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Information on EC 2.7.11.19 - phosphorylase kinase
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EC Tree
2.7.11.19 phosphorylase kinaseIUBMB 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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Word Map
- 2.7.11.19
- calmodulin
-
camp-dependent
- amp
- phosphatases
- myosin
- glycogenosis
- casein
- autophosphorylation
-
holoenzyme
- alpha-subunits
- glucagon
- troponin
-
nonactivated
-
x-linked
-
calmodulin-dependent
- phosphoprotein
-
gamma-subunits
-
glycogenolytic
- mgatp
- hepatomegaly
-
calmodulin-binding
-
sarcoplasmic
-
cohen
- inhibitor-1
- phosphopeptide
-
hexadecameric
-
phosphorylatable
-
delta4
-
debranching
-
2.4.1.1
- trifluoperazine
-
bisbeta-aminoethyl
-
phosphatase-2a
-
amp-independent
- phosvitin
- amylo-1,6-glucosidase
-
cyclic-amp-dependent
-
kinase-catalyzed
-
3':5'-monophosphate
-
kinase-deficient
-
seryl
- gizzard
-
carlson
-
calmodulin-sepharose
-
delta-subunits
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
phosphorylase kinase, phosphorylase b kinase, glycogen phosphorylase kinase, phkg1, phk alpha, dphk-gamma, glycogen phosphorylase b kinase, psk-c3, kpi-2 kinase, phosphorylase kinase beta, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dephosphophosphorylase kinase
-
-
-
-
EC 2.7.1.38
glycogen phosphorylase b kinase
Glycogen phosphorylase kinase
GPK
kinase, phosphorylase (phosphorylating)
-
-
-
-
PhK
PHKB
PhKG1
Phosphorylase b kinase
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
phosphorylase B kinase gamma catalytic chain, testis/liver isoform
phosphorylase kinase
phosphorylase kinase beta
PSK-C3
-
-
-
-
SkM Phk
EC 2.7.1.38
-
formerly, transferred to EC 2.7.11.19
Glycogen phosphorylase kinase
-
-
-
-
PhK
-
-
Phosphorylase b kinase
-
-
-
-
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
-
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
-
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
-
phosphorylase B kinase gamma catalytic chain, testis/liver isoform
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
mechanism
-
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9001-88-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + alphagammadelta subunit complex
ADP + activated alphagammadelta subunit complex
-
autophosphorylation, by incorporation of phosphate into alpha subunit
-
?
ATP + glycogen phosphorylase
?
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen phosphorylase
ADP + phosphorylated glycogen phosphorylase
-
-
-
-
?
ATP + glycogen S peptide
ADP + phosphorylated glycogen S peptide
-
synthetic peptide corresponding to residues 5-18 of its convertible region
-
-
?
ATP + Lys-Arg-Glu-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Glu-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp
-
-
-
-
?
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp-Gly-Ile
-
-
-
-
?
ATP + Lys-Arg-Lys-Glu-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Glu-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + Lys-Glu-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Glu-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + peptides derived from glycogen synthase
?
-
rabbit, overview
-
-
?
ATP + protein
ADP + phosphoprotein
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 + 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
-
-
-
-
?
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
-
i.e. phosphorylase b peptide (5-18)
-
-
?
ATP + synthetic pentadecapeptide
?
-
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
?
-
overview, phosphorylation at the same site as glycogen synthase
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
glycogen phosphorylase brain form, PYGB
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
rabbit muscle GP
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
-
?
2 ATP + phosphorylase b
2 ADP + phosphorylase a
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
the phosphorylase kinase phosphorylates proteins and proteolytic fragments thereof, phosphorylation of multiple residues in the substrate sequence by mammary gland casein kinase
-
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
-
activation of Ca2+-transporting ATPase, EC 3.6.3.8, accelerating the Ca2+ transport in the sarcoplasmic reticulum of muscle, regulatory role, effect of the enzyme on Ca2+ transport and enzyme kinetics
-
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
-
activation of Ca2+-transporting ATPase, EC 3.6.1.3, accelerating the Ca2+ transport in the sarcoplasmic reticulum of muscle, regulatory role, effect of the enzyme on Ca2+ transport and enzyme kinetics
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
activation of glycogen phosphorylase which acts as a Ca2+-dependent blood glucose sensor liberating glucose from glycogen as needed, involved in regulation of the glycogen phosphorylase
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
regulatory enzyme in the activation cascade of glycogenolysis
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
the enzyme catalyzes the phosphorylation of inactive glycogen phosphorylase b on Ser-14 resulting in the formation of active glycogen phosphorylase a
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
activation of glycogen phosphorylase b, EC 2.4.1.1, accelerating the glycogenolysis in muscle, regulatory role
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
activation of glycogen phosphorylase b, EC 2.4.1.1, accelerating the glycogenolysis in muscle, regulatory role
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
the hexadecameric enzyme complex that catalyzes the phosphorylation and activation of glycogen phosphorylase b
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
PhK catalyzes the Ca2+- and cAMP-dependent glycogen phosphorylase b phosphorylation and activation
-
-
?
ATP + glycogen synthase
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen synthase
?
-
conversion to a glucose 6-phosphate dependent form
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
-
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
rabbit phosphorylase kinase
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
inactivation of skeletal muscle glycogen synthase in the presence or absence of EGTA
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
glycogen synthase a
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
phosphorylatable residue: Ser-7
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
at high concentration, from rabbit skeletal muscle
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
at the same rate as phosphorylase b
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
inactivation of skeletal muscle glycogen synthase in the presence or absence of EGTA
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
at high concentration, from rabbit skeletal muscle
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
at high concentration, from yeast
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
-
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
in the presence of Mg2+ and Ca2+
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
phosphorylation sites
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
-
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
phosphorylates alpha and beta, not gamma or delta subunits
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
ATP can be replaced by dATP or adenosine 5'-(3-thiotriphosphate) with 50% and 10% efficiency, respectively
-
?
ATP + phosphorylase b
?
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
?
-
vital process for short term energy supply to the cell, located at an interface between signalling and metabolic pathway
-
-
?
ATP + phosphorylase b
?
-
involved in glycogen metabolism regulation
-
-
?
ATP + phosphorylase b
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylase b from heart
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
binding studies with immobilized substrate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
incorporation of terminal phosphate of ATP into phosphorylase b
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site located 14 residues from amino terminal
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
the enzyme interacts with glycogen and phosphorylase b
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylated phosphorylase b
-
KPI-2 reacts with Ser residues either preceded by or followed by Pro residues, does not strictly require an adjacent Pro residue
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
overview
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
overview
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
rabbit
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
overview
-
-
?
ATP + synthetic tetradecapeptide
?
-
i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
-
-
?
ATP + synthetic tetradecapeptide
?
-
substrate for holoenzyme and for catalytic gamma subunit
-
-
?
ATP + synthetic tetradecapeptide
?
