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Information on EC 2.4.1.1 - glycogen phosphorylase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.1 glycogen phosphorylase
IUBMB 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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This record set is specific for:
Homo sapiens
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
glycogen phosphorylase, phosphorylase a, phosphorylase b, myophosphorylase, muscle phosphorylase, glycogen phosphorylase b, glycogen phosphorylase a, muscle glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-glucan phosphorylase
-
-
-
-
alpha-glucan phosphorylase
-
-
-
-
amylopectin phosphorylase
-
-
-
-
amylophosphorylase
-
-
-
-
glucan phosphorylase
-
-
-
-
glucosan phosphorylase
-
-
-
-
glycogen phosphorylase
glycogen phosphorylase a
-
-
GPBB
-
-
granulose phosphorylase
-
-
-
-
maltodextrin phosphorylase
-
-
-
-
muscle phosphorylase
-
-
-
-
muscle phosphorylase a and b
-
-
-
-
myophosphorylase
phosphorylase a
-
-
-
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phosphorylase, alpha-glucan
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-
-
-
polyphosphorylase
-
-
-
-
potato phosphorylase
-
-
-
-
starch phosphorylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
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 hide
9035-74-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycogen + phosphate
glycogen + alpha-D-glucose 1-phosphate
show the reaction diagram
-
-
-
r
[(1->4)-alpha-D-glucosyl]n + phosphate
[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
-
the liver enzyme catalyzes the forward reaction
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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'-butane-1,4-diylbis[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
(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
-
-
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-[(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-[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-[[(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
2,3-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-(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-3,4-dihydroxy-5-methoxybenzoic acid
-
-
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
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-methoxypterolactone
-
-
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
-
-
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
i.e. AVE5688, binding to enzyme is exclusively enthalpic
4-hydroxy-3-methoxybenzoic acid
-
-
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-hydroxy-2,3-dihydro-1H-inden-5-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-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
crystallization data
5-chloro-N-[4-(2-hydroxyethyl)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
-
alpha-boswellic acid
-
-
beta-amyrin
-
-
beta-amyrone
-
-
beta-boswellic acid
-
-
beta-O-trans-caffeoyl-morolic acid
-
-
Caffeine
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-320626
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
D-Fructose 1-phosphate
-
-
D-glucose
D-glucose 6-phosphate
-
-
DTNB
-
-
gallic acid
-
-
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
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-[(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
-
50% inhibition at 0.135 microM
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
-
-
pterolactone
-
-
riboflavin
inhibition of the liver enzyme, counteracted by AMP
UDP-glucose
-
-
uric acid
inhibition of the liver enzyme, counteracted by AMP
[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]acetic acid
-
-
[[(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
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
stimulation via P2Y receptor signaling, primarily through P2Y2 receptors
dithiothreitol
-
required to maintain activity
Insulin
Insulin promotes conversion of GPa to GPb via protein kinase B activation
-
UTP
-
stimulation via P2Y receptor signaling, primarily through P2Y2 receptors
additional information
the muscle isoform of phosphorylase is activated by phosphorylation (GPb to GPa conversion)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000018 - 0.0015
(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
0.00004 - 0.0012
(2-[[(2-chloro-6H-thieno[2,3-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
0.000057
(2-[[(5-chloro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00026
(2-[[(5-chloro-1H-pyrrolo[2,3-c]pyridin-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000076
(2-[[(5-chloro-6-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000052
(2-[[(5-chloro-7-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00016
(2-[[(5-fluoro-1H-indol-2-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000026 - 0.00043
