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Information on EC 2.7.11.19 - phosphorylase kinase and Organism(s) Oryctolagus cuniculus and UniProt Accession P00518

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IUBMB Comments
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 . The gamma subunit of the tetrameric enzyme is the catalytic subunit.
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Select one or more organisms in this record:
This record set is specific for:
Oryctolagus cuniculus
UNIPROT: P00518
Word Map
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dephosphophosphorylase kinase, DphK-gamma, EC 2.7.1.38, glycogen phosphorylase b kinase, Glycogen phosphorylase kinase, GPK, kinase kinase/phosphatase/inhibitor-2, kinase, phosphorylase (phosphorylating), KPI-2 kinase, More, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dephosphophosphorylase kinase
-
-
-
-
EC 2.7.1.38
Glycogen phosphorylase kinase
-
-
-
-
kinase, phosphorylase (phosphorylating)
-
-
-
-
Phosphorylase b kinase
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
265930
-
phosphorylase kinase
255
-
PSK-C3
-
-
-
-
additional information
255
formerly EC 2.7.1.38
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
show the reaction diagram
mechanism
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
the enzyme catalyzes the phosphorylation of inactive glycogen phosphorylase b on Ser-14 resulting in the formation of active glycogen phosphorylase a
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
show the reaction diagram
2 ATP + phosphorylase b
2 ADP + 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+-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-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 + 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 + sarcolemmal Na+,K+ ATPase
?
show the reaction diagram
-
rabbit
-
-
-
ATP + sarcolemmal protein
?
show the reaction diagram
-
-
-
-
-
ATP + sarcoplasmic protein
?
show the reaction diagram
-
-
-
-
-
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
-
overview
-
-
-
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
-
phosphorylation is very slow, binds tightly to enzyme and acts as inhibitor for the phosphorylation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
SDQEKRKQISVRGL + ATP
?
show the reaction diagram
-
artificial substrate
-
-
-
additional information
?
-
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
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
show the reaction diagram
-
-
-
-
?
2 ATP + phosphorylase b
2 ADP + phosphorylase a
show the reaction diagram
P18688 AND P12798
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
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
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
Calcium
-
dependent on
(NH4)2SO4
-
activation, 0.05-0.1 M, inhibits above 0.2 M
phosphate
additional information
INHIBITOR
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
6'-bromoindirubin-3'-oxime
-
-
6,5-dichloroindirubin
-
-
6,5-dichloroindirubin-3'-acetoxime
-
-
6,5-dichloroindirubin-3'-oxime
-
-
6,6'-dibromoindirubin-3'-oxime
-
-
6-bromo-5-methylindirubin
-
-
6-bromo-5-methylindirubin-3'-acetoxime
-
-
6-bromo-5-nitroindirubin
-
-
6-bromo-5-nitroindirubin-3'-acetoxime
-
-
6-bromo-5-nitroindirubin-3'-oxime
-
-
6-bromo-N-methylindirubin
-
-
6-bromo-N-methylindirubin-3'-acetoxime
-
-
6-bromoindirubin
-
-
6-bromoindirubin-3'-acetoxime
-
-
6-bromoindirubin-3'-oxime
-
-
6-chloroindirubin
-
-
6-chloroindirubin-3'-oxime
-
-
6-fluoroindirubin
-
-
6-fluoroindirubin-3'-oxime
-
-
6-iodoindirubin-3'-oxime
-
-
6-methoxindirubin-3'-acetoxime
-
-
6-methoxindirubin-3'-oxime
-
-
6-vinylindirubin
-
-
6-vinylindirubin-3'-acetoxime
-
-
6-vinylindirubin-3'-oxime
-
-
7-bromo-N-methylindirubin
-
-
7-bromo-N-methylindirubin-3'-acetoxime
-
-
7-bromo-N-methylindirubin-3'-methoxime
-
-
7-bromo-N-methylindirubin-3'-oxime
-
-
7-bromoindirubin
-
-
7-bromoindirubin-3'-acetoxime
-
-
7-bromoindirubin-3'-methoxime
-
-
7-bromoindirubin-3'-oxime
-
-
7-carboxylindirubin
-
-
actin
-
inhibits activation of subunit gamma-troponin C or subunit gamma-calmodulin complexes
Antibodies to rabbit phosphorylase kinase
-
rabbit
-
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
-
-
-
GTP
-
gammadelta subunit complex
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
indirubin 3'-oxime
-
-
indirubin-3'-acetoxime
-
-
-
indirubin-3'-methoxime
-
-
indirubin-3'-oxime
-
phosphorylase kinase ATP-binding site inhibitor
ITP
-
not (gammadelta subunit complex)
K252a
-
microbial broth product, highly selective
KT5720
-
phosphorylase kinase ATP-binding site inhibitor
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
-
NH4Cl
Phenothiazin
-
blocks activation by extrinsic calmodulin
Phosphotetradecapeptide
-
product inhibition
-
poly-L-lysine
-
strong, activated and nonactivated enzyme, stimulates autophosphorylation
Polyaspartic acid
-
pH 8.2
proline
-
inhibits enzyme self-association and interaction with glycogen and phosphorylase b
protamine
-
pH 8.2
Protein phosphatase
-
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
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
-
activation, made by mixing actin, tropomyosin and troponin complex
-