-
from amino-terminal of phosphorylase b
-
-
?
ATP + synthetic tetradecapeptide
?
-
i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
-
-
?
ATP + synthetic tetradecapeptide
?
-
phosphorylation site: Ser between Ile and Val
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
phosphorylation site (Thr-residue)
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
not rabbit or dogfish troponin I
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
rabbit phosphorylase kinase
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
not rabbit or dogfish troponin I
-
-
?
ATP + troponin T
ADP + phosphotroponin T
-
not rabbit or dogfish troponin T
-
-
?
ATP + troponin T
ADP + phosphotroponin T
-
not rabbit or dogfish troponin T
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
-
phosphorylation is very slow, binds tightly to enzyme and acts as inhibitor for the phosphorylation of glycogen phosphorylase b
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
-
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
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
-
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
catalyzes phosphorylation and activation of glycogen phosphorylase b and hence plays a key role in the cascade system of regulation of glycogen metabolism
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
regulates energy production through its Ca2+-dependent activation of glycogen phosphorylase in the cascade activation of glycogenolysis, only known kinase that activates glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
GTP + phosphorylase b
GDP + phosphorylase a
-
cosubstrate: Mg-UTP complex
-
-
?
UTP + phosphorylase b
UDP + phosphorylase a
-
cosubstrate: Mg-UTP complex
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
enzyme is required in early embryonic processes, such as gastrulation and mesoderm formation
-
-
?
additional information
?
-
-
protein kinases and protein phosphatases regulate enzyme activities in the cell, overview
-
-
?
additional information
?
-
-
poor activity on free amino acids, consensus sequence of PhK is R-XXS/TF-F
-
-
?
additional information
?
-
-
troponin (whole complex) and histone IIAS are no substrates
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
mutations in PHKG2, the catalytic gamma subunit, are associated with an increased cirrhosis risk
-
-
?
additional information
?
-
-
mutations in PHKG2, the catalytic gamma subunit, are associated with an increased cirrhosis risk
-
-
?
additional information
?
-
-
modeling of glycogen phosphorylase regulation by Ca2+-oscillations, and dephosphorylation and phosphorylation involving the enzyme and a phosphatase, overview
-
-
?
additional information
?
-
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
?
additional information
?
-
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
?
additional information
?
-
-
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
?
additional information
?
-
-
correlation of gene transcriptional processing and catalytic regulation of PhK subunits, overview
-
-
?
additional information
?
-
-
hormonal regulation of KPI-2, kinase KPI-2 reveals reactivity with cystic fibrosis transmembrane conductance regulator and phosphorylase
-
-
?
additional information
?
-
-
phosphorylase-b kinase deficient patients, suffering glycogen storage disease GSD IXa, show an accumulation of fat in the liver that resolves with aging, overview
-
-
?
additional information
?
-
plays a regulatory role in a cascade of enzymatic reactions controlling glycogen breakdown
-
-
?
additional information
?
-
-
plays a regulatory role in a cascade of enzymatic reactions controlling glycogen breakdown
-
-
?
additional information
?
-
-
substrate specificity, the enzyme depends on basic residues for substrate recognition, overview, the residues at the substrate phosphorylation site greatly influence the enzyme activity, autoregulation by a pseudosubstrate mechanism, overview
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
creatine phosphate, phosphoenolpyruvate, actin, parvalbumin, protamin, dogfish or rabbit myosin, adenosine 5'-(3-methyltriphosphate), 5'-adenylylimidodiphosphate (dogfish) are no substrates
-
-
?
additional information
?
-
-
no substrates are phosphorylase kinase gamma subunit
-
-
?
additional information
?
-
-
Lys-Gln-Ile-Ser-Val-Arg, Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Gly-Ser-Gly-Arg-Gly-Leu, Lys-Gln-Ile-Thr-Val-Arg, Arg-Lys-Gln-Ile-Thr-Val-Arg are no substrates
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
no spontaneous or MnSO4-induced dephosphorylation of activated enzyme
-
-
?
additional information
?
-
-
polylysine and polyarginine are no substrates
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation
-
-
?
additional information
?
-
-
interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle
-
-
?
additional information
?
-
-
key enzyme in regulating glycogenolytic flux in skeletal muscle in response to changing energy demands, phosphorylase kinase associates with the cytoskeletal organizing protein Cdc42-interacting protein 4, CIP4, in vivo in skeletal muscle, the cognate binding domain on CIP4 lies between residues 398 and 545, the interaction is independent of the SH3 domain
-
-
?
additional information
?
-
-
the enzyme complex regulates glycogenolysis
-
-
?
additional information
?
-
-
subunit PhKalpha is autophosphorylated
-
-
?
additional information
?
-
the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme
-
-
?
additional information
?
-
development of a highly sensitive and nonradioactive assay for phosphorylase kinase activity by measuring the enhanced glycogen phosphorylase activity towards a pyridylaminated maltohexaose, method evaluation, phosphate quantification by the FiskeSubbarow method, overview
-
-
?
additional information
?
-
the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
no spontaneous or MnSO4-induced dephosphorylation of activated enzyme
-
-
?
additional information
?
-
the enzyme performs autophosphorylation
-
-
?
additional information
?
-
-
creatine phosphate, phosphoenolpyruvate, actin, parvalbumin, protamin, dogfish or rabbit myosin, adenosine 5'-(3-methyltriphosphate), 5'-adenylylimidodiphosphate (dogfish) are no substrates
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + glycogen phosphorylase
?
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen phosphorylase
ADP + phosphorylated glycogen phosphorylase
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
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
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
-
?
2 ATP + phosphorylase b
2 ADP + phosphorylase a
-
-
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
-
activation of Ca2+-transporting ATPase, EC 3.6.3.8, accelerating the Ca2+ transport in the sarcoplasmic reticulum of muscle, regulatory role, effect of the enzyme on Ca2+ transport and enzyme kinetics
-
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
-
activation of Ca2+-transporting ATPase, EC 3.6.1.3, accelerating the Ca2+ transport in the sarcoplasmic reticulum of muscle, regulatory role, effect of the enzyme on Ca2+ transport and enzyme kinetics
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
activation of glycogen phosphorylase which acts as a Ca2+-dependent blood glucose sensor liberating glucose from glycogen as needed, involved in regulation of the glycogen phosphorylase
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
regulatory enzyme in the activation cascade of glycogenolysis
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
activation of glycogen phosphorylase b, EC 2.4.1.1, accelerating the glycogenolysis in muscle, regulatory role
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
activation of glycogen phosphorylase b, EC 2.4.1.1, accelerating the glycogenolysis in muscle, regulatory role
-
-
?
ATP + glycogen synthase
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen synthase
?
-
conversion to a glucose 6-phosphate dependent form
-
-
?
ATP + phosphorylase b
?
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
?
-
vital process for short term energy supply to the cell, located at an interface between signalling and metabolic pathway
-
-
?
ATP + phosphorylase b
?