(2E,2'E)-N,N'-(oxydiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
0.000012 - 0.00045
(2E,2'E)-N,N'-(thiodiethane-2,1-diyl)bis[3-(3,4-dichlorophenyl)acrylamide]
0.000043 - 0.00042
(2E,2'E)-N,N'-butane-1,4-diylbis[3-(3,4-dichlorophenyl)-acrylamide]
0.000023 - 0.00026
(2E,2'E)-N,N'-pentane-1,5-diylbis[3-(3,4-dichlorophenyl)acrylamide]
0.00001
(2R)-2-cyclohexyl-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]propanoic acid
Homo sapiens
-
-
0.000009
(2S)-2-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]heptanoic acid
Homo sapiens
-
0.000006
(2S)-cyclohexyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
Homo sapiens
-
-
0.000014
(2S)-cyclopentyl[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]ethanoic acid
Homo sapiens
-
-
0.000014
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclodecanecarboxylic acid
Homo sapiens
-
-
0.000005
1-[[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]amino]cyclooctanecarboxylic acid
Homo sapiens
-
-
0.000017 - 0.00017
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
0.0077
2-amino-3,4-dihydroxy-5-methoxybenzoic acid
Homo sapiens
-
-
0.000056
3-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)propanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.26
3-methoxypterolactone
Homo sapiens
-
-
0.000056
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
Homo sapiens
-
pH and temperature not specified in the publication
0.000059
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
Homo sapiens
-
pH and temperature not specified in the publication
0.000054
4-(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)butanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.091
4-hydroxy-3-methoxybenzoic acid
Homo sapiens
-
-
0.000042
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
Homo sapiens
-
pH and temperature not specified in the publication
0.00002
5-chloro-N-(1,3,6,6-tetrafluoro-(R)-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.000048
5-chloro-N-(1,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.00044
5-chloro-N-(1-hydroxy-2,3-dihydro-1H-inden-5-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.000063
5-chloro-N-(3,6,6-trifluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.00032
5-chloro-N-(5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.000068
5-chloro-N-(6,6-difluoro-5-hydroxy-5,6,7,8-tetrahydronaphthalen-2-yl)-1H-indole-2-carboxamide
Homo sapiens
-
-
0.00042
5-chloro-N-[2-chloro-4-(1,2-dihydroxyethyl)-phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.00034
5-chloro-N-[4-(1,2-dihydroxyethyl)-3-(trifluoromethyl)phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.0009
5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.0012
5-chloro-N-[4-(2-hydroxyethyl)phenyl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.00044
5-chloro-N-[5-(1,2-dihydroxyethyl)pyrazin-2-yl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.00025
5-chloro-N-[5-(1,2-dihydroxyethyl)pyridin-2-yl]-1H-indole-2-carboxamide
Homo sapiens
pH 6.8, 22C
0.037
alpha-boswellic acid
Homo sapiens
-
-
0.047
beta-amyrin
Homo sapiens
-
-
0.06
beta-amyrone
Homo sapiens
-
-
0.026
beta-boswellic acid
Homo sapiens
-
-
0.044
beta-O-trans-caffeoyl-morolic acid
Homo sapiens
-
-
0.0066
Caffeine
Homo sapiens
-
-
0.00092
CP-320626
Homo sapiens
pH 6.8, 22C
0.0068
gallic acid
Homo sapiens
-
-
0.000023
N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-norleucine
Homo sapiens
-
0.000006
O-(1-methylcyclopentyl)-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
Homo sapiens
-
0.000007
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-allothreonine
Homo sapiens
-
0.000044
O-tert-butyl-N-[(3-[[(2,4,6-trimethylphenyl)carbamoyl]amino]naphthalen-2-yl)carbonyl]-L-serine
Homo sapiens
-
0.008
oleanolic acid
Homo sapiens
-
-
0.232
pterolactone
Homo sapiens
-
-
0.00003
[(2-[[(2,3-dichloro-4H-thieno[3,2-b]pyrrol-5-yl)carbonyl]amino]-2,3-dihydro-1H-inden-1-yl)oxy]acetic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00004
[[(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
Homo sapiens
-
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoforms phosphorylase a and b
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
glycogen degradation and synthesis during the diurnal cycle are mediated by changes in the activities of phosphorylase and glycogen synthase. Phosphorylase is regulated by phosphorylation of Ser14. Only the phosphorylated form of liver phosphorylase (GPa) is catalytically active. Interconversion between GPa and GPb (unphosphorylated) is dependent on the activities of phosphorylase kinase and of phosphorylase phosphatase. The latter comprises protein phosphatase-1 in conjunction with a glycogen-targeting protein (G-subunit) of the PPP1R3 family. Both GPa and phosphorylated glycogen synthase serve as substrates for the catalytic subunit of protein phosphatase-1 in association with G-subunits
