Information on EC 2.7.11.19 - phosphorylase kinase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
2.7.11.19
-
RECOMMENDED NAME
GeneOntology No.
phosphorylase kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:phosphorylase-b phosphotransferase
Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis---glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b [5]. The gamma subunit of the tetrameric enzyme is the catalytic subunit.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-88-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
blowfly
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
silk moth
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
hypothetical protein
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
commercial baker's yeast
-
-
Manually annotated by BRENDA team
scorpion fish
-
-
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
fragment of the beta subunit
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + alphagammadelta subunit complex
ADP + activated alphagammadelta subunit complex
show the reaction diagram
-
autophosphorylation, by incorporation of phosphate into alpha subunit
-
-
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
show the reaction diagram
ATP + Ca2+-dependent transport ATPase
?
show the reaction diagram
-
rabbit
-
-
-
ATP + casein
?
show the reaction diagram
ATP + glycogen phosphorylase
?
show the reaction diagram
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
show the reaction diagram
ATP + glycogen S peptide
ADP + phosphorylated glycogen S peptide
show the reaction diagram
-
synthetic peptide corresponding to residues 5-18 of its convertible region
-
-
?
ATP + glycogen synthase
?
show the reaction diagram
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
ATP + histone H1
?
show the reaction diagram
-
-
-
-
-
ATP + liver dephosphophosphorylase
?
show the reaction diagram
ATP + Lys-Arg-Glu-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Glu-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp
show the reaction diagram
-
-
-
-
-
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp-Gly-Ile
show the reaction diagram
-
-
-
-
-
ATP + Lys-Arg-Lys-Glu-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Glu-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Glu-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Glu-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Pro-Val-Thr-Arg-Glu-Ile-Ser-Ile-Arg-NH2
?
show the reaction diagram
-
i.e. S-peptide
-
-
-
ATP + melittin
ADP + phosphomelittin
show the reaction diagram
-
-
-
-
ATP + modified phosphorylase b
?
show the reaction diagram
-
modification at AMP-site
-
-
-
ATP + myelin basic protein
?
show the reaction diagram
-
-
-
-
-
ATP + myosin light chain kinase
?
show the reaction diagram
-
rabbit
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
ATP + peptides derived from glycogen synthase
?
show the reaction diagram
-
rabbit, overview
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
ATP + phosphorylase b
ADP + phosphorylated phosphorylase b
show the reaction diagram
ATP + protein
ATP + phosphoprotein
show the reaction diagram
in the presence of Ca2+/calmodulin, the isoform PhK-gamma T of the catalytic subunit is able to efficiently phosphorylate glycogen phosphorylase and convert it from an inactive to an active form
-
-
?
ATP + sarcolemmal Na+,K+ ATPase
?
show the reaction diagram
-
rabbit
-
-
-
ATP + sarcolemmal protein
?
show the reaction diagram
-
-
-
-
-
ATP + sarcoplasmic protein
?
show the reaction diagram
-
-
-
-
-
ATP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
ADP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp
show the reaction diagram
-
-
-
-
-
ATP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
ADP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp-Gly-Ile
show the reaction diagram
-
i.e. phosphorylase b peptide (5-18)
-
-
-
ATP + synthetic pentadecapeptide
?
show the reaction diagram
-
from amino-terminal of glycogen synthase, i.e. Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ser-Ser-Leu-Pro-Gly-Leu-Glu
-
-
-
ATP + synthetic peptides derived from glycogen synthase
?
show the reaction diagram
-
overview, phosphorylation at the same site as glycogen synthase
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
ATP + synthetic tetradecapeptide
?
show the reaction diagram
ATP + troponin I
ADP + phosphotroponin I
show the reaction diagram
ATP + troponin T
ADP + phosphotroponin T
show the reaction diagram
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
show the reaction diagram
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
GTP + phosphorylase b
GDP + phosphorylase a
show the reaction diagram
SDQEKRKQISVRGL + ATP
?
show the reaction diagram
-
artificial substrate
-
-
-
UTP + phosphorylase b
UDP + phosphorylase a
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
show the reaction diagram
ATP + glycogen phosphorylase
?
show the reaction diagram
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
show the reaction diagram
-
-
-
-
?
ATP + glycogen synthase
?
show the reaction diagram
ATP + phosphorylase b
?
show the reaction diagram
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
ATP + phosphorylase b
ADP + phosphorylated phosphorylase b
show the reaction diagram
-
-
-
-
?
ATP + protein
ATP + phosphoprotein
show the reaction diagram
P31325
in the presence of Ca2+/calmodulin, the isoform PhK-gamma T of the catalytic subunit is able to efficiently phosphorylate glycogen phosphorylase and convert it from an inactive to an active form
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxy-ADP
-
activation, can replace ADP
Calmodulin
additional information
-
capable of binding FAD, binding of FAD suppresses self association of enzyme
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2SO4
-
activation, 0.05-0.1 M, inhibits above 0.2 M
Calcium
-
dependent on
Cd2+
-
can partially substitue Mg2+
phosphate
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(D)-Arg-(D)-Leu-(D)-Ser-(D)-Leu
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
(D)-Leu-(D)-Ser-(D)-Leu-(D)-Arg
-
-
(D)-Leu-(D)-Ser-(D)-Tyr-(D)-Arg-(D)-Arg-(D)-Tyr-(D)-Ser-(D)-Leu
-
-
(NH4)2SO4
-
above 0.2 M, stimulates at 0.05-0.1 M
1,2-Dimethoxyethane
-
above 10% v/v, stimulates below
5'-adenylylimidodiphosphate
-
substrate-directed dead end inhibitor
actin
-
inhibits activation of subunit gamma-troponin C or subunit gamma-calmodulin complexes
Antibodies to delta subunit of phosphorylase kinase
-
-
-
Antibodies to rabbit phosphorylase kinase
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rabbit
-
Antibodies to rat testis calmodulin
-
calmodulin or troponin (the latter at high concentrations) reverses
-
Arg-Lys-Gln-Ile-Thr-Val-Arg
-
synthetic peptides as substrate
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Ca2+
-
inhibition in millimolar, activation in micromolar range
Calcineurin
-
i.e. calmodulin-binding protein, blocks activation by calmodulin
-
Calmodulin
-
inhibits cAMP-dependent protein kinase mediated activation of phosphorylase kinase, kinetics
FAD
-
FAD at high concentrations completely inhibits the second stage of enzyme binding to glycogen particles containing glycogen phosphorylase b, the inhibitory effect of FAD is not complete and reaches a maximal value at FAD concentrations around 0.03 mM
glucose
-
less effective than glucose 6-phosphate, pH 8.2
glucose 6-phosphate
glyceraldehyde-3-phosphate dehydrogenase
heparin
-
depending on pH it inhibits or activates nonactivated enzyme
Hexametaphosphate
-
pH 8.2
Histone VIIS
-
gammadelta subunit complex
-
Ile-Ser-Val-Arg-Gly
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
indirubin
-
phosphorylase kinase ATP-binding site inhibitor
indirubin-3'-oxime
-
phosphorylase kinase ATP-binding site inhibitor
K252a
-
microbial broth product, highly selective
KT5720
-
phosphorylase kinase ATP-binding site inhibitor
LLRDPYALRSVRHLIDNCAFRL
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 336-357
Lys-Pro-Val-Thr-Arg-Glu-Ile-Val-Ile-Arg-NH2
-
i.e. V-peptide
Melittin
-
model calmodulin-binding peptide, mechanism, kinetic, phosphorylase b as substrate
MgADP-
-
product inhibition
Monospecific antibodies against alpha, beta and gamma subunits
-
mechanism, kinetic, anti-beta subunit reverses inhibition by anti-alpha at pH 6.8
-
Phenothiazin
phosphorylase b
-
high concentration
Phosphotetradecapeptide
-
product inhibition
-
poly-L-lysine
-
strong, activated and nonactivated enzyme, stimulates autophosphorylation
Polyaspartic acid
proline
-
inhibits enzyme self-association and interaction with glycogen and phosphorylase b
protamine
Protein phosphatase
quercetin
-
ATP does not reverse
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Asp-Val-Arg-Gly-Leu
-
substrate-directed dead end inhibitor
staurosporine
Synthetic peptide PhK13
Synthetic peptide PhK5
Trifluoperazine
Trimethylamine N-oxide
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
UTP
-
weak, gammadelta subunit complex
VIRDPYALPPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 333-354
VIRDPYALRPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 332-353
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2-Dimethoxyethane
-
activation, 10% v/v, stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
adenosine 3',5'-monophosphate
adenosine 3'-phosphate 5'-phosphosulfate
-
activation, can replace ADP to some extent
adenosine 5'-phosphosulfate
-
activation, can replace ADP to some extent
Artificial thin filaments
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Ca2+-dependent protease
Ca2+/calmodulin
-
the phosphorylase kinase is activated by both cAMP-dependent protein kinase and Ca2+/calmodulin
-
Calmodulin
-
influences the conformational substates of the subunits, overview
cAMP
-
dependent on
casein protein kinase
caspase-3
-
selective in vitro cleavage of the regulatory alpha-subunit increasing the enzyme activity 2fold
-
Catalytic subunit of cAMP-dependent protein kinase
Catalytic subunit of cGMP-dependent protein kinase
Chymotrypsin
glycogen
heparin
papain
poly-L-arginine
-
strong, phosphorylase kinase as substrate, i.e. autophosphorylation
poly-L-lysine
-
strong, only with phosphorylase kinase as substrate, i.e. autophosphorylation, inhibits activity of activated and nonactivated enzyme with other substrates
Proteases
Protein kinases
Trimethylamine N-oxide
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Troponin
-
i.e. complex of troponin C, I and T, activation, as effective as troponin C, forms complex with beta subunit
-
troponin C
Trypsin
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 0.95
ATP
0.0093
glycogen phosphorylase b
-
at pH 8.2 in the presence of calcium
0.9 - 1
Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
pH 8.2
0.0098
Melittin
-
-
0.017 - 0.1
MgATP2-
0.2 - 3.5
peptides
0.002 - 0.37
phosphorylase b
0.21 - 0.28
S-peptide
2
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
-
activated enzyme, pH 8.2
1.2 - 3.5
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
0.3085 - 0.47
tetradecapeptide
additional information
additional information