-
involved in glycogen metabolism regulation
-
-
?
ATP + phosphorylase b
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
the enzyme interacts with glycogen and phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
catalyzes phosphorylation and activation of glycogen phosphorylase b and hence plays a key role in the cascade system of regulation of glycogen metabolism
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
regulates energy production through its Ca2+-dependent activation of glycogen phosphorylase in the cascade activation of glycogenolysis, only known kinase that activates glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
additional information
?
-
enzyme is required in early embryonic processes, such as gastrulation and mesoderm formation
-
-
?
additional information
?
-
-
protein kinases and protein phosphatases regulate enzyme activities in the cell, overview
-
-
?
additional information
?
-
mutations in PHKG2, the catalytic gamma subunit, are associated with an increased cirrhosis risk
-
-
?
additional information
?
-
-
mutations in PHKG2, the catalytic gamma subunit, are associated with an increased cirrhosis risk
-
-
?
additional information
?
-
-
modeling of glycogen phosphorylase regulation by Ca2+-oscillations, and dephosphorylation and phosphorylation involving the enzyme and a phosphatase, overview
-
-
?
additional information
?
-
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
?
additional information
?
-
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
?
additional information
?
-
-
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
?
additional information
?
-
-
correlation of gene transcriptional processing and catalytic regulation of PhK subunits, overview
-
-
?
additional information
?
-
-
hormonal regulation of KPI-2, kinase KPI-2 reveals reactivity with cystic fibrosis transmembrane conductance regulator and phosphorylase
-
-
?
additional information
?
-
-
phosphorylase-b kinase deficient patients, suffering glycogen storage disease GSD IXa, show an accumulation of fat in the liver that resolves with aging, overview
-
-
?
additional information
?
-
plays a regulatory role in a cascade of enzymatic reactions controlling glycogen breakdown
-
-
?
additional information
?
-
-
plays a regulatory role in a cascade of enzymatic reactions controlling glycogen breakdown
-
-
?
additional information
?
-
-
interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle
-
-
?
additional information
?
-
-
key enzyme in regulating glycogenolytic flux in skeletal muscle in response to changing energy demands, phosphorylase kinase associates with the cytoskeletal organizing protein Cdc42-interacting protein 4, CIP4, in vivo in skeletal muscle, the cognate binding domain on CIP4 lies between residues 398 and 545, the interaction is independent of the SH3 domain
-
-
?
additional information
?
-
-
the enzyme complex regulates glycogenolysis
-
-
?
additional information
?
-
the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme
-
-
?
additional information
?
-
the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
capable of binding FAD, binding of FAD suppresses self association of enzyme
-
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
can partially replace ATP in the activation of nonactivated enzyme
ATP
-
-
ATP
-
activation of nonactivated enzyme by phosphorylation of subunits A and B, not C
Calmodulin
-
activation of recombinant gamma subunit at pH 6.8, slightly at pH 8.2
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit
Calmodulin
-
no activation of phosphorylated or proteolytically modified enzyme by delta'-subunit
Calmodulin
-
activation of nonactivated enzyme and alphagammadelta subunit complex
Calmodulin
-
in the presence of Ca2+: 1 mol extrinsic calmodulin per mol alphabetagammadelta rabbit enzyme
Calmodulin
-
tightly bound molecule interacts with additional calmodulin in the presence of Ca2+
Calmodulin
-
in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation
Calmodulin
-
in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation
Calmodulin
-
no activation of bovine red skeletal muscle or rabbit cardiac enzymes
Calmodulin
-
mediates Ca2+-sensitivity of the enzyme, calmodulin is identical with the delta-subunit
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Co2+
Fe3+
Li+
Mg2+
Mn2+
phosphate
Sr2+
additional information
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Ca2+
-
Ca2+-sensitivity of the enzyme is mediated by the delta-subunit which is identical with calmodulin
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Ca2+
-
-
Ca2+
phosphorylase kinase is a Ca2+-regulated, multisubunit enzyme that contains calmodulin as an integral subunit, the gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin
Ca2+
-
irreversible activation of nonactivated kinase by preincubation together with a separate kinase-activating factor independent of cAMP, kinetics
Ca2+
-
required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Ca2+
-
stabilization, no absolute requirement for catalytic subunit gamma2
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction
Ca2+
-
stimulates autophosphorylation in micromolar range at pH 6.8, inhibits at millimolar range
Ca2+
-
requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
-
stimulates phosphorylase b binding to enzyme, but to a considerable lesser extent than Mg2+
Ca2+
-
activates, binding structure modeling, Ca2+-binding induces structural perturbation of the subunits and promotes redistribution of density throughout the lobes and bridges of the enzyme structure
Ca2+
-
dependent on, induces enzyme self-association and increases interaction with glycogen
Ca2+
-
activates, the four integral delta subunits of the phosphorylase kinase complex are identical to calmodulin and confer Ca2+ sensitivity to the enzyme, but bind independently of Ca2+, Ca2+ influences the conformational substrates of the subunits, overview
Ca2+
-
is an obligatory allosteric activator absolutely required by the enzyme, Ca2+ activates PhK by binding to its nondissociable calmodulin subunits, it couples the cascade activation of glycogenolysis with muscle contraction, enzyme surface electrostatic properties of solvent accessible charged and polar groups are altered upon the binding of Ca2+ ions
Ca2+
-
induces association, obligatory allosteric activator, binds to an integral, nondissociable molecule of calmodulin (delta-subunit), and thus reveals the protein kinase activity of the catalytic gamma-subunit, which in the absence of Ca2+ ions is constrained by the regulatory alpha- and beta-subunits
Ca2+
-
required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction
Ca2+
-
requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
required for activity phosphorylation by (cAMP-dependent protein kinase)
Mg2+
-
dependent on, Mg2+ is the physiologic metal ion, other divalent cations are able to support nucleotide binding, but only Mn2+, Co2+, and Cd2+ can substitute Mg2+ in supporting the catalytic activity
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
Mg2+
-
required for activity phosphorylation by (cAMP-dependent protein kinase)
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
Mg2+
-
requirement
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
effect of Mg2+ on Ca2+-binding properties of nonactivated enzyme at pH 6.8
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
Mg2+
-
required for activity phosphorylation by (cAMP-dependent protein kinase)
Mg2+
-
dependent on, induces enzyme self-association and increases interaction with glycogen
Mg2+
-
activator, changes in the physicochemical properties of the enzyme induced by Mg2+ under nonactivating (pH 6.8) and activating (pH 8.2) conditions are investigated by circular dichroism spectroscopy, zeta potential analyses, dynamic light scattering, second derivative UV absorption, negative stain electron microscopy, and differential chemical crosslinking. The effects of the activator Mg2+ on some of the properties of the enzyme measured by these techniques are quite different at the two pH values.
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
Mg2+
-
required for activity phosphorylation by (cAMP-dependent protein kinase)
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
required for activity phosphorylation by (cAMP-dependent protein kinase)
Mn2+
-
stimulates activation by catalytic subunit of cAMP-dependent protein kinase
Mn2+
-
at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
alphagammadelta complex undergoes autophosphorylation: up to 4.2 mol phosphate/mol complex incorporated into alpha subunit
phosphate
-
requirement, phosphate containing enzyme
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
phosphate
-
gammadelta subunit complex cannot phosphorylate itself but phosphorylates and activates native enzyme, even in the presence of EGTA or protein kinase inhibitor
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
additional information
-
synopsis of activity by Ca2+/Mg2+ and phosphorylation
additional information
Ca2+ and Mg2+ induce self-aggregation of PhK at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
actin
-
inhibits activation of subunit gamma-troponin C or subunit gamma-calmodulin complexes
Antibodies to rat testis calmodulin
-
calmodulin or troponin (the latter at high concentrations) reverses
-
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
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
Ile-Ser-Val-Arg-Gly
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
LLRDPYALRSVRHLIDNCAFRL
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 336-357
Melittin
-
model calmodulin-binding peptide, mechanism, kinetic, phosphorylase b as substrate
Monospecific antibodies against alpha, beta and gamma subunits
-
mechanism, kinetic, anti-beta subunit reverses inhibition by anti-alpha at pH 6.8
-
poly-L-lysine
-
strong, activated and nonactivated enzyme, stimulates autophosphorylation
proline
-
inhibits enzyme self-association and interaction with glycogen and phosphorylase b
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Asp-Val-Arg-Gly-Leu
-
substrate-directed dead end inhibitor
Trimethylamine N-oxide
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
VIRDPYALPPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 333-354
VIRDPYALRPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 332-353
ATP
-
otherwise activating; total inhibition if ATP concentration exceeds that of divalent cation
ATP
-
otherwise activating; total inhibition if ATP concentration exceeds that of divalent cation (i.e. Mg2+)
ATP
enzyme PhK shows substrate inhibition at high ATP concentration above 3 mM
DTNB
-
only gradual loss of activity after more than 10 min, pH-dependent
EGTA
-
Ca2+ restores; irreversible upon prolonged incubation (liver enzyme); kinetics
EGTA
-
alphagammadelta and gammadelta subunit complexes less sensitive than holoenzyme; Ca2+ restores; effect on kinetic parameters
glucose 6-phosphate
-
Mg2+ protects, phosphorylase b as substrate, mechanism, kinetics; no inhibition with modified phosphorylase b or a tetradecapeptide as substrate
Synthetic peptide PhK13
derived from gamma subunit region, residues 302-326; kinetic; synergistic with PhK5
Synthetic peptide PhK5
derived from gamma subunit region, residues 342-366; kinetic; synergistic with PhK13
Trifluoperazine
-
nonspecific inactivation, at high concentrations, together with EGTA additive effect
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
additional information
-
KPI-2 is inhibited in living cells by addition of nerve growth factor or serum
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose
-
additional information
-
after treatment of differentiated C2C12 muscle myoblasts with apoptosis inducers staurosporine, N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine, doxorubicin, or UV radiation the enzyme alpha-subunit disappears
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
additional information
-
gamma subunit with autoinhibitory domains; regions of the gamma-subunit represented by PhK5 and PhK13 work in concert as regulatory subdomains that transduce Ca2+-induced conformational changes in the delta-subunit to the catalytic gamma-subunit through a pseudosubstrate autoinhibitory mechanism
-
additional information
gamma subunit with autoinhibitory domains; regions of the gamma-subunit represented by PhK5 and PhK13 work in concert as regulatory subdomains that transduce Ca2+-induced conformational changes in the delta-subunit to the catalytic gamma-subunit through a pseudosubstrate autoinhibitory mechanism
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by spermidine, spermine, F-; no inhibition by UDPglucose
-
additional information
-
no inhibition by diethyldithiocarbamic acid, 2,2'-dipyridyl
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose
-
additional information
-
no inhibition by CTP, caffeine, cAMP, cGMP, IMP, glucose 6-phosphate (gammadelta subunit complex); no inhibition by glucose 1-phosphate (gammadelta subunit complex)
-
additional information
-
phosphorylase kinase alpha and beta subunits suppress catalytic activity of gamma subunit in holoenzyme
-
additional information
-
gamma subunit with autoinhibitory domains; inhibition study with modified gamma subunit
-
additional information
-
effect of molecular crowding, osmolytes inhibit complex formation with substrate phosphorylase b
-
additional information
-
FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, in the presence of 1 M trimethylamine-N-oxide, FAD has an inhibitory effect on self-association of phosphorylase kinase
-
additional information
loss of activity through proteolysis only by ficin digestion
-
additional information
-
evaluation of indirubin analogues as phosphorylase kinase inhibitors, structure-activity relationship analysis, docking, overview. The inhibitory effects arises from binding at the kinase domain, i.e. gamma-subunit
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dimethoxyethane
-
activation, 10% v/v, stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
adenosine 3'-phosphate 5'-phosphosulfate
-
activation, can replace ADP to some extent
adenosine 5'-phosphosulfate
-
activation, can replace ADP to some extent
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Ca2+/calmodulin
-
the phosphorylase kinase is activated by both cAMP-dependent protein kinase and Ca2+/calmodulin
-
caspase-3
-
selective in vitro cleavage of the regulatory alpha-subunit increasing the enzyme activity 2fold
-
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
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
-
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
adenosine 3',5'-monophosphate
-
i.e. cAMP, activation of nonactivated enzyme, not alone, only in the presence of Mg2+ or Mn2+
adenosine 3',5'-monophosphate
-
no enhancement or inhibition of this activation by various nucleotides and other compounds, overview
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
Artificial thin filaments
-
activation, made by mixing actin, tropomyosin and troponin complex
-
Artificial thin filaments
-
activation, made by mixing actin, tropomyosin and troponin complex
-
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Calmodulin
-
influences the conformational substrates of the subunits, overview
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
or alphagammadelta subunit complex
-
Catalytic subunit of cAMP-dependent protein kinase
-
and beta
-
Catalytic subunit of cAMP-dependent protein kinase
-
by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation by enhancing vmax selectively for A2 activity
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
chymotrypsin
-
by limited proteolysis of alpha subunit, not gamma or delta subunits
-
glycogen
-
stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
glycogen
significantly stimulates the enzyme PhK. GPb molecules located on the glycogen surface might serve as good connecting molecules between PhK and glycogen and, consequently, promote indirect binding of PhK to the glycogen surface. Under conditions of high ionic strength and high ATP concentration in the body, direct binding of PhK to glycogen is reported to be very weak. The ternary PhK-GPbn-glycogen complex produces active GPa very efficiently compared with PhK, either alone or in the binary complex, i.e. the PhK-GPb complex. The effect is inhibited by gamma-cyclodextrin
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
troponin C
-
presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
troponin C
-
presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
accompanied by loss of absolute requirement for Ca2+, activates holoenzyme and alphagammadelta subunit complex, not gammadelta complex
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits
-
Trypsin
-
vmax enhancement of all three activities of the kinase: A0, A1 and A2
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits or delta subunits
-
Trypsin
-
accompanied by loss of absolute requirement for Ca2+, activates holoenzyme and alphagammadelta subunit complex, not gammadelta complex
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
KIAA1199 enhanced the phosphorylation of glycogen phosphorylase brain form
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
hexadecamer of (alphabetagammadelta)4 with variable degree of activity depending on pH, metal ions, allosteric effectors, covalent modifications, etc.
-
additional information
-
no activation by g adenine, adenosine, 5'-AMP, 2',5'-ADP, 3',5'-ADP, adenosine 2':3'cyclicphosphate 5'-monophosphate, alpha,beta-methylene-ADP, adenosine 2'-phosphate 5'-phosphosulfate, adenosine 5'-diphosphoglucose, adenosine 5'-diphosphoribose, ADP-3'-diphosphate, adenylylimidodiphosphate, diadenosine diphosphate
-
additional information
-
the nonactivated enzyme (i.e. Dephospho-enzyme)
-
additional information
-
no activation by glucose 6-phosphate, UDPglucose, dogfish myosin, actin, tropomyosin, rabbit glycogen synthase
-
additional information
-
no activation of nonactivated enzyme by renin (with or without Ca2+), thrombin (with or without Ca2+), phospholipase D from Clostridium perfringens or phospholipase from Crotalus adamanteus
-
additional information
-
no activation by g poly-aspartic acid, hexametaphosphate, yeast nucleic acid, at pH 6.8
-
additional information
-
no stimulation of autophosphorylation by poly-L-alanine, poly-L-asparagine, putrescine, spermidine or spermine
-
additional information
-
No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate
-
additional information
-
No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
-
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
-
additional information
-
location of an allosteric activation switch in the multisubunit phosphorylase kinase complex, overview
-
additional information
activation of phosphorylase kinase by physiological temperature
-
additional information
-
activation of phosphorylase kinase by physiological temperature
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
no activation by glucose 6-phosphate, UDPglucose, dogfish myosin, actin, tropomyosin, rabbit glycogen synthase
-
additional information
-
No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0093
glycogen phosphorylase b
at pH 8.2 in the presence of calcium
0.018
ATP
-
phosphorylase b, truncated form of phosphorylase kinase gamma subunit
0.2
ATP
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, nonactivated enzyme, pH 8.2
1.2
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
nonactivated enzyme, pH 8.2
3.5
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
activated enzyme, pH 8.2
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
influence on kinetic parameters, glycogen decreases Km-values for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic parameters of catalytically active gamma subunit at pH 6.8 and 8.5
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
kinetic parameters for different enzyme forms
-
additional information
additional information
-
kinetic properties of covalently modified and nonmodified phosphorylase kinase
-
additional information
additional information
-
effect of isolated delta subunit on kinetic parameters of nonactivated holoenzyme and alphagammadelta complex
-
additional information
additional information
-
influence of anti-subunit antibodies
-
additional information
additional information
-
kinetic data of holoenzyme and catalytically active proteolytic fragment
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic properties of subunit complexes at pH 6.8 and 8.5
-
additional information
additional information
-
kinetic parameters for recombinant wild-type gamma subunit and its mutant form
-
additional information
additional information
-
random kinetic mechanism, reaction order can be influenced by the sort of substrate
-
additional information
additional information
-
kinetics of phosphorylase kinase-glycogen complex formation
-
additional information
additional information
the rate of product formation by the basal activity of PhK is not linear
-
additional information
additional information
-
the rate of product formation by the basal activity of PhK is not linear
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
134
glycogen phosphorylase b
at pH 8.2 in the presence of calcium
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00029
6'-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00082
6,5-dichloroindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0002
6,5-dichloroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00233
6,6'-dibromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-5-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00036
6-bromo-5-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-5-nitroindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0012
6-bromo-5-nitroindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.001
6-bromo-5-nitroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-N-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-N-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00033
6-bromoindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00034
6-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00023
6-chloroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00022
6-fluoroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00033
6-iodoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00113
6-methoxindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0007
6-methoxindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00054
6-vinylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00055
6-vinylindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.01
7-bromoindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromoindirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0018
7-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00017
indirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
-
0.00034
indirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.68
additional information
additional information
activity of purified native and recombinant enzymes and subunit subcomplexes at different pH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
8.2
8.5
8.8
additional information
additional information
-
nonactivated kinase activity ratios at pH 6.8/8.2: between 0.01-0.05, activated kinase activity ratio: about 0.6
additional information
-
pH-activity profiles of alphagammadelta and gammadelta subunit complexes
additional information
-
activity ratios pH 6.8/8.2 of nonactivated enzyme: 0.07 (in the presence of 0.05-0.07 M Ca2+) and 0.23 (after calmodulin addition)
additional information
-
activity ratios at pH 6.8/8.2: 0.01-0.02 (phosphorylase kinase a), 0.36 (phosphorylase kinase sa), 0.67 (phosphorylase kinase a')
additional information
-
activated enzyme has a higher pH-optimum than nonactivated enzyme
additional information
-
influence of activation by protein kinase on pH-activity profile
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 7.6
-
about half-maximal activity at pH 6.2 and 7.6, nonactivated enzyme
6.2 - 8
-
progressive increase of activity, about half-maximal activity at pH 7.4
6.2 - 9.3
-
progressive increase of activity from 10% to 100% of maximal activity, with half-maximal activity at pH 7
6.2 - 9.5
-
about half-maximal activity at pH 6.2 and about 70% of maximal activity at pH 9.5
6.5 - 8.5
-
progressive increase of activity, biphasic with dogfish phosphorylase b as substrate: then about half-maximal activity at pH 7.2-7.6 (dogfish activated enzyme)
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
additional information
activity of purified native and recombinant enzymes and subunit subcomplexes at different pH, the latter show higher activity at pH 6.8, while the native enzyme shows higher activity at pH 8.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
40
activation of phosphorylase kinase by physiological temperature
additional information
-
reaction and conformation temperature dependence, overview
30
-
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
the activity at pH 6.8 of nonphosphorylated PhK predictably increases, but between 30°C and 40°C, 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 40°C than at 30°C. The probable underlying mechanism for the dramatic increase in PhK's activity between 30°C and 40°C is an abrupt change in the conformations of the regulatory beta and catalytic gamma subunits between these two temperatures. Activity profiles, overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
10 week old girl with severe hypertrophy of the septal and atrial walls, progressive ventricular wall thickening, girl died at the age of 5 month from aspiration pneumonia, decreased activity of phosphorylase kinase
