
Evaluation of novel hyphodermin derivatives as glycogen phosphorylase a inhibitors
Bioorg. Med. Chem.
16
6172-6178
2008
Oryctolagus cuniculus
Bertus, P.; Szymoniak, J.; Jeanneau, E.; Docsa, T.; Gergely, P.; Praly, J.P.; Vidal, S.
Synthesis of a C-glucosylated cyclopropylamide and evaluation as a glycogen phosphorylase inhibitor
Bioorg. Med. Chem. Lett.
18
4774-4778
2008
Oryctolagus cuniculus
Meremyanin, A.V.; Eronina, T.B.; Chebotareva, N.A.; Kurganov, B.I.
Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: mechanism of protective action of alpha-crystallin
Biopolymers
89
124-134
2008
Oryctolagus cuniculus
Chen, J.; Gong, Y.; Liu, J.; Hua, W.; Zhang, L.; Sun, H.
Synthesis and biological evaluation of novel pyrazolo[4,3-b]oleanane derivatives as inhibitors of glycogen phosphorylase
Chem. Biodivers.
5
1304-1312
2008
Oryctolagus cuniculus
Pautsch, A.; Stadler, N.; Wissdorf, O.; Langkopf, E.; Moreth, W.; Streicher, R.
Molecular recognition of the protein phosphatase 1 glycogen targeting subunit by glycogen phosphorylase
J. Biol. Chem.
283
8913-8918
2008
Oryctolagus cuniculus, Homo sapiens (P06737)
Wen, X.; Sun, H.; Liu, J.; Cheng, K.; Zhang, P.; Zhang, L.; Hao, J.; Zhang, L.; Ni, P.; Zographos, S.E.; Leonidas, D.D.; Alexacou, K.M.; Gimisis, T.; Hayes, J.M.; Oikonomakos, N.G.
Naturally occurring pentacyclic triterpenes as inhibitors of glycogen phosphorylase: synthesis, structure-activity relationships, and X-ray crystallographic studies
J. Med. Chem.
51
3540-3554
2008
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Dairou, J.; Pluvinage, B.; Noiran, J.; Petit, E.; Vinh, J.; Haddad, I.; Mary, J.; Dupret, J.M.; Rodrigues-Lima, F.
Nitration of a critical tyrosine residue in the allosteric inhibitor site of muscle glycogen phosphorylase impairs its catalytic activity
J. Mol. Biol.
372
1009-1021
2007
Mus musculus, Oryctolagus cuniculus (P00489)
Tiraidis, C.; Alexacou, K.M.; Zographos, S.E.; Leonidas, D.D.; Gimisis, T.; Oikonomakos, N.G.
FR258900, a potential anti-hyperglycemic drug, binds at the allosteric site of glycogen phosphorylase
Protein Sci.
16
1773-1782
2007
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Gregus, Z.; Nemeti, B.
Glutathione-dependent reduction of arsenate by glycogen phosphorylase responsiveness to endogenous and xenobiotic inhibitors
Toxicol. Sci.
100
44-53
2007
Oryctolagus cuniculus
Sharov, V.S.; Galeva, N.A.; Dremina, E.S.; Williams, T.D.; Schoeneich, C.
Inactivation of rabbit muscle glycogen phosphorylase b by peroxynitrite revisited: does the nitration of Tyr613 in the allosteric inhibition site control enzymatic function?
Arch. Biochem. Biophys.
484
155-166
2009
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Anderka, O.; Loenze, P.; Klabunde, T.; Dreyer, M.K.; Defossa, E.; Wendt, K.U.; Schmoll, D.
Thermodynamic characterization of allosteric glycogen phosphorylase inhibitors
Biochemistry
47
4683-4691
2008
Oryctolagus cuniculus, Homo sapiens (P06737)
Chebotareva, N.A.; Meremyanin, A.V.; Makeeva, V.F.; Eronina, T.B.; Kurganov, B.I.
Glycogen phosphorylase b and phosphorylase kinase binding to glycogen under molecular crowding conditions. Inhibitory effect of FAD
Biochemistry
74
562-568
2009
Oryctolagus cuniculus
Zhu, P.; Bi, Y.; Xu, J.; Li, Z.; Liu, J.; Zhang, L.; Ye, W.; Wu, X.
Terpenoids. III: Synthesis and biological evaluation of 23-hydroxybetulinic acid derivatives as novel inhibitors of glycogen phosphorylase
Bioorg. Med. Chem. Lett.
19
6966-6969
2009
Oryctolagus cuniculus
Karis, N.D.; Loughlin, W.A.; Jenkins, I.D.; Healy, P.C.
Glycogen phosphorylase inhibitory effects of 2-oxo-1,2-dihydropyridin-3-yl amide derivatives
Bioorg. Med. Chem.
17
4724-4733
2009
Oryctolagus cuniculus
Toth, M.; Kun, S.; Bokor, E.; Benltifa, M.; Tallec, G.; Vidal, S.; Docsa, T.; Gergely, P.; Somsak, L.; Praly, J.P.
Synthesis and structure-activity relationships of C-glycosylated oxadiazoles as inhibitors of glycogen phosphorylase
Bioorg. Med. Chem.