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Ca2+-dependent protease
-
Calmodulin
cAMP
-
dependent on
casein protein kinase
-
activation of nonactivated enzyme
-
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
-
proteolytic activation of nonactivated enzyme
-
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
0.042
ATP
-
at pH 8.2 in the presence of calcium
0.0093
glycogen phosphorylase b
-
at pH 8.2 in the presence of calcium
0.018 - 0.95
ATP
0.0098
Melittin
-
-
0.017 - 0.098
MgATP2-
0.2 - 3.5
peptides
0.01 - 0.37
phosphorylase b
0.3085 - 0.47
tetradecapeptide
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
97
ATP
-
at pH 8.2 in the presence of calcium
134
glycogen phosphorylase b
-
at pH 8.2 in the presence of calcium
0.0983
Melittin
-
-
57.1 - 104
phosphorylase b
23.6
tetradecapeptide
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000037
KT5720
-
30C, pH 8.2
0.0000184
staurosporine
-
30C, pH 8.2
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00029
6'-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6,5-dichloroindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00082
6,5-dichloroindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.0002
6,5-dichloroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00233
6,6'-dibromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-bromo-5-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00036
6-bromo-5-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-bromo-5-nitroindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.0012
6-bromo-5-nitroindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.001
6-bromo-5-nitroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-bromo-N-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-bromo-N-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-bromoindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00033
6-bromoindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00034
6-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-chloroindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00023
6-chloroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-fluoroindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00022
6-fluoroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00033
6-iodoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00113
6-methoxindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.0007
6-methoxindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
6-vinylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00054
6-vinylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00055
6-vinylindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
7-bromo-N-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
7-bromo-N-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
7-bromo-N-methylindirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
7-bromo-N-methylindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
7-bromoindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.01
7-bromoindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
7-bromoindirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.0018
7-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.05
7-carboxylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.00045
glyceraldehyde-3-phosphate dehydrogenase
Oryctolagus cuniculus
-
-
-
0.05
indirubin
0.00021
indirubin 3'-oxime
Oryctolagus cuniculus
-
pH not spefified in the publication, 30C
0.00017
indirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
-
0.00034
indirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30C
0.000144
indirubin-3'-oxime
Oryctolagus cuniculus
-
30C, pH 8.2
0.0000184
KT5720
Oryctolagus cuniculus
-
30C, pH 8.2
0.00000037
staurosporine
Oryctolagus cuniculus
-
30C, pH 8.2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
nonphosphorylated enzyme PhK, pH 6.8, 30C
0.67
-
nonphosphorylated enzyme PhK, pH 6.8, 40C
1.3
-
phosphorylated enzyme PhK, pH 6.8, 30C
2.5
-
nonphosphorylated enzyme PhK, pH 8.2, 30C
3.09
-
phosphorylated enzyme PhK, pH 6.8, 40C
3.1
-
phosphorylated enzyme PhK, pH 8.2, 30C
6.7
-
nonphosphorylated enzyme PhK, pH 8.2, 40C
7.4
-
phosphorylated enzyme PhK, pH 8.2, 40C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7
-
assay at
7.6
-
above, nonactivated rabbit enzyme
8.3
-
assay at, substrate glycogen S peptide
9.5
-
muscle enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11.5
-
about half-maximal activity at pH 6 and 11.5, liver enzyme
6.2 - 9.5
-
about half-maximal activity at pH 6.2 and about 70% of maximal activity at pH 9.5
6.6 - 9.1
-
about half-maximal activity at pH 6.6 and 9.1, activity increases up to pH 8, sharp drop above 9
6.8 - 8.2
-
activity increases dramatically when the pH is raised from 6.8 to 8.2
6.8 - 8.5
-
about half-maximal activity at pH 6.8 and maximal activity at pH 8.5, activated rabbit enzyme
8.1 - 8.5
-
about half-maximal activity at pH 8.1 and maximal activity at pH 8.5, nonactivated rabbit enzyme
9 - 10
-
about half-maximal activity at pH 9 and 10, muscle enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
25 - 37
-
assay at
40
-
activation of phosphorylase kinase by physiological temperature
additional information
-
reaction and conformation temperature dependence, overview
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
-