-
-
brenda
gene PHKG1; the subunits of the muscle isozyme are encoded by different genes
SwissProt
brenda
liver isoform, alpha subunit; patients with XLG I, with a deficiency in phosphorylase kinase activity in peripheral blood cells and liver; and with XLG II, with normal in vitro PHK activity in peripheral blood cells and with variable activity in liver
UniProt
brenda
the subunits of the muscle isozyme are encoded by different genes
SwissProt
brenda
-
492092, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492137, 492138, 492139, 492140, 492141, 492142, 492146, 492149, 492150, 492152, 492154, 661075, 662670, 662844, 663347, 672305, 691329, 702389
-
-
brenda
subunits alpha and beta
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
postmortem tissue, 8fold increase in glycogen concentration and no detectable phosphorylase kinase activity
brenda
additional information
-
-
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492145, 492149, 492152, 492154, 492155, 661075, 662670, 662844, 663335, 663347, 671763, 672305, 677034, 691329, 702389, 740880, 761263, 762340, 762341
brenda
additional information
-
PhK shows a wide tissue distribution, expression of subunits, overview
brenda
additional information
-
isozyme distribution in different tissues
brenda
additional information
-
isozyme distribution in different tissues
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
due to protein-protein interactions in glycogen particles the proteins behave differently from those in cytosol
-
brenda
-
together with other enzymes of glycogen metabolism linked together on glycogen particles
-
brenda
-
together with other enzymes of glycogen metabolism linked together on glycogen particles
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
PhKG1 knockdown reduces human umbilical vein endothelial cell tube formation and migration
malfunction
-
PhKG1a knockdown inhibits angiogenic intersegmental vessels formation
malfunction
KIAA1199 protein silencing by siRNA results in a marked reduction in the phosphorylation of glycogen phosphorylase brain form, PYGB, by PHK
malfunction
-
phosphorylase kinase beta knockdown impairs proliferation of colorectal cancer in vitro and in vivo and induced cell cycle arrest
metabolism
proposed model of glycogen metabolism through the activation of PHK and PYG pathways in cancer cells with or without KIAA1199 overexpression, overview. PYG plays a central role in the mobilization of carbohydrate reserves in a wide variety of organs and tissues
metabolism
the enzyme plays a key role in the cascade system for regulating glycogen metabolism
metabolism
-
the enzyme phosphorylates and activates glycogen phosphorylase in the cascade activation of glycogenolysis
physiological function
-
phosphorylase kinase subunit G1 (PhKG1) is implicated in angiogenesis
physiological function
-
phosphorylase kinase subunit G1 (PhKG1) is implicated in angiogenesis
physiological function
the enzyme regulates glycogenolysis in skeletal muscle
physiological function
-
the phosphorylase kinase enzyme complex regulates glycogenolysis
physiological function
glycogen phosphorylase kinase (PHK) is a serine/threonine-specific protein kinase that phosphorylates a serine residue in glycogen phosphorylase (PYG), triggering the activation of this latter enzyme that catalyzes the phosphorolytic cleavage of the alpha-1,4 glycosidic linkages of glycogen, releasing glucose-1-phosphate as the reaction product. The glycogen phosphorylase kinase beta-subunit (PHKB) interacts with the C-terminal region of KIAA1199 protein, that is associated with cancer cell migration or invasion and a poor prognosis and with non-syndromic hearing loss. KIAA1199 protein also interacts with glycogen phosphorylase brain form (PYGB) under serum-free conditions. The interaction promotes glycogen breakdown and cancer cell survival. KIAA1199 binding protein pull down assay, overview
physiological function
glycogen phosphorylase, EC 2.4.1.1, exists in two interconvertible forms, GPa (phosphorylated form, high activity) and GPb (nonphosphorylated form, low activity). Phosphorylase kinase catalyses the phosphorylation of GPb and plays a key role in the cascade system for regulating glycogen metabolism
physiological function
the enzyme is a Ca2+-dependent regulatory enzymethat catalyzes phosphorylation and activation of glycogen phosphorylase b
physiological function
-
the enzyme plays a key role in the neural and hormonal regulation of glycogenolysis in skeletal muscle
physiological function
-
the over (or high) expression of enzyme subunit PHKB greatly hinders hepatocellular carcinoma cell invasion and increases apoptosis rates. The enzyme subunit PHKB inhibits AKT and STAT3 signaling pathway activation in hepatocellular carcinoma
Show AA Sequence and Transmembrane Helices (2131 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
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
1300000
1330000
134000
-
4 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
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
140000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
145000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
16680
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
18000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, 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
44700
45000
46000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
48000
-
4 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
86000
-
catalytically active gammagamma subunit complex, gel filtration
additional information
125000
-
4 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
125000
-
4 * alpha + 4 * 125000 (beta) + 4 * gamma + 4 * delta, beta-gamma-conjugate 1700000 Da, SDS-PAGE
125200
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
125200
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
125200
-
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
130000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
130000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
138400
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
138400
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
138400
-
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
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)
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)
16700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
16700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
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)
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
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
44700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
44700
-
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
45000
-
2 * 45000, rabbit, catalytically active gammagamma subunit, SDS-PAGE
45000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
additional information
-
amino acid sequence in regulatory domain of gamma subunit
additional information
-
enzyme aggregates to high polymeric forms which arise as artifacts during isolation procedure due to sensitivity to high hydrostatic pressure, e.g. during sucrose density gradient centrifugation at very high angular velocities
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 45000, rabbit, catalytically active gammagamma subunit, SDS-PAGE
hexadecamer
oligomer
tetramer
additional information
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
-
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)
hexadecamer
-
4 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
hexadecamer
-
2 major isozymes in muscle: (alphabetagammadelta)4 and (alpha'betagammadelta)4
hexadecamer
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
hexadecamer
-
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)
hexadecamer
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
hexadecamer
-
2 major isozymes in muscle: (alphabetagammadelta)4 and (alpha'betagammadelta)4
hexadecamer
-
tertiary and secondary structure of PhK measured in presence or absence of Ca2+, conformational changes induced by Ca2+, surface electrostatic properties of solvent accessible charged and polar groups are altered upon the binding of Ca2+ ions, overview
hexadecamer
-
4 * alpha + 4 * 125000 (beta) + 4 * gamma + 4 * delta, beta-gamma-conjugate 1700000 Da, SDS-PAGE
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
hexadecamer
-
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
hexadecamer
-
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
hexadecamer
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
hexadecamer
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
hexadecamer
the beta subunit is helical and forms the 4-bridged core in the (alphabetagammadelta)4 kinase complex. Activity of the catalytic gamma subunit is regulated by allosteric activators targeting the regulatory alpha beta and delta subunits
hexadecamer
(alphabetagammadelta)4 , 4 x 138400, alpha-subunit, + 4 * 125200, beta-subunit, + 4 * 44700, gamma-subunit, + 4 * 16700, delta-subunit, about, mass spectrometry
hexadecamer
-
4 * 138400 + 125200 + 4 * 66700 + 4 * 16700, calculated from amino acid sequence
hexadecamer
-
4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, calculated from amino acid sequence
hexadecamer
-
(alphabetagammadelta)4 , 4 x 138400, alpha-subunit, + 4 * 125200, beta-subunit, + 4 * 44700, gamma-subunit, + 4 * 16700, delta-subunit, about, mass spectrometry
-
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
alpha4beta4gamma4delta4, alpha and beta subunits are regulatory, delta is calmodulin, and the gamma subunit is catalytic
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
tetramer
-
the enzyme forms a (alphabetagammadelta)4 complex, location of an allosteric activation switch in the multisubunit phosphorylase kinase complex, overview
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
-
phosphorylase kinase is a multisubunit protein kinase with molecular weight above 1000000 Da
additional information
-
gamma' subunit is not identical with rabbit skeletal muscle gamma subunit
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
chicken gamma and alpha' subunits compared to that of rabbit red muscle enzyme
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
PHK is an enzyme comprised of four subunits, of which the gamma-subunit possesses enzymatic activity that is tightly regulated by the other three regulatory subunits in response to changes in intracellular Ca2+ concentrations (sensed by the delta-subunit, calmodulin) and cAMP levels that stimulate protein kinase A to phosphorylate the alpha- and beta-subunits (PHKA and PHKB). Upon phosphorylation, these two subunits, which basically inhibit the activity of the gamma-subunit, reduce their function as gamma-inhibitors, resulting in the enzymatic activation of PHK
additional information
-
the enzyme has an open, active conformation and a closed, inactive conformation
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
-
composed of 3 regulatory and 1 catalytic subunit
additional information
-
the delta subunit is firmly bound to holoenzyme whereas delta' subunit (i.e. calmodulin) is bound only in the presence of Ca2+
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
alpha and beta subunits are regulatory subunits controlled by phosphorylation and proteolysis, Ca2+-sensitivity is conferred to delta subunit
additional information
-
the catalytic gamma subunit contains a kinase domain and a calmodulin binding domain
additional information
-
homology with catalytic subunit of cAMP dependent protein kinase
additional information
homology with catalytic subunit of cAMP dependent protein kinase
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
-
calmodulin is identical with the delta subunit
additional information
-
calmodulin is identical with the delta subunit, determination and analysis of enzyme three-dimensional structure with a resolution of 25 A by cryoelectron microscopy
additional information
-
calmodulin is identical with the delta subunit, X-ray light-scattering structure modeling of unactivated enzyme or enzyme after structural changes induced by Ca2+-binding, structure analysis, overview
additional information
-
self-association is induced by Mg2+ and Ca2+, kinetics
additional information
-
conformational substrates of PhK subunit bound or unbound to calmodulin and Ca2+, overview
additional information
Ca2+and Mg2+ions induce the self-association of PhK. Effects of arginine on protein-protein interactions in the enzyme polymer: arginine induces aggregation of Ca2+-free enzyme PhK. But when studying Ca2+, Mg2+-induced aggregation of PhK at 37°C, the protective effect of arginine is demon-strated, disruption of PhK hexadecameric structure occurs under the action of arginine. Although HspB6 and HspB5 suppress aggregation of PhK they do not block the disruption effect of arginine with respect to both forms of PhK (Ca2+-free and Ca2+, Mg2+-bound conformers). Aggregation of PhK induced by 0.5 M Arg is significantly suppressed in the presence of 1 M trimethylamine N-oxide dihydrate (TMAO)
additional information
mass spectrometric analysis of surface-exposed regions in the hexadecameric phosphorylase kinase complex, overview. Phosphorylase kinase is a 1.3 MDa (alphabetagammadelta)4 enzyme complex, in which alphabetagammadelta protomers associate in D2 symmetry to form two large octameric lobes that are interconnected by four bridges. The alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme. Enzyme structure analysis by mass spectrometry, small-angle X-ray scattering, and transmission electron microscopy
additional information
-
mass spectrometric analysis of surface-exposed regions in the hexadecameric phosphorylase kinase complex, overview. Phosphorylase kinase is a 1.3 MDa (alphabetagammadelta)4 enzyme complex, in which alphabetagammadelta protomers associate in D2 symmetry to form two large octameric lobes that are interconnected by four bridges. The alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme. Enzyme structure analysis by mass spectrometry, small-angle X-ray scattering, and transmission electron microscopy
-
additional information
subunit composition of alpha4beta4gamma4delta4, in which the alpha and beta subunits are regulatory, delta is calmodulin, and the gamma subunit is catalytic
additional information
-
the delta subunit is firmly bound to holoenzyme whereas delta' subunit (i.e. calmodulin) is bound only in the presence of Ca2+
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
the delta subunit is identical with calmodulin
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
additional information
phosphoprotein
-
the phosphorylase kinase is activated by cAMP-dependent protein kinase
phosphoprotein
-
autophosphorylation, the site often depends more on structure than on primary sequence
phosphoprotein
-
autophosphorylation results in a 40fold activation of phosphorylase conversion at pH 6.8
phosphoprotein
the phoshorylase kinase i phosphorylated and activated
phosphoprotein
when PhK is phosphorylated, the alpha subunit is cleaved in the same loop regions (656-748 and 967-1015). A new region (627-662) proximal to the former loop is observed. Additionally, two new regions near the C-terminus of alpha appear, as well as a peptide corresponding to residues 1103-1113 and one of residues 1217-1224. Cys1234 is modified only in the phosphorylated complex. The entire C-terminus from residues 1217 to 1237 may be more exposed in the activated conformer
phosphoprotein
-
the enzyme is activated by phosphorylation of its alpha and beta subunits
phosphoprotein
-
the enzyme is activated by phosphorylation of Ser26 on beta subunit by cAMP-dependent protein kinase
phosphoprotein
-
when PhK is phosphorylated, the alpha subunit is cleaved in the same loop regions (656-748 and 967-1015). A new region (627-662) proximal to the former loop is observed. Additionally, two new regions near the C-terminus of alpha appear, as well as a peptide corresponding to residues 1103-1113 and one of residues 1217-1224. Cys1234 is modified only in the phosphorylated complex. The entire C-terminus from residues 1217 to 1237 may be more exposed in the activated conformer
-
phosphoprotein
-
the phoshorylase kinase i phosphorylated and activated
-
phosphoprotein
regulation by de-/phosphorylation performed by cAMP-dependent protein kinase, EC 2.7.11.11
proteolytic modification
-
specific cleavage of caspase-3 at a specific cleavage site within the alpha-subunit in vivo
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
-
the native and the recombinant enzyme performs autophosphorylation of its alpha and beta subunits
additional information
loss of activity through proteolysis only by ficin digestion
additional information
-
loss of activity through proteolysis only by ficin digestion
-
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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
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, i.e. Phkgammatrnc, in the presence of Mg-ATP, X-ray data
-
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D299V
naturally occurring mutation in gene PHKB, encoding subunit beta, missense mutation leads to enzyme deficiency in vivo
DELTA189-190
naturally occurring mutation in XLG II patient, increased activity blood cells
E1125K
naturally occurring mutation in XLG I patient, low activity in blood cells
Q1169X
naturally occurring mutation in XLG I patient, CAG codon is replaced by a TAG stop codon, very low activity in blood cells
Q657K
naturally occurring heterozygous single amino acid replacement in gene PHKB, might not be significant for enzyme deficiency disease, patient shows low enzyme activity
R295H
naturally occurring mutation in XLG I and XLG II patients, very low activity in blood cells and liver
Y770C
naturally occurring heterozygous single amino acid replacement in gene PHKB, might not be significant for enzyme deficiency disease, patient shows low enzyme activity
additional information
additional information
regulatory enzyme of glycogen metabolism, mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit cause autosomal liver glycogenosis. Mutation V106E, G189E and D215N are responsible for autosomal form of Phk deficiency
additional information
-
regulatory enzyme of glycogen metabolism, mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit cause autosomal liver glycogenosis. Mutation V106E, G189E and D215N are responsible for autosomal form of Phk deficiency
additional information
a B2 repeat insertion generates alternate structures of the mouse muscle gamma-phosphorylase kinase gene
additional information
-
a B2 repeat insertion generates alternate structures of the mouse muscle gamma-phosphorylase kinase gene
additional information
-
construction of PhKbeta subunit deletion mutants
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h stable
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
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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 0°C dissociates the 23 S enzyme to active 7.5 S and 14 S subunits, with LiBr it produces 5 S subunits
-
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
-
Rapid irreversible inactivation during desalting by gel filtration or dialysis at ionic strength below 0.1, sucrose, glycerol, salts, SH-compounds or reagents does not stabilize, glycogen, glucose, glucose 1-phosphate, glucose 6-phosphate, mono-, di- and trinucleotides or divalent metal ions and protease inhibitors do not protect
-
unstable in dilute solutions
With strong tendency to aggregate, unstable in high concentrations of ammonium sulfate for prolonged periods
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, 3 mg dogfish enzyme/ml, in 0.1 M glycerophosphate, 2 mM EDTA, pH 7, 0.3 M NaCl or in 0.1 M glycerophosphate, 2 mM EDTA, 10% sucrose, 1 mM ATP, pH 7, 1 mM DTT, about 50% loss of activity within 1 week
-
-15°C, partially purified dogfish enzyme, lyophilized, almost indefinitely
-
-20°C, in 0.25 M sucrose, 0.1 M Tris-HCl, 0.5 mM DTT, pH 7.4, 50% glycerol, several weeks
-
-20°C, in 50 mM sodium glycerophosphate, 0.1% v/v 2-mercaptoethanol, pH 7, 2 mM EDTA, 50% v/v glycerol, at least 1 year
-
-70°C, in 20 mM triethanolamine-HCl, pH 7.5, 20% v/v glycerol, 1 mM DTT, 0.02% NaN3, stable
-
-80°C in 50 mM HEPES buffer (pH 6.8, 10% w/v sucrose, and 0.2 mM EDTA)
-
0-4°C, in 5-20% glycerol, 70% loss of activity within 5 h, more rapid inactivation in 5-20% sucrose
-
0°C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 30% loss of activity within 4 h
-
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
-
20°C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h
-
Frozen in liquid N2, in 50 mM beta-glycerophosphate, pH 7, 2 mM EDTA, 1 mM DTT, 10% sucrose, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic subunit (i.e. gamma subunit, from holoenzyme by dissociation)
-
heart
native enzyme from skeletal muscle by anion exchange chromatography to homogeneity
-
native enzyme from skeletal muscle, recombinant enzyme subunit subcomplexes from Sf9 insect cells
-
partial
recombinant c-Myc-/His6-tagged full-length KPI-2 from Sf9 cells by nickel affinity and ion exchange chromatography, and gel filtration
-
recombinant holoenzyme and enzyme subunit subcomplexes from Sf9 insect cells
to near homogeneity
-
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
DNA sequence determination and structural analysis, genetic organization, the subunits of the muscle isozyme are encoded by different genes, subunit alpha is encoded by gene PHKA1, genes PHKA1, PHKB1, PHKG1, CALM1, CALM2, and CALM3 are involved, relation to several pseudogenes
DNA sequence determination and structural analysis, genetic organization, the subunits of the muscle isozyme are encoded by different genes, subunit gamma is encoded by gene PHKG1, genes PHKA1, PHKB1, PHKG1, CALM1, CALM2, and CALM3 are involved, relation to several pseudogenes
expressed as a N-terminal GST fusion, expressed in B834 (DE3)pLyS cells at 18°C
-
expression of c-Myc-/His6-tagged full-length KPI-2 and minimal kinase fold, residues 137-407 plus an additional C-terminal segment in HEK-293 cells and in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit
isolation of cDNA clones for the catalytic gamma subunit of mouse muscle phosphorylase kinase
mouse catalytic gamma subunit, Baculovirus-directed expression in Sf9 insect cells
-
PhK isozymes, DNA sequence and genomic localization determination and analysis, genetic organization, the genes encoding the alpha, beta, and gamma subunits of PhK undergo extensive transcriptional processing, e.g. exon 6 of PhKG1 is a 3' composite terminal exon due to the presence of weak polyadenylation and cleavage site in intron 6
-
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, expressed in Escherichia coli
-
subcloning of subunits in Escherichia coli, overexpression of the soluble holoenzyme and of soluble trimeric alphagammadelta and dimeric gammadelta subunit subcomplexes, as well as coexpression with the beta subunit of the rabbit enzyme also resulting in subunit complex formation, in Spodoptera frugiperda Sf9 cells via the baculovirus infection system
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PhKG1 is upregulated in human tumor samples from a range of tumor types. PhKG1 mRNA levels are elevated by more than 2fold in the majority of human tumors tested, no upregulation of PhKG1 is detected in prostate cancer
phosphorylase kinase beta mRNA and protein are overexpressed in colorectal cancer tissue compared to the levels in normal mucosa
-
the expression of subunit PHKB is significantly decreased in hepatocellular carcinoma tissues
-
PhKG1 is upregulated in human tumor samples from a range of tumor types. PhKG1 mRNA levels are elevated by more than 2fold in the majority of human tumors tested, no upregulation of PhKG1 is detected in prostate cancer
-
PhKG1 is upregulated in human tumor samples from a range of tumor types. PhKG1 mRNA levels are elevated by more than 2fold in the majority of human tumors tested, no upregulation of PhKG1 is detected in prostate cancer
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
elevated expression of phosphorylase kinase beta is an independent prognostic factor in patients with colorectal cancer
medicine
-
the low expression of enzyme subunit PHKB can serve as an independent indicator for predicting poor prognosis in hepatocellular carcinoma
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EXTERNAL LINKS (specific for EC-Number 2.7.11.19)
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Release 2023.1 (January 2023)
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