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2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
2 ATP + phosphorylase b
2 ADP + phosphorylase a
ATP + a protein
ADP + a phosphoprotein
ATP + alphagammadelta subunit complex
ADP + activated alphagammadelta subunit complex
-
autophosphorylation, by incorporation of phosphate into alpha subunit
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
ATP + Ca2+-dependent transport ATPase
?
-
rabbit
-
-
?
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 + glycogen phosphorylase a
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
ATP + glycogen S peptide
ADP + phosphorylated glycogen S peptide
-
synthetic peptide corresponding to residues 5-18 of its convertible region
-
-
?
ATP + glycogen synthase
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
ATP + histone H1
?
-
-
-
-
?
ATP + liver dephosphophosphorylase
?
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 + Lys-Pro-Val-Thr-Arg-Glu-Ile-Ser-Ile-Arg-NH2
?
-
i.e. S-peptide
-
-
?
ATP + melittin
ADP + phosphomelittin
-
-
-
?
ATP + modified phosphorylase b
?
-
modification at AMP-site
-
-
?
ATP + myelin basic protein
?
-
-
-
-
?
ATP + myosin light chain kinase
?
-
rabbit
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
ATP + peptides derived from glycogen synthase
?
-
rabbit, overview
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
ATP + phosphorylase b
ADP + phosphorylated 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
-
-
?
ATP + sarcolemmal Na+,K+ ATPase
?
-
rabbit
-
-
?
ATP + sarcolemmal protein
?
-
-
-
-
?
ATP + sarcoplasmic protein
?
-
-
-
-
?
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
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
ATP + synthetic tetradecapeptide
?
ATP + tetradecapeptide
ADP + phosphorylated tetradecapeptide
-
-
-
-
?
ATP + troponin I
ADP + phosphotroponin I
ATP + troponin T
ADP + phosphotroponin T
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
GTP + phosphorylase b
GDP + phosphorylase a
SDQEKRKQISVRGL + ATP
?
-
artificial substrate
-
-
?
UTP + phosphorylase b
UDP + phosphorylase a
additional information
?
-
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
-
-
-
?
2 ATP + phosphorylase b
2 ADP + phosphorylase a
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
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 + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
-
-
-
-
?
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
-
-
-
-
?
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 + casein
?
-
rabbit
-
-
?
ATP + casein
?
-
kappa-casein
-
-
?
ATP + casein
?
-
very poor substrate
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
?
-
decreases activity of this substrate
-
-
?
ATP + glycogen synthase
?
-
conversion to a glucose 6-phosphate dependent form
-
-
?
ATP + glycogen synthase
?
-
decreases activity of this substrate
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
at high concentration, from yeast
-
-
?
ATP + liver dephosphophosphorylase
?
-
-
-
-
?
ATP + liver dephosphophosphorylase
?
-
-
-
-
?
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
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
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
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
main reaction
-
-
?
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
-
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
-
main reaction
-
-
?
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
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
main reaction
-
-
?
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
-
-
-
?
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
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
main reaction
-
-
?
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
-
r
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
best substrate
-
-
?
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
-
main reaction
-
-
?
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
-
human, rat
-
-
?
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
-
best substrate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
liver (rat)
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
main reaction
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
liver
-
-
?
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
-
yeast
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
main reaction
-
-
?
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
-
main reaction
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
dogfish
-
-
?
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 + phosphorylated phosphorylase b
-
-
-
-
?
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
?
-
overview
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
overview
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
overview
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
overview
-
-
?
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
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
-
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
phosphorylation site
-
-
?
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
-
-
-
?
ATP + troponin T
ADP + phosphotroponin T
-
-
-
?
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
-
-
-
-
?
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
-
-
?
GTP + phosphorylase b
GDP + phosphorylase a
-
not (dogfish)
-
-
?
UTP + phosphorylase b
UDP + phosphorylase a
-
cosubstrate: Mg-UTP complex
-
-
?
UTP + phosphorylase b
UDP + phosphorylase a
-
not (dogfish)
-
-
?
additional information
?
-
-
ITP, and CTP are no substrates
-
-
?
additional information
?
-
-
ITP, and CTP are no substrates
-
-
?
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
?
-
-
phosvitin is no substrate
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
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
?
-
-
involved in the activation of phosphorylase
-
-
?
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
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
creatine phosphate, phosphoenolpyruvate, actin, parvalbumin, protamin, dogfish or rabbit myosin, adenosine 5'-(3-methyltriphosphate), 5'-adenylylimidodiphosphate (dogfish) are no substrates
-
-
?
additional information
?
-
-
ITP, and CTP are no substrates
-
-
?
additional information
?
-
-
ITP, and CTP 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
?
-
-
histone H2B is no substrate
-
-
?
additional information
?
-
-
histone II-A is no substrate
-
-
?
additional information
?
-
-
phosvitin is no substrate
-
-
?
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
?
-
-
histone H2B is no substrate
-
-
?
additional information
?
-
-
histone II-A is no substrate
-
-
?
additional information
?
-
-
phosvitin is no substrate
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
no spontaneous or MnSO4-induced dephosphorylation of activated enzyme
-
-
?
additional information
?
-
-
no substrate is histone V-S
-
-
?
additional information
?
-
key enzyme in glycogen metabolism
-
-
?
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
?
-
-
ITP, and CTP are no substrates
-
-
?
additional information
?
-
-
histone II-A is no substrate
-
-
?
additional information
?
-
-
phosvitin is no substrate
-
-
?
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.
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
2 ATP + phosphorylase b
2 ADP + phosphorylase a
ATP + a protein
ADP + a phosphoprotein
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
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 + glycogen phosphorylase a
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
-
-
-
?
ATP + glycogen synthase
?
ATP + phosphorylase b
ADP + phosphorylase a
ATP + phosphorylase b
ADP + phosphorylated 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
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
additional information
?
-
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
-
-
-
?
2 ATP + phosphorylase b
2 ADP + phosphorylase a
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
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
?
-
decreases activity of this substrate
-
-
?
ATP + glycogen synthase
?
-
conversion to a glucose 6-phosphate dependent form
-
-
?
ATP + glycogen synthase
?
-
decreases activity of this substrate
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
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
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
?
-
involved in glycogenolysis
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
-
?
ATP + phosphorylase b
ADP + 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
?
-
-
involved in the activation of phosphorylase
-
-
?
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
-
-
?
additional information
?
-
key enzyme in glycogen metabolism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(NH4)2SO4
-
activation, 0.05-0.1 M, inhibits above 0.2 M
Cd2+
-
can partially substitue Mg2+
Ba2+
-
-
Ba2+
-
activation, can replace Ca2+ with 60% efficiency
Ba2+
-
activation, can replace Ca2+ with 26% efficiency
Ca2+
required
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+
-
synergism with Mg2+
Ca2+
-
allosteric mechanism
Ca2+
-
required for activity and activation
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+
-
synergism with Mg2+
Ca2+
-
allosteric mechanism
Ca2+
-
required for activity and activation
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+
-
synergism with Mg2+
Ca2+
-
allosteric mechanism
Ca2+
-
required for activity and activation
Ca2+
-
Ca2+-sensitivity of the enzyme is mediated by the delta-subunit which is identical with calmodulin
Ca2+
required, interacts with the delta subunit
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+
-
synergism with Mg2+
Ca2+
-
allosteric mechanism
Ca2+
-
required for activity and activation
Ca2+
-
Ca2+-dependent reaction
Ca2+
-
-
492100, 492104, 492106, 492109, 492120, 492122, 492123, 492124, 492125, 492154, 662844, 675419
Ca2+
-
required for activity
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+
-
synergism with Mg2+
Ca2+
-
stabilization, no absolute requirement for catalytic subunit gamma2
Ca2+
-
12 mol Ca2+ per mol (alphabetagammadelta)4
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction
Ca2+
-
allosteric mechanism
Ca2+
-
Ca2+-independent activity: A0
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+
-
required for activity and activation
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+
-
activates, dependent on, required for binding of calmodulin
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+
-
required for complex formation
Ca2+
-
Ca2+-dependent reaction
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, binds to the delta subunit
Ca2+
-
Ca2+ stimulates enzyme activity
Ca2+
-
activation, 0.0001-0.001 mM, inhibits above 0.001 mM
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+
-
synergism with Mg2+
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction
Ca2+
-
allosteric mechanism
Ca2+
-
requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
-
required for activity and activation
Ca2+
activates, dependent on, required for binding of 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+
-
synergism with Mg2+
Ca2+
-
allosteric mechanism
Ca2+
-
required for activity and activation
Co2+
-
can partially substitue Mg2+
Co2+
-
activation, can replace Ca2+ with 10% efficiency
Fe3+
-
not
Fe3+
-
activation, can replace Ca2+ with 10% efficiency
Li+
-
activation
Li+
-
can replace Ca2+ with 10% efficiency
Mg2+
-
requirement
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
synergism with Ca2+
Mg2+
-
Mg2+ added in excess of ATP concentration stimulates
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+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
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+
-
synergism with Ca2+
Mg2+
-
Mg2+ added in excess of ATP concentration stimulates
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+
-
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+
-
synergism with Ca2+
Mg2+
-
Mg2+ added in excess of ATP concentration stimulates
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+
-
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+
-
synergism with Ca2+
Mg2+
-
Mg2+ added in excess of ATP concentration stimulates
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+
-
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+
-
synergism with Ca2+
Mg2+
-
Mg2+ added in excess of ATP concentration stimulates
Mg2+
-
greatly enhances affinity for phosphorylase b
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+
major role of Mg2+: cosubstrate in Mg2+-ATP complex
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+
-
required for complex formation and activity
Mg2+
-
induces association
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+
-
Mg2+ stimulates enzyme activity
Mg2+
-
required in form of Mg2+
Mg2+
-
free Mg2+ inhibits activated enzyme
Mg2+
-
free Mg2+ stimulates (nonactivated enzyme)
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
synergism with Ca2+
Mg2+
-
Mg2+ added in excess of ATP concentration stimulates
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+
-
required for activity and activation (by autophosphorylation)
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+
-
synergism with Ca2+
Mg2+
-
Mg2+ added in excess of ATP concentration stimulates
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)
Mn2+
-
requirement
Mn2+
-
can substitute for Mg2+ (less effective)
Mn2+
-
can partially substitue Mg2+
Mn2+
-
can substitute for Mg2+
Mn2+
-
stimulates activation by catalytic subunit of cAMP-dependent protein kinase
Mn2+
-
can replace Ca2+ with 15% efficiency
Mn2+
-
can substitute for Ca2+
Mn2+
-
free Mn2+ inhibits
Mn2+
-
at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+
Mn2+
-
enhances enzyme/phosphorylase b interaction more effectively
Mn2+
-
optimal at ATP:Mg ratio of 1:1
Mn2+
-
can replace Ca2+ with 15% efficiency
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
nonactivated enzyme is activated by phosphorylation
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
nonactivated enzyme is activated by phosphorylation
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
nonactivated enzyme is activated by phosphorylation
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
nonactivated enzyme is activated by phosphorylation
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
-
20 mol/mol holoenzyme, phosphate content of subunits
phosphate
requirement, phosphate containing enzyme
phosphate
requirement, phosphate containing enzyme
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
-
nonactivated enzyme is activated by phosphorylation
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
-
nonactivated enzyme is activated by phosphorylation
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
nonactivated enzyme is activated by phosphorylation
Sr2+
-
activation, can replace Ca2+ with 60% efficiency
Sr2+
-
activation, can replace Ca2+ with 45% efficiency
Sr2+
-
activation, can replace Ca2+ with 45% efficiency
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
-
no activation by Cu2+, Cd2+, Sn2+, Al3+
additional information
-
Fe2+, Zn2+ or Ni2+
additional information
-
Fe2+, Zn2+ or Ni2+
additional information
Ca2+ and Mg2+ induce self-aggregation of PhK at 37°C
additional information
-
no activation by Cu2+, Cd2+, Sn2+, Al3+
additional information
-
Fe2+, Zn2+ or Ni2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(D)-Arg-(D)-Leu-(D)-Ser-(D)-Leu
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
(D)-Leu-(D)-Ser-(D)-Leu-(D)-Arg
-
-
(D)-Leu-(D)-Ser-(D)-Tyr-(D)-Arg-(D)-Arg-(D)-Tyr-(D)-Ser-(D)-Leu
-
-
(NH4)2SO4
-
above 0.2 M, stimulates at 0.05-0.1 M
1,2-dimethoxyethane
-
above 10% v/v, stimulates below
5'-adenylylimidodiphosphate
-
substrate-directed dead end inhibitor
6'-bromoindirubin-3'-oxime
-
-
6,5-dichloroindirubin
-
-
6,5-dichloroindirubin-3'-acetoxime
-
-
6,5-dichloroindirubin-3'-oxime
-
-
6,6'-dibromoindirubin-3'-oxime
-
-
6-bromo-5-methylindirubin
-
-
6-bromo-5-methylindirubin-3'-acetoxime
-
-
6-bromo-5-nitroindirubin
-
-
6-bromo-5-nitroindirubin-3'-acetoxime
-
-
6-bromo-5-nitroindirubin-3'-oxime
-
-
6-bromo-N-methylindirubin
-
-
6-bromo-N-methylindirubin-3'-acetoxime
-
-
6-bromoindirubin-3'-acetoxime
-
-
6-bromoindirubin-3'-oxime
-
-
6-chloroindirubin-3'-oxime
-
-
6-fluoroindirubin-3'-oxime
-
-
6-iodoindirubin-3'-oxime
-
-
6-methoxindirubin-3'-acetoxime
-
-
6-methoxindirubin-3'-oxime
-
-
6-vinylindirubin-3'-acetoxime
-
-
6-vinylindirubin-3'-oxime
-
-
7-bromo-N-methylindirubin
-
-
7-bromo-N-methylindirubin-3'-acetoxime
-
-
7-bromo-N-methylindirubin-3'-methoxime
-
-
7-bromo-N-methylindirubin-3'-oxime
-
-
7-bromoindirubin-3'-acetoxime
-
-
7-bromoindirubin-3'-methoxime
-
-
7-bromoindirubin-3'-oxime
-
-
actin
-
inhibits activation of subunit gamma-troponin C or subunit gamma-calmodulin complexes
Antibodies to delta subunit of phosphorylase kinase
-
-
-
Antibodies to rabbit phosphorylase kinase
-
rabbit
-
Antibodies to rat testis calmodulin
-
calmodulin or troponin (the latter at high concentrations) reverses
-
Arg-Lys-Gln-Ile-Thr-Val-Arg
-
synthetic peptides as substrate
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Ca2+
-
inhibition in millimolar, activation in micromolar range
Calcineurin
-
i.e. calmodulin-binding protein, blocks activation by calmodulin
-
Calmodulin
-
inhibits cAMP-dependent protein kinase mediated activation of phosphorylase kinase, kinetics
FAD
-
FAD at high concentrations completely inhibits the second stage of enzyme binding to glycogen particles containing glycogen phosphorylase b, the inhibitory effect of FAD is not complete and reaches a maximal value at FAD concentrations around 0.03 mM
glucose
-
less effective than glucose 6-phosphate, pH 8.2
glyceraldehyde-3-phosphate dehydrogenase
-
heparin
-
depending on pH it inhibits or activates nonactivated enzyme
Hexametaphosphate
-
pH 8.2
Histone VIIS
-
gammadelta subunit complex
-
Ile-Ser-Val-Arg-Gly
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
indirubin-3'-acetoxime
-
-
-
indirubin-3'-methoxime
-
-
indirubin-3'-oxime
-
phosphorylase kinase ATP-binding site inhibitor
K252a
-
microbial broth product, highly selective
KT5720
-
phosphorylase kinase ATP-binding site inhibitor
LLRDPYALRSVRHLIDNCAFRL
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 336-357
Lys-Pro-Val-Thr-Arg-Glu-Ile-Val-Ile-Arg-NH2
-
i.e. V-peptide
Melittin
-
model calmodulin-binding peptide, mechanism, kinetic, phosphorylase b as substrate
MgADP-
-
product inhibition
Monospecific antibodies against alpha, beta and gamma subunits
-
mechanism, kinetic, anti-beta subunit reverses inhibition by anti-alpha at pH 6.8
-
phosphorylase b
-
high concentration
Phosphotetradecapeptide
-
product inhibition
-
poly-L-lysine
-
strong, activated and nonactivated enzyme, stimulates autophosphorylation
proline
-
inhibits enzyme self-association and interaction with glycogen and phosphorylase b
quercetin
-
ATP does not reverse
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
UTP
-
weak, gammadelta subunit complex
VIRDPYALPPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 333-354
VIRDPYALRPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 332-353
ADP
-
gammadelta subunit complex
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
ATP
-
free ATP, reversible
DTNB
-
-
DTNB
-
only gradual loss of activity after more than 10 min, pH-dependent
EDTA
-
Ca2+ restores; less effective than EGTA
EDTA
-
Ca2+ and Mg2+ partially protect
EDTA
complete inhibition at 50 mM
EGTA
-
Ca2+ restores
EGTA
-
Ca2+ restores; strong
EGTA
-
nonactivated enzyme, more effective than EDTA; strong
EGTA
-
Ca2+ restores; irreversible upon prolonged incubation (liver enzyme); kinetics
EGTA
-
Ca2+ restores; strong
EGTA
-
Ca2+ and Mg2+ partially protect
EGTA
-
alphagammadelta and gammadelta subunit complexes less sensitive than holoenzyme; Ca2+ restores; effect on kinetic parameters
EGTA
-
together with trifluoperazime additive effect
EGTA
-
influence on helical structure
EGTA
-
autophosphorylation
EGTA
-
addition of EGTA reverses Ca2+ induced association
EGTA
-
Ca2+ restores; strong
glucose 6-phosphate
-
-
glucose 6-phosphate
-
pH 8.2
glucose 6-phosphate
-
Mg2+ protects, phosphorylase b as substrate, mechanism, kinetics; no inhibition with modified phosphorylase b or a tetradecapeptide as substrate
glucose 6-phosphate
-
not (gammadelta subunit complