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Information on EC 2.7.11.19 - phosphorylase kinase
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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
- casein
- glycogenosis
- myosin
-
holoenzyme
- autophosphorylation
-
x-linked
- alpha-subunits
- glucagon
- troponin
-
nonactivated
-
gamma-subunits
-
calmodulin-dependent
-
glycogenolytic
-
calmodulin-binding
-
hexadecameric
- phosphopeptide
- inhibitor-1
-
cohen
- mgatp
-
sarcoplasmic
- hepatomegaly
- trifluoperazine
-
bisbeta-aminoethyl
-
delta4
-
phosphorylatable
-
debranching
-
2.4.1.1
-
kinase-deficient
-
seryl
- gizzard
-
amp-independent
-
carlson
-
delta-subunits
-
kinase-catalyzed
- phosvitin
-
phosphatase-2a
-
calmodulin-sepharose
-
3':5'-monophosphate
-
cyclic-amp-dependent
- amylo-1,6-glucosidase
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
dephosphophosphorylase kinase, DphK-gamma, EC 2.7.1.38, glycogen phosphorylase b kinase, Glycogen phosphorylase kinase, GPK, kinase kinase/phosphatase/inhibitor-2, kinase, phosphorylase (phosphorylating), KPI-2 kinase, More, 
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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
PhKG1
Phosphorylase b kinase
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
phosphorylase B kinase gamma catalytic chain, testis/liver isoform
phosphorylase kinase
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
-
-
-
-
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
mechanism
-
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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 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
ATP + 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
-
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
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
491214, 491218, 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
?
-
-
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
?
-
-
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
?
-
-
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 b
ADP + phosphorylated glycogen phosphorylase b
-
-
-
-
?
ATP + protein
ATP + 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 + 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
?
-
-
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
?
-
-
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
?
-
-
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
-
activation; can partially replace ATP in the activation of nonactivated enzyme
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ATP
-
-
490801, 661075, 662670, 662844, 663335, 663347, 672305, 675419, 677024, 677034, 702389, 706785, 740075, 740638, 740880
ATP
-
activation of nonactivated enzyme by phosphorylation of subunits A and B, not C
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; in the presence of Ca2+: 1 mol extrinsic calmodulin per mol alphabetagammadelta rabbit enzyme; no activation of bovine red skeletal muscle or rabbit cardiac enzymes; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit; in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation; requirement
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit; in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation; requirement
Calmodulin
-
activation of nonactivated enzyme and alphagammadelta subunit complex; calmodulin containing enzyme i.e. tightly bound delta subunit; interacts with alpha subunit; requirement
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit; calmodulin containing enzyme in the absence of Ca2+; requirement; tightly bound molecule interacts with additional calmodulin in the presence of Ca2+
Calmodulin
-
additional activation; no activation of phosphorylated or proteolytically modified enzyme by delta'-subunit
Calmodulin
-
activation of recombinant gamma subunit at pH 6.8, slightly at pH 8.2; additional activation
Calmodulin
-
mediates Ca2+-sensitivity of the enzyme, calmodulin is identical with the delta-subunit
Calmodulin
encoded by 3 different genes CALM1-3; encoded by 3 different genes CALM1-3
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+
-
allosteric mechanism; 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; required for activity and activation; requirement; synergism with Mg2+
Ca2+
-
allosteric mechanism; 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; required for activity and activation; requirement; synergism with Mg2+
Ca2+
-
allosteric mechanism; 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; required for activity and activation; requirement; synergism with Mg2+
Ca2+
-
Ca2+-sensitivity of the enzyme is mediated by the delta-subunit which is identical with calmodulin
Ca2+
-
allosteric mechanism; 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; required for activity and activation; requirement; synergism with Mg2+
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+
-
-
Ca2+
-
allosteric mechanism; 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; required for activity and activation; synergism with Mg2+
Ca2+
-
required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme
Ca2+
-
stabilization, no absolute requirement for catalytic subunit gamma2
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction; requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
-
Ca2+-independent activity: A0; required for activity and activation; stimulates autophosphorylation in micromolar range at pH 6.8, inhibits at millimolar range
Ca2+
-
stimulates phosphorylase b binding to enzyme, but to a considerable lesser extent than Mg2+
Ca2+
-
dependent on, induces enzyme self-association and increases interaction with glycogen
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+
-
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 substates 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+
-
allosteric mechanism; 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; required for activity and activation; synergism with Mg2+
Ca2+
-
required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction; requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
-
allosteric mechanism; 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; required for activity and activation; requirement; synergism with Mg2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
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+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
491214, 491218, 492094, 492096, 492097, 492098, 492099, 492100, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154
Mg2+
-
can replace Mn2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; not; requirement
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
effect of Mg2+ on Ca2+-binding properties of nonactivated enzyme at pH 6.8; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement; synergism with Ca2+
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
10 mM; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement
Mg2+
-
greatly enhances affinity for phosphorylase b; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
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+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity and activation (by autophosphorylation); required for activity phosphorylation by (cAMP-dependent protein kinase); requirement
Mg2+
-
10 mM; free Mg2+ inhibits activated enzyme; free Mg2+ stimulates (nonactivated enzyme); major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mn2+
-
at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+; can substitute for Mg2+; free Mn2+ inhibits; optimal at ATP:Mg ratio of 1:1; requirement
Mn2+
-
activation; stimulates activation by catalytic subunit of cAMP-dependent protein kinase
Mn2+
-
enhances enzyme/phosphorylase b interaction more effectively; requirement
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation; requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
491214, 491218, 492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492114, 492116, 492117, 492118, 492120, 492124, 492125, 492128, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
phosphate
-
alphagammadelta complex undergoes autophosphorylation: up to 4.2 mol phosphate/mol complex incorporated into alpha subunit; gammadelta subunit complex cannot phosphorylate itself but phosphorylates and activates native enzyme, even in the presence of EGTA or protein kinase inhibitor; requirement, phosphate containing enzyme
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation; requirement, phosphate containing enzyme
phosphate
-
20 mol/mol holoenzyme, phosphate content of subunits; requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
additional information
-
Fe2+, Zn2+ or Ni2+; no activation by Cu2+, Cd2+, Sn2+, Al3+
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
additional information
-
Fe2+, Zn2+ or Ni2+; no activation by Cu2+, Cd2+, Sn2+, Al3+
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
-
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+; 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
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
i.e. kinase-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Calmodulin
-
influences the conformational substates of the subunits, overview
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; and beta (not gamma); by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; 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; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; 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; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; 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; at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; or alphagammadelta subunit complex
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation by enhancing vmax selectively for A2 activity; alpha; and beta
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; alpha; and beta
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; and beta; by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; Mn2+ stimulates; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; kinetics
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each
-
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
-
activation of nonactivated enzyme; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-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
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
chymotrypsin
-
by limited proteolysis of alpha subunit, not gamma or delta subunits; proteolytic activation of nonactivated enzyme
-
glycogen
-
activation; 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
heparin
-
activation; stimulates only holoenzyme, not subunit complexes
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
-
activation; can replace extrinsic calmodulin; presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
troponin C
-
activation; can replace extrinsic calmodulin; presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
Trypsin
-
increase of pH 6.8 activity, not pH 8.2 activity; proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme; strong, by limited proteolysis of alpha and beta subunits; strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
proteolytic activation of nonactivated enzyme; strong, by limited proteolysis of alpha and beta subunits; strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
at low concentration; proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-