physiological function
additional information
despite a high degree of conservation of residues between liver and muscle isoforms in the ligand binding residues at the catalytic and allosteric sites, the kinetic properties of liver phosphorylase differ from the muscle isoform
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PYGB_HUMAN
843
0
96696
Swiss-Prot
other Location (Reliability: 4)
PYGL_HUMAN
847
0
97149
Swiss-Prot
other Location (Reliability: 3)
PYGM_HUMAN
842
0
97092
Swiss-Prot
other Location (Reliability: 4)
Q6P1L4_HUMAN
248
0
28634
TrEMBL
Mitochondrion (Reliability: 4)
B2R825_HUMAN
847
0
97068
TrEMBL
other Location (Reliability: 3)
B4DRW6_HUMAN
832
0
95904
TrEMBL
other Location (Reliability: 4)
Q59GM9_HUMAN
865
0
98829
TrEMBL
Secretory Pathway (Reliability: 1)
B4DSD8_HUMAN
752
0
85787
TrEMBL
other Location (Reliability: 2)
B4DRQ4_HUMAN
595
0
67689
TrEMBL
other Location (Reliability: 2)
H0Y4Z6_HUMAN
245
0
27557
TrEMBL
other Location (Reliability: 5)
A0A0M4FEM1_HUMAN
842
0
97122
TrEMBL
other Location (Reliability: 4)
E9PK47_HUMAN
819
0
94070
TrEMBL
other Location (Reliability: 3)
Q8TDG6_HUMAN
202
0
22841
TrEMBL
other Location (Reliability: 2)
B2RB32_HUMAN
842
0
97044
TrEMBL
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
175000
-
phosphorylase b, sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
the more active phosphorylated form, glycogen phosphorylase a, of the enzyme is a homodimer having an inhibitory allosteric binding site at the dimer interface for which synthetic ligands
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the muscle isoform of phosphorylase is activated by phosphorylation (GPb to GPa conversion)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization and structure determination of liver and muscle enzymes
dialysis against 50 mM Tris and 40 mM 2-mercaptoethanol, pH 6.8 at 0°C
-
hanging drop method, crystal structure of liver phosphorylase bound to a glycogen targeting subunit-derived peptide. C-terminus of glycogen targeting subunit of protein phosphatase 1 binds in a hydrophobically collapsed conformation to the allosteric regulator-binding site at the phosphorylase dimer interface
in complex with inhibitor (2E,2'E)-N,N'-pentane-1,5-diylbis[3-(3,4-dichlorophenyl)acrylamide]. Inhibitor is bound at the dimer interface site, the 3,4-dichlorophenyl moiety interacts hydroühobically with the enzyme
in complex with inhibitors 4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid, 1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid, and 1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid. Binding to inhibitor 4-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-3-(trifluoromethoxy)benzoic acid is exclusively enthalpic. The inhibitors 1-[2-([[(2-chloro-4,5-difluorophenyl)carbonyl]carbamoyl]amino)-4-fluorophenyl]piperidine-4-carboxylic acid, and 1-(2-carboxyphenyl)-6-[(2-chloro-4,6-difluorophenyl)amino]-4-oxo-1,2,3,4-tetrahydroquinoline-3-carboxylic acid fully exploit the volume of the binding pocket and show pronounced binding entropy
in complexwith inhibitor 5-chloro-N-[4-(1,2-dihydroxyethyl)phenyl]-1H-indole-2-carboxamide, inhibitor binds to a solvent cavity at the dimer interface, with the two hydroxyl groups making favorable electrostatic interactions with the enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
crystalline, several h stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
storage in frozen or lyophilized state, crystalline human, not rabbit, phosphorylase a or b, stable to
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
the enzyme is a target for inhibitor design in development of drugs for treatment of type 2 diabetes
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Ercan-Fang, N.; Taylor, M.R.; Treadway, J.L.; Levy, C.B.; Genereux, P.E.; Gibbs, E.M.; Rath, V.L.; Kwon, Y.; Gannon, M.C.; Nuttall, F.Q.
Endogenous effectors of human liver glycogen phosphorylase modulate effects of indole-site inhibitors
Am. J. Physiol. Endocrinol. Metab.
289
E366-E372
2005
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Peetz, D.; Post, F.; Schinzel, H.; Schweigert, R.; Schollmayer, C.; Steinbach, K.; Dati, F.; Noll, F.; Lackner, K.J.
Glycogen phosphorylase BB in acute coronary syndromes
Clin. Chem. Lab. Med.
43
1351-1358
2005
Homo sapiens
Manually annotated by BRENDA team
Dixon, C.J.; White, P.J.; Hall, J.F.; Kingston, S.; Boarder, M.R.
Regulation of human hepatocytes by P2Y receptors: control of glycogen phosphorylase, Ca2+, and mitogen-activated protein kinases
J. Pharmacol. Exp. Ther.
313
1305-1313
2005
Homo sapiens
Manually annotated by BRENDA team
Evans, K.A.; Li, Y.H.; Coppo, F.T.; Graybill, T.L.; Cichy-Knight, M.; Patel, M.; Gale, J.; Li, H.; Thrall, S.H.; Tew, D.; Tavares, F.; Thomson, S.A.; Weiel, J.E.; Boucheron, J.A.; Clancy, D.C.; Epperly, A.H.; Golden, P.L.
Amino acid anthranilamide derivatives as a new class of glycogen phosphorylase inhibitors
Bioorg. Med. Chem. Lett.
18
4068-4071
2008
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Cristina Pacheco, M.; Miles, L.; Bove, K.E.
False negative histochemical reaction for myophosphorylase activity in fulminant sepsis due to methicillin resistant Staphylococcus aureus
Neuromuscul. Disord.
17
983-985
2007
Homo sapiens
Manually annotated by BRENDA team
Li, J.; Lu, Y.; Su, X.; Li, F.; She, Z.; He, X.; Lin, Y.
A norsesquiterpene lactone and a benzoic acid derivative from the leaves of Cyclocarya paliurus and their glucosidase and glycogen phosphorylase inhibiting activities
Planta Med.
74
287-289
2008
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Sparks, S.M.; Banker, P.; Bickett, D.M.; Carter, H.L.; Clancy, D.C.; Dickerson, S.H.; Dwornik, K.A.; Garrido, D.M.; Golden, P.L.; Nolte, R.T.; Peat, A.J.; Sheckler, L.R.; Tavares, F.X.; Thomson, S.A.; Wang, L.; Weiel, J.E.
Anthranilimide-based glycogen phosphorylase inhibitors for the treatment of type 2 diabetes: 1. Identification of 1-amino-1-cycloalkyl carboxylic acid headgroups
Bioorg. Med. Chem. Lett.
19
976-980
2009
Homo sapiens (P06737)
Manually annotated by BRENDA team
Sparks, S.M.; Banker, P.; Bickett, D.M.; Clancy, D.C.; Dickerson, S.H.; Garrido, D.M.; Golden, P.L.; Peat, A.J.; Sheckler, L.R.; Tavares, F.X.; Thomson, S.A.; Weiel, J.E.
Anthranilimide-based glycogen phosphorylase inhibitors for the treatment of Type 2 diabetes: 2. Optimization of serine and threonine ether amino acid residues
Bioorg. Med. Chem. Lett.
19
981-985
2009
Homo sapiens
Manually annotated by BRENDA team
Onda, K.; Shiraki, R.; Ogiyama, T.; Yokoyama, K.; Momose, K.; Katayama, N.; Orita, M.; Yamaguchi, T.; Furutani, M.; Hamada, N.; Takeuchi, M.; Okada, M.; Ohta, M.; Tsukamoto, S.
Design, synthesis, and pharmacological evaluation of N-bicyclo-5-chloro-1H-indole-2-carboxamide derivatives as potent glycogen phosphorylase inhibitors
Bioorg. Med. Chem.
16
10001-10012
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Onda, K.; Suzuki, T.; Shiraki, R.; Yonetoku, Y.; Negoro, K.; Momose, K.; Katayama, N.; Orita, M.; Yamaguchi, T.; Ohta, M.; Tsukamoto, S.
Synthesis of 5-chloro-N-aryl-1H-indole-2-carboxamide derivatives as inhibitors of human liver glycogen phosphorylase a
Bioorg. Med. Chem.
16
5452-5464
2008
Mus musculus, Homo sapiens (P06737), Homo sapiens
Manually annotated by BRENDA team
Onda, K.; Shiraki, R.; Yonetoku, Y.; Momose, K.; Katayama, N.; Orita, M.; Yamaguchi, T.; Ohta, M.; Tsukamoto, S.
Synthesis and pharmacological evaluation of bis-3-(3,4-dichlorophenyl)acrylamide derivatives as glycogen phosphorylase inhibitors
Bioorg. Med. Chem.
16
8627-8634
2008
Homo sapiens (P06737), Homo sapiens
Manually annotated by BRENDA team
Bennett, S.N.; Campbell, A.D.; Hancock, A.; Johnstone, C.; Kenny, P.W.; Pickup, A.; Plowright, A.T.; Selmi, N.; Simpson, I.; Stocker, A.; Whalley, D.P.; Whittamore, P.R.
Discovery of a series of indan carboxylic acid glycogen phosphorylase inhibitors
Bioorg. Med. Chem. Lett.
20
3511-3514
2010
Homo sapiens
Manually annotated by BRENDA team
Agius, L.
Role of glycogen phosphorylase in liver glycogen metabolism
Mol. Aspects Med.
46
34-45
2015
Homo sapiens (P06737)
Manually annotated by BRENDA team