17
4773-4785
2009
Oryctolagus cuniculus
Nagy, V.; Benltifa, M.; Vidal, S.; Berzsenyi, E.; Teilhet, C.; Czifrak, K.; Batta, G.; Docsa, T.; Gergely, P.; Somsak, L.; Praly, J.P.
Glucose-based spiro-heterocycles as potent inhibitors of glycogen phosphorylase
Bioorg. Med. Chem.
17
5696-5707
2009
Oryctolagus cuniculus
Zhang, L.; Li, H.; Zhu, Q.; Liu, J.; Chen, L.; Leng, Y.; Jiang, H.; Liu, H.
Benzamide derivatives as dual-action hypoglycemic agents that inhibit glycogen phosphorylase and activate glucokinase
Bioorg. Med. Chem.
17
7301-7312
2009
Oryctolagus cuniculus (P00489)
Benltifa, M.; Hayes, J.M.; Vidal, S.; Gueyrard, D.; Goekjian, P.G.; Praly, J.P.; Kizilis, G.; Tiraidis, C.; Alexacou, K.M.; Chrysina, E.D.; Zographos, S.E.; Leonidas, D.D.; Archontis, G.; Oikonomakos, N.G.
Glucose-based spiro-isoxazolines: a new family of potent glycogen phosphorylase inhibitors
Bioorg. Med. Chem.
17
7368-7380
2009
Oryctolagus cuniculus (P00489)
Bokor, E.; Docsa, T.; Gergely, P.; Somsak, L.
Synthesis of 1-(D-glucopyranosyl)-1,2,3-triazoles and their evaluation as glycogen phosphorylase inhibitors
Bioorg. Med. Chem.
18
1171-1180
2010
Oryctolagus cuniculus
Eronina, T.B.; Chebotareva, N.A.; Bazhina, S.G.; Makeeva, V.F.; Kleymenov, S.Y.; Kurganov, B.I.
Effect of proline on thermal inactivation, denaturation and aggregation of glycogen phosphorylase b from rabbit skeletal muscle
Biophys. Chem.
141
66-74
2009
Oryctolagus cuniculus
Cheng, K.; Liu, J.; Liu, X.; Li, H.; Sun, H.; Xie, J.
Synthesis of glucoconjugates of oleanolic acid as inhibitors of glycogen phosphorylase
Carbohydr. Res.
344
841-850
2009
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Makino, Y.; Omichi, K.
Sensitive assay of glycogen phosphorylase activity by analysing the chain-lengthening action on a fluorogenic [corrected] maltooligosaccharide derivative
J. Biochem.
146
71-76
2009
Oryctolagus cuniculus
Cheng, K.; Zhang, P.; Liu, J.; Xie, J.; Sun, H.
Practical synthesis of bredemolic acid, a natural inhibitor of glycogen phosphorylase
J. Nat. Prod.
71
1877-1880
2008
Oryctolagus cuniculus
Cecioni, S.; Argintaru, O.; Docsa, T.; Gergely, P.; Praly, J.; Vidal, S.
Probing multivalency for the inhibition of an enzyme: Glycogen phosphorylase as a case study
New J. Chem.
33
148-156
2009
Oryctolagus cuniculus
-
Bigley, A.N.; Reinhart, G.D.
The N-terminus of glycogen phosphorylase b is not required for activation by adenosine 5-monophosphate
Biochemistry
49
4760-4765
2010
Oryctolagus cuniculus
Tsirkone, V.G.; Tsoukala, E.; Lamprakis, C.; Manta, S.; Hayes, J.M.; Skamnaki, V.T.; Drakou, C.; Zographos, S.E.; Komiotis, D.; Leonidas, D.D.
1-(3-Deoxy-3-fluoro-beta-D-glucopyranosyl) pyrimidine derivatives as inhibitors of glycogen phosphorylase b: kinetic, crystallographic and modelling studies
Bioorg. Med. Chem.
18
3413-3425
2010
Oryctolagus cuniculus
Alexacou, K.M.; Tenchiu Deleanu, A.C.; Chrysina, E.D.; Charavgi, M.D.; Kostas, I.D.; Zographos, S.E.; Oikonomakos, N.G.; Leonidas, D.D.
The binding of beta-D-glucopyranosyl-thiosemicarbazone derivatives to glycogen phosphorylase: a new class of inhibitors
Bioorg. Med. Chem.
18
7911-7922
2010
Oryctolagus cuniculus
Nagy, V.; Felfoeldi, N.; Konya, B.; Praly, J.P.; Docsa, T.; Gergely, P.; Chrysina, E.D.; Tiraidis, C.; Kosmopoulou, M.N.; Alexacou, K.M.; Konstantakaki, M.; Leonidas, D.D.; Zographos, S.E.; Oikonomakos, N.G.; Kozmon, S.; Tvaroska, I.; Somsak, L.
N-(4-Substituted-benzoyl)-N'-(beta-D-glucopyranosyl)ureas as inhibitors of glycogen phosphorylase: synthesis and evaluation by kinetic, crystallographic, and molecular modelling methods
Bioorg. Med. Chem.
20
1801-1816
2012
Oryctolagus cuniculus
Cheng, K.; Liu, J.; Sun, H.; Xie, J.
Synthesis of oleanolic acid dimers as inhibitors of glycogen phosphorylase
Chem. Biodivers.
7
690-697
2010
Oryctolagus cuniculus
Liang, Z.; Zhang, L.; Li, L.; Liu, J.; Li, H.; Zhang, L.; Chen, L.; Cheng, K.; Zheng, M.; Wen, X.; Zhang, P.; Hao, J.; Gong, Y.; Zhang, X.; Zhu, X.; Chen, J.; Liu, H.; Jiang, H.; Luo, C.; Sun, H.
Identification of pentacyclic triterpenes derivatives as potent inhibitors against glycogen phosphorylase based on 3D-QSAR studies
Eur. J. Med. Chem.
46
2011-2021
2011
Oryctolagus cuniculus
Kantsadi, A.L.; Manta, S.; Psarra, A.M.; Dimopoulou, A.; Kiritsis, C.; Parmenopoulou, V.; Skamnaki, V.T.; Zoumpoulakis, P.; Zographos, S.E.; Leonidas, D.D.; Komiotis, D.
The binding of C5-alkynyl and alkylfurano[2,3-d]pyrimidine glucopyranonucleosides to glycogen phosphorylase b: synthesis, biochemical and biological assessment
Eur. J. Med. Chem.
54
740-749
2012
Oryctolagus cuniculus
Tite, T.; Tomas, L.; Docsa, T.; Gergely, P.; Kovensky, J.; Gueyrard, D.; Wadouachi, A.
Synthesis of N-aryl spiro-sulfamides as potential glycogen phosphorylase inhibitors
Tetrahedron Lett.
53
959-961
2012
Oryctolagus cuniculus
-
Polyak, M.; Varga, G.; Szilagyi, B.; Juhasz, L.; Docsa, T.; Gergely, P.; Begum, J.; Hayes, J.M.; Somsak, L.
Synthesis, enzyme kinetics and computational evaluation of N-(beta-D-glucopyranosyl) oxadiazolecarboxamides as glycogen phosphorylase inhibitors
Bioorg. Med. Chem.
21
5738-5747
2013
Oryctolagus cuniculus (P00489)
Parmenopoulou, V.; Kantsadi, A.L.; Tsirkone, V.G.; Chatzileontiadou, D.S.; Manta, S.; Zographos, S.E.; Molfeta, C.; Archontis, G.; Agius, L.; Hayes, J.M.; Leonidas, D.D.; Komiotis, D.
Structure based inhibitor design targeting glycogen phosphorylase B. Virtual screening, synthesis, biochemical and biological assessment of novel N-acyl-beta-D-glucopyranosylamines
Bioorg. Med. Chem.
22
4810-4825
2014
Oryctolagus cuniculus (P00489), Rattus norvegicus (P09811), Rattus norvegicus Wistar (P09811)
Bokor, E.; Szennyes, E.; Csupasz, T.; Toth, N.; Docsa, T.; Gergely, P.; Somsak, L.
C-(2-Deoxy-d-arabino-hex-1-enopyranosyl)-oxadiazoles: synthesis of possible isomers and their evaluation as glycogen phosphorylase inhibitors
Carbohydr. Res.
412
71-79
2015
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Bokor, E.; Szeles, Z.; Docsa, T.; Gergely, P.; Somsak, L.
C-Glucopyranosyl-1,2,4-triazol-5-ones: synthesis and inhibition of glycogen phosphorylase
Carbohydr. Res.
429
128-134
2016
Oryctolagus cuniculus (P00489), Oryctolagus cuniculus
Xu, X.; Mathieu, C.; Boitard, S.E.; Dairou, J.; Dupret, J.M.; Agbulut, O.; Rodrigues-Lima, F.
Skeletal muscle glycogen phosphorylase is irreversibly inhibited by mercury: molecular, cellular and kinetic aspects
FEBS Lett.
588
138-142
2014
Oryctolagus cuniculus (P00489), Mus musculus (Q9WUB3), Mus musculus Swiss (Q9WUB3)
Kyriakis, E.; Stravodimos, G.A.; Kantsadi, A.L.; Chatzileontiadou, D.S.; Skamnaki, V.T.; Leonidas, D.D.
Natural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase b
FEBS Lett.
589
1787-1794
2015
Oryctolagus cuniculus (P00489)
Makino, Y.; Fujii, Y.; Taniguchi, M.
Properties and functions of the storage sites of glycogen phosphorylase
J. Biochem.
157
451-458
2015
Oryctolagus cuniculus (P00489)
Begum, J.; Varga, G.; Docsa, T.; Gergely, P.; Hayes, J.; Juhasz, L.; Somsak, L.
Computationally motivated synthesis and enzyme kinetic evaluation of N-(beta-D-glucopyranosyl)-1,2,4-triazolecarboxamides as glycogen phosphorylase inhibitors
MedChemComm
6
80-89
2015
Oryctolagus cuniculus (P00489)
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