the activity at pH 6.8 of nonphosphorylated PhK predictably increases, but between 30C and 40C, there is a dramatic jump in activity, resulting in the nonactivated enzyme having a far greater activity at body temperature than was previously realized. Both stimulation (by ADP and phosphorylation) and inhibition (by phosphate) were considerably less pronounced at 40C than at 30C. The probable underlying mechanism for the dramatic increase in PhK's activity between 30C and 40C is an abrupt change in the conformations of the regulatory beta and catalytic gamma subunits between these two temperatures. Activity profiles, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
the enzyme plays a key role in the cascade system for regulating glycogen metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PHKG1_RABIT
387
0
44803
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44673
-
x * 44673, calculation from amino acid sequence
130000
-
gel filtration
16680
-
4 * 118000-145000 + 4 * 108000-128000 + 4 * 44673 + 4 * 16680, (alphabetagammadelta)4, rabbit, SDS-PAGE, 2 isozymes that differ in size of the largest subunit (alpha: 118000-145000 and alpha: 133000-140000)
16696
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
16700
16784
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
16787
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
17000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
17700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 17700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits
44000
-
2 * 69000 + 2 * 44000, rabbit, proteolytic form, SDS-PAGE
44643
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
44667
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
44669
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
44673
-
4 * 118000-145000 + 4 * 108000-128000 + 4 * 44673 + 4 * 16680, (alphabetagammadelta)4, rabbit, SDS-PAGE, 2 isozymes that differ in size of the largest subunit (alpha: 118000-145000 and alpha: 133000-140000)
44700
45000
69000
-
2 * 69000 + 2 * 44000, rabbit, proteolytic form, SDS-PAGE
86000
-
catalytically active gammagamma subunit complex, gel filtration
125000
-
4 * alpha + 4 * 125000 (beta) + 4 * gamma + 4 * delta, beta-gamma-conjugate 1700000 Da, SDS-PAGE
125084
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
125200
125602
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
125660
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
130000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
138325
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
138400
138792
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
139358
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
145000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
205000
-
trypsinized or chymotrypsinized enzyme form, gel filtration
243000
-
alpha/gamma/delta complex, gel filtration
1220000
-
HPLC gel filtration
1260000
-
gel filtration
1299000
-
calculated from sequence, hexadecameric complex
1300000
1305000
-
mass spectrometry, hexadecameric complex
1330000
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 44673, calculation from amino acid sequence
heterotetramer
-
x-ray crystallography
dimer
-
2 * 45000, rabbit, catalytically active gammagamma subunit, SDS-PAGE
hexadecamer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
proteolytic modification
-
specific cleavage of caspase-3 at a specific cleavage site within the alpha-subunit at residue 46 in the sequence DWMD*G
additional information
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structures of the catalytic core, residues 1-298, of the gamma-subunit, the binary complex with Mn2+/beta-gamma-imidoadenosine 5'-triphosphate to a resolution of 2.6 A and the binary complex with Mg2+/ADP to a resolution of 3.0 A
-
structure of a truncated form of the gamma-subunit of phosphorylase kinase in a ternary complex with a non-hydrolysable ATP analogue, adenylylimidodiphosphate, and a heptapeptide substrate related in sequence to both the natural substrate and to the optimal peptide substrate
-
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, i.e. Phkgammatrnc, in the presence of Mg-ATP, X-ray data
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
construction of PhKbeta subunit deletion mutants
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
PhK is almost inactive at pH 6.8
706785
6
-
below, rapid irreversible inactivation
492109
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h stable
30
-
at least 30 min
37
-
50% loss of nonactivated enzyme activity within 15 min, 50% loss of alphagammadelta subunit complex activity within 7 min, 90% loss of gammadelta subunit complex activity within 5 min
40
-
t1/2: 3 min, in 10% ethylene glycol, pH 8
45
-
t1/2: 1 min, in 10% ethylene glycol, pH 8
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
About 70% loss of activity during centrifugation for 5 h on a glycerol density gradient
-
Delta-Subunit remains tightly bound to alphagammadelta subunit complex even in the presence of 8 M urea
-
Effects of protein concentration, buffer and ATP on stability and dissociation behaviour of trypsin-activated enzyme
-
In the presence of ATP nonactivated enzyme does not dissociate into catalytically active subunits as trypsin-activated enzyme does
-
Inactive gamma subunit after reverse-phase HPLC can be reactivated by dilution into ice-cold, pH 8.2, Ca2+/calmodulin containing buffer
-
Incubation of nonactivated enzyme with 100 mM ATP at 0C dissociates the 23 S enzyme to active 7.5 S and 14 S subunits, with LiBr it produces 5 S subunits
-
isoelectric focusing inactivates
-
Nonactivated or protein kinase-activated enzyme stable in the cold, not trypsin-activated enzyme
-
Rabbit muscle enzyme is subject to pressure denaturation leading to the formation of polydisperse aggregates
-
unstable in dilute solutions
-
Unstable in the presence of Mg2+
-
With strong tendency to aggregate, unstable in high concentrations of ammonium sulfate for prolonged periods
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, in 50 mM sodium glycerophosphate, 0.1% v/v 2-mercaptoethanol, pH 7, 2 mM EDTA, 50% v/v glycerol, at least 1 year
-
-20C, partially purified, at least 2 months
-
-25C, in 50% ethylene glycol, at least 1 month
-
-80C in 50 mM HEPES buffer (pH 6.8, 10% w/v sucrose, and 0.2 mM EDTA)
-
-80C, 50 mM Hepes, pH 6.8, 0.2 mM EDTA, 10% sucrose
-
0-4C, in 5-20% glycerol, 70% loss of activity within 5 h, more rapid inactivation in 5-20% sucrose
-
0C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 30% loss of activity within 4 h
-
0C, in 10% ethylene glycol, at least 1 week
-
20 C, 25 mM Na-glycerol phosphate buffer, pH 7.05, 1 mM EDTA, 0.5 mM 2-mercaptoetanol, 50% glycerol, stored for 3 weeks
-
20C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h
-
Frozen, at least 6 months
-
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
2 isozymes separable by calmodulin affinity chromatography; isolation of denatured subunits; overview
-
active gamma subunit from inactive form by reverse-phase HPLC)
-
alpha, alpha' and beta subunits by preparative SDS-PAGE
-
as in vivo activated phosphorylase sa
-
as nonactivated enzyme; to near homogeneity (phosphorylase b is a persistent contaminant)
-
by affinity chromatography on calmodulin-Sepharose 4B; catalytically active alphagammadelta complexes; catalytically active gammadelta complexes
-
catalytic subunit (i.e. gamma subunit, from holoenzyme by dissociation)
-
catalytic subunit as expressed in Escherichia coli
-
catalytically active alphagammadelta complexes
-
catalytically active proteolytic product of holoenzyme; liver; to near homogeneity
-
DEAE Toyopearl 650M column chromatography
-
delta subunit
-
from protein-glycogen complex; to near homogeneity
-
from skeletal muscle
-
homogenous alpha, beta and gamma subunits
-
isolation of denatured subunits (from nonactivated enzyme)
-
native and proteolytically generated enzyme forms
-
native enzyme from psoas muscle
-
native enzyme from skeletal muscle by anion exchange chromatography to homogeneity
-
native enzyme from skeletal muscle, recombinant enzyme subunit subcomplexes from Sf9 insect cells
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit
-
alpha, gamma, delta-trimer, complex is shown to be unable to phosphorylate glyceraldehyde-3-phosphate dehydrogenase
-
cooverexpression with the beta subunit of the rabbit enzyme with the rat holoenzyme and rat alphagammadelta and gammadelta subunit complexes in Spodoptera frugiperda Sf9 cells via the baculovirus infection system, resulting in formation of subunit subcomplexes, overview
-
expressed as a N-terminal GST fusion, expressed in B834 (DE3)pLyS cells at 18C
-
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, expressed in Escherichia coli
-
two hybrid rabbit DNA library screening using the yeast strain EGY48 and a C-terminal fragment of isozyme PhKalpha, expression of the enzyme and interaction partners in C2C12 cells
-
two-hybrid plasmid construction of fusions containing the PhK beta subunit and its deletion mutants and expression in a yeast two-hybrid system
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kemp, B.E.; Pearson, R.B.; House, M.
Pseudosubstrate-based peptide inhibitors
Methods Enzymol.
201
287-304
1991
Homo sapiens, Mus musculus, Oryctolagus cuniculus
Manually annotated by BRENDA team
da Cruz e Silva, E.F.; Cohen, P.T.
Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase
FEBS Lett.
220
36-42
1987
Oryctolagus cuniculus, Oryctolagus cuniculus (P00518)
Manually annotated by BRENDA team
Dasgupta, M.; Blumenthal, D.K.
Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory
J. Biol. Chem.
270
22283-22289
1995
Oryctolagus cuniculus, Oryctolagus cuniculus (P00518)
Manually annotated by BRENDA team
Dasgupta, M.; Honeycutt, T.; Blumenthal, D.K.
The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin
J. Biol. Chem.
264
17156-17163
1989
Oryctolagus cuniculus (P00518)
Manually annotated by BRENDA team
Lowe, E.D.; Noble, M.E.; Skamnaki, V.T.; Oikonomakos, N.G.; Owen, D.J.; Johnson, L.N.
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition
EMBO J.
16
6646-6658
1997
Oryctolagus cuniculus (P00518)
Manually annotated by BRENDA team
Owen, D.J.; Noble, M.E.; Garman, E.F.; Papageorgiou, A.C.; Johnson, L.N.
Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product
Structure
3
467-482
1995
Oryctolagus cuniculus, Oryctolagus cuniculus (P00518)
Manually annotated by BRENDA team
Reimann, E.M.; Titani, K.; Ericsson, L.H.; Wade, R.D.; Fischer, E.H.; Walsh, K.A.
Homology of the gamma subunit of phosphorylase b kinase with cAMP-dependent protein kinase
Biochemistry
23
4185-4192
1984
Oryctolagus cuniculus, Oryctolagus cuniculus (P00518)
Manually annotated by BRENDA team
Krebs, E.G.; Fischer, E.H.
Phosphorylase b-to-a converting enzyme of rabbit skeletal muscle
Biochim. Biophys. Acta
20
150-157
1956
Oryctolagus cuniculus
Manually annotated by BRENDA team
Krebs, E.G.; Love, D.S.; Bratvold, G.E.; Trayser, K.A.; Meyer, W.L.; Fischer, E.H.
Purification and properties of rabbit skeletal muscle phosphorylase b kinase
Biochemistry
3
1022-1033
1964
Oryctolagus cuniculus
Manually annotated by BRENDA team
Meyer, W.L.; Fischer, E.H.; Krebs, E.G.
Activation of skeletal muscle phosphorylase b kinase by calcium ion
Biochemistry
3
1033-1039
1964
Oryctolagus cuniculus
Manually annotated by BRENDA team
Graves, D.J.; Hayakawa, T.; Horvitz, R.A.; Beckman, E.; Krebs, E.G.
Studies on the subunit structure of trypsin-activated phosphorylase kinase
Biochemistry
12
580-585
1973
Oryctolagus cuniculus
Manually annotated by BRENDA team
Hayakawa, T.; Perkins, J.P.; Walsh, D.A.; Krebs, E.G.
Physiochemical properties of rabbit skeletal muscle phosphorylase kinase
Biochemistry
12
567-573
1973
Oryctolagus cuniculus
Manually annotated by BRENDA team
Hayakawa, T.; Perkins, J.P.; Krebs, E.G.
Studies of the subunit structure of rabbit skeletal muscle phosphorylase kinase
Biochemistry
12
574-580
1973
Oryctolagus cuniculus
Manually annotated by BRENDA team
Tu, J.I.; Graves, D.J.
Inhibition of the phosphorylase kinase catalyzed reaction by glucose-6-P
Biochem. Biophys. Res. Commun.
53
59-65
1973
Oryctolagus cuniculus
Manually annotated by BRENDA team
Yeoman, S.J.; Cohen, P.
The hormonal control of activity of skeletal muscle phosphorylase kinase. Phosphorylation of the enzyme at two sites in vivo in response to adrenalin
Eur. J. Biochem.
51
93-104
1975
Oryctolagus cuniculus
Manually annotated by BRENDA team
Pickett-Gies, C.A.; Walsh, D.A.
Phosphorylase kinase
The Enzymes, 3rd. Ed. (Boyer, P. D. , Krebs, E. G. , eds. )
17
395-456
1986
Bos taurus, Cavia porcellus, Gallus gallus, Mus musculus, Oryctolagus cuniculus, Rattus norvegicus, Saccharomyces cerevisiae, Squalus acanthias
-
Manually annotated by BRENDA team
Kilimann, M.; Heilmeyer, L.M.G.
The effect of Mg2+ on the Ca2+-binding properties of non-activated phosphorylase kinase
Eur. J. Biochem.
73
191-197
1977
Oryctolagus cuniculus
Manually annotated by BRENDA team
Cohen, P.; Burchell, A.; Foulkes, J.G.; Cohen, P.T.W.; Vanaman, T.C.; Nairn, A.C.
Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase
FEBS Lett.
92
287-293
1978
Oryctolagus cuniculus
Manually annotated by BRENDA team
Sakai, K.; Matsumura, S.; Okimura, Y.; Yamamura, H.; Nishizuka, Y.
Liver glycogen phosphorylase kinase. Partial purification and characterization
J. Biol. Chem.
254
6631-6637
1979
Oryctolagus cuniculus
Manually annotated by BRENDA team
Vandenheede, J.R.; De Wulf, H.; Merlevede, W.
Liver phosphorylase b kinase. Cyclic-AMP-mediated activation and properties of the partially purified rat-liver enzyme
Eur. J. Biochem.
101
51-58
1979
Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
Carlson, G.M.; Bechtel, P.J.; Graves, D.J.
Chemical and regulatory properties of phosphorylase kinase and cyclic AMP-dependent protein kinase
Adv. Enzymol. Relat. Areas Mol. Biol.
50
41-115
1979
Calliphoridae, Mus musculus, Oryctolagus cuniculus, Squalus acanthias
Manually annotated by BRENDA team
Skuster, J.R.; Chan, K.F.J.; Graves, D.J.
Isolation and properties of the catalytically active gamma subunit of phosphorylase b kinase
J. Biol. Chem.
255
2203-2210
1980
Oryctolagus cuniculus
Manually annotated by BRENDA team
Pocinwong, S.; Blum, H.; Malencik, D.; Fisher, E.H.
Phosphorylase kinase from dogfish skeletal muscle. Purification and properties
Biochemistry
20
7219-7226
1981
Oryctolagus cuniculus, Squalus acanthias
Manually annotated by BRENDA team
Cohen, P.; Klee, C.B.; Picton, C.; Shenolikar, S.
Calcium control of muscle phosphorylase kinase through the combined action of calmodulin and troponin
Ann. N. Y. Acad. Sci.
356
151-161
1980
Oryctolagus cuniculus, Rattus norvegicus
Manually annotated by BRENDA team
King, M.M.; Carslon, G.M.
Synergistic effect of Ca2+ and Mg2+ in promoting an activity of phosphorylase kinase that is insensitive to ethylene glycol bis(beta-aminoethyl ether)-N,N-tetraacetic acid
Arch. Biochem. Biophys.
209
517-523
1981
Oryctolagus cuniculus
Manually annotated by BRENDA team
King, M.M.; Carslon, G.M.
Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions
J. Biol. Chem.
256
11058-11064
1981
Oryctolagus cuniculus
Manually annotated by BRENDA team
Chan, K.F.J.; Graves, D.J.
Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexes
J. Biol. Chem.
257
5948-5955
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Chan, K.F.J.; Graves, D.J.
Rabbit skeletal muscle phosphorylase kinase. Interactions between subunits and influence of calmodulin on different complexes
J. Biol. Chem.
257
5956-5961
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kilimann, M.W.; Heilmeyer, L.M.G.
Multiple activities on phosphorylase kinase. 1. Characterization of three partial activities by their response to calcium ion, magnesium ion, pH, and ammonium chloride and effect of activation by phosphorylation and proteolysis
Biochemistry
21
1727-1734
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kilimann, M.W.; Heilmeyer, L.M.G.
Multiple activities on phosphorylase kinase. 2. Different specificities toward the protein substrates phosphorylase b, troponin, and phosphorylase kinase
Biochemistry
21
1735-1739
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Chan, K.F.J.; Graves, D.J.
Isolation and physicochemical properties of active complexes of rabbit muscle phosphorylase kinase
J. Biol. Chem.
257
5939-5947
1982
Oryctolagus cuniculus
Manually annotated by BRENDA team
Picton, C.; Shenolikar, S.; Grand, R.; Cohen, P.
Calmodulin as an integral subunit of phosphorylase kinase from rabbit skeletal muscle
Methods Enzymol.
102
219-227
1983
Oryctolagus cuniculus
Manually annotated by BRENDA team
Cohen, P.
Phosphorylase kinase from rabbit skeletal muscle
Methods Enzymol.
99
243-250
1983
Oryctolagus cuniculus
Manually annotated by BRENDA team
Sul, H.S.; Dirden, B.; Angelos, K.L.; Hallenbeck, P.; Walsh, D.
Cardiac phosphorylase kinase: preparation and properties
Methods Enzymol.
99
250-259
1983
Bos taurus, Oryctolagus cuniculus
Manually annotated by BRENDA team
Chan, K.F.J.; Graves, D.J.
Separation of the subunits of muscle phosphorylase kinase
Methods Enzymol.
99
259-267
1983
Oryctolagus cuniculus
Manually annotated by BRENDA team
Graves, D.J.
Use of peptide substrates to study the specificity of phosphorylase kinase phosphorylation
Methods Enzymol.
99
268-278
1983
Oryctolagus cuniculus
Manually annotated by BRENDA team
Negami, A.; Sakai, K.; Kobayashi, T.; Tabuchi, H.; Nakamura, S.; Yamamura, H.
Two diverse effects of poly(L-lysine) on rabbit skeletal muscle phosphorylase kinase: stimulation of autophosphorylation and inhibition of its activity
FEBS Lett.
166
335-338
1984
Oryctolagus cuniculus
Manually annotated by BRENDA team
Crabb, J.W.; Heilmeyer, L.M.G.
High performance liquid chromatography purification and structural characterization of the subunits of rabbit muscle phosphorylase kinase
J. Biol. Chem.
259
6346-6350
1984
Oryctolagus cuniculus
Manually annotated by BRENDA team
Srivastava, A.K.
Inhibition of phosphorylase kinase, and tyrosine protein kinase activities by quercetin
Biochem. Biophys. Res. Commun.
131
1-5
1985
Oryctolagus cuniculus
Manually annotated by BRENDA team
Jennissen, H.P.; Petersen-von Gehr, J.K.H.; Botzet, G.
Activation and inhibition of phosphorylase kinase by monospecific antibodies against preparatively isolated alpha, beta and gamma subunits
Eur. J. Biochem.
147
619-630
1985
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kee, S.M.; Graves, D.J.
Properties of the gamma subunit of phosphorylase kinase
J. Biol. Chem.
262
9448-9453
1987
Oryctolagus cuniculus
Manually annotated by BRENDA team
Paudel, H.K.; Carlson, G.M.
Inhibition of the catalytic subunit of phosphorylase kinase by its alpha/beta subunits
J. Biol. Chem.
262
11912-11915
1987
Oryctolagus cuniculus
Manually annotated by BRENDA team
Cox, D.E.; Meinke, M.H.; Edstrom, R.D.
Mechanism of calmodulin inhibition of cAMP-dependent protein kinase activation of phosphorylation kinase
Arch. Biochem. Biophys.
259
350-362
1987
Oryctolagus cuniculus
Manually annotated by BRENDA team
Crabb, J.W.; Harris, W.R.; Johnson, C.M.; Sotiroudis, T.G.; Kuhn, C.C.; Heilmeyer, L.M.G.
Electrophoretic purification of the alpha and beta subunits of phosphorylase kinase and evidence in support of the deduced amino acid sequences
Electrophoresis
11
133-140
1990
Oryctolagus cuniculus
Manually annotated by BRENDA team
Elliott, L.H.; Wilkinson, S.E.; Sedgwick, A.D.; Hill, C.H.; Lawton, G.; Davis, P.D.; Nixon, J.S.
K252a is a potent and selective inhibitor of phosphorylase kinase
Biochem. Biophys. Res. Commun.
171
148-154
1990
Oryctolagus cuniculus
Manually annotated by BRENDA team
Farrar, Y.J.K.; Carlson, G.M.
Kinetic characterization of the calmodulin-activated catalytic subunit of phosphorylase kinase
Biochemistry
30
10274-10279
1991
Oryctolagus cuniculus
Manually annotated by BRENDA team
Beleta, J.; Benedicto, P.; Gella, F.J.
Regulatory properties of rabbit liver phosphorylase kinase
Int. J. Biochem.
22
453-460
1990
Oryctolagus cuniculus
Manually annotated by BRENDA team
Beleta, J.; Benedicto, P.; Aymerich, P.; Gella, F.J.
Purification and characterization of native and proteolytic forms of rabbit liver phosphorylase kinase
Int. J. Biochem.
22
443-451
1990
Oryctolagus cuniculus
Manually annotated by BRENDA team
Paudel, H.K.; Carlson, G.M.
Functional and structural similarities between the inhibitory region of troponin I coded by exon VII and the calmodulin-binding regulatory region of the catalytic subunit of phosphorylase kinase
Proc. Natl. Acad. Sci. USA
87
7285-7289
1990
Oryctolagus cuniculus
Manually annotated by BRENDA team
Heilmeyer, L.M.G.
Molecular basis of signal integration in phosphorylase kinase
Biochim. Biophys. Acta
1094
168-174
1991
Oryctolagus cuniculus
Manually annotated by BRENDA team
Paudel, H.K.; Xu, Y.H.; Jarrett, H.W.; Carlson, G.M.
The model calmodulin-binding peptide melittin inhibits phosphorylase kinase by interacting with its catalytic center
Biochemistry
32
11865-11872
1993
Oryctolagus cuniculus
Manually annotated by BRENDA team
Cheng, A.; Fitzgerald, T.J.; Carlson, G.M.
Adenosine 5-diphosphate as an allosteric effector of phosphorylase kinase from rabbit skeletal muscle
J. Biol. Chem.
260
2535-2542
1985
Oryctolagus cuniculus
Manually annotated by BRENDA team
Huang, C.Y.F.; Yuan, C.J.; Blumenthal, D.K.; Graves, D.J.
Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit
J. Biol. Chem.
270
7183-7188
1995
Oryctolagus cuniculus
Manually annotated by BRENDA team
Owen, D.J.; Papageorgiou, A.C.; Garman, E.F.; Noble, M.E.M.; Johnson, L.N.
Expression, purification and crystallisation of phosphorylase kinase catalytic domain
J. Mol. Biol.
246
374-381
1995
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kee, S.M.; Graves, D.J.
Isolation and properties of the active gamma subunit of phosphorylase kinase
J. Biol. Chem.
261
4732-4737
1986
Oryctolagus cuniculus
Manually annotated by BRENDA team
Xu, Y.H.; Wilkinson, D.A.; Carlson, G.M.
Divalent cations but not other activators enhance phosphorylase kinases affinity for glycogen phosphorylase
Biochemistry
35
5014-5021
1996
Oryctolagus cuniculus
Manually annotated by BRENDA team
Kumar, P.; Brushia, R.J.; Hoye, E.; Walsh, D.A.
Baculovirus-mediated overexpression of the phosphorylase b kinase holoenzyme and alpha gamma delta and gamma delta subcomplexes
Biochemistry
43
10247-10254
2004
Oryctolagus cuniculus, Rattus norvegicus (Q64649)
Manually annotated by BRENDA team
Chebotareva, N.A.; Andreeva, I.E.; Makeeva, V.F.; Livanova, N.B.; Kurganov, B.I.
Effect of molecular crowding on self-association of phosphorylase kinase and its interaction with phosphorylase b and glycogen
J. Mol. Recognit.
17
426-432
2004
Oryctolagus cuniculus
Manually annotated by BRENDA team
Hilder, T.L.; Carlson, G.M.; Haystead, T.A.; Krebs, E.G.; Graves, L.M.
Caspase-3 dependent cleavage and activation of skeletal muscle phosphorylase b kinase
Mol. Cell. Biochem.
275
233-242
2005
Mus musculus, Oryctolagus cuniculus
Manually annotated by BRENDA team
Priddy, T.S.; MacDonald, B.A.; Heller, W.T.; Nadeau, O.W.; Trewhella, J.; Carlson, G.M.
Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering
Protein Sci.
14
1039-1048
2005
Oryctolagus cuniculus
Manually annotated by BRENDA team
Nadeau, O.W.; Gogol, E.P.; Carlson, G.M.
Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase
Protein Sci.
14
914-920
2005
Oryctolagus cuniculus
Manually annotated by BRENDA team
Archila, S.; King, M.A.; Carlson, G.M.; Rice, N.A.
The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle
Biochem. Biophys. Res. Commun.
345
1592-1599
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Makeeva, V.F.; Chebotareva, N.A.; Andreeva, I.E.; Livanova, N.B.; Kurganov, B.I.
Interaction of phosphorylase kinase from rabbit skeletal muscle with flavin adenine dinucleotide
Biochemistry (Moscow)
71
652-657
2006
Oryctolagus cuniculus
Manually annotated by BRENDA team
Nadeau, O.W.; Anderson, D.W.; Yang, Q.; Artigues, A.; Paschall, J.E.; Wyckoff, G.J.; McClintock, J.L.; Carlson, G.M.
Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides
J. Mol. Biol.
365
1429-1445
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Priddy, T.S.; Price, E.S.; Johnson, C.K.; Carlson, G.M.
Single molecule analyses of the conformational substates of calmodulin bound to the phosphorylase kinase complex
Protein Sci.
16
1017-1023
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Priddy, T.S.; Middaugh, C.R.; Carlson, G.M.
Electrostatic changes in phosphorylase kinase induced by its obligatory allosteric activator Ca2+
Protein Sci.
16
517-527
2007
Oryctolagus cuniculus
Manually annotated by BRENDA team
Boulatnikov, I.G.; Nadeau, O.W.; Daniels, P.J.; Sage, J.M.; Jeyasingham, M.D.; Villar, M.T.; Artigues, A.; Carlson, G.M.
The regulatory beta subunit of phosphorylase kinase interacts with glyceraldehyde-3-phosphate dehydrogenase
Biochemistry
47
7228-7236
2008
Mus musculus, Oryctolagus cuniculus
Manually annotated by BRENDA team
Chebotareva, N.A.; Meremyanin, A.V.; Makeeva, V.F.; Livanova, N.B.; Kurganov, B.I.
Cooperative self-association of phosphorylase kinase from rabbit skeletal muscle
Biophys. Chem.
133
45-53
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team
Nadeau, O.W.; Wyckoff, G.J.; Paschall, J.E.; Artigues, A.; Sage, J.; Villar, M.T.; Carlson, G.M.
CrossSearch, a user-friendly search engine for detecting chemically cross-linked peptides in conjugated proteins
Mol. Cell. Proteomics
7
739-749
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team
Liu, W.; Priddy, T.S.; Carlson, G.M.
Physicochemical changes in phosphorylase kinase associated with its activation
Protein Sci.
17
2111-2119
2008
Oryctolagus cuniculus
Manually annotated by BRENDA team
Carriere, C.; Mornon, J.; Venien-Bryan, C.; Boisset, N.; Callebaut, I.
Calcineurin B-like domains in the large regulatory alpha /beta subunits of phosphorylase kinase
Proteins Struct. Funct. Bioinform.
71
1597-1606
2008
Aedes aegypti (Q171G3), Caenorhabditis elegans (P34335), Oryctolagus cuniculus (P12798), Oryctolagus cuniculus (P18688), Oryza sativa (A2WRR1), Takifugu rubripes (Q9W6R1), Tetraodon nigroviridis (Q4S8G1)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Venien-Bryan, C.; Jonic, S.; Skamnaki, V.; Brown, N.; Bischler, N.; Oikonomakos, N.G.; Boisset, N.; Johnson, L.N.
The structure of phosphorylase kinase holoenzyme at 9.9 A resolution and location of the catalytic subunit and the substrate glycogen phosphorylase
Structure
17
117-127
2009
Oryctolagus cuniculus (P00518)
Manually annotated by BRENDA team
Nadeau, O.W.; Lane, L.A.; Xu, D.; Sage, J.; Priddy, T.S.; Artigues, A.; Villar, M.T.; Yang, Q.; Robinson, C.V.; Zhang, Y.; Carlson, G.M.
Structure and location of the regulatory beta subunits in the (alphabetagammadelta)4 phosphorylase kinase complex
J. Biol. Chem.
287
36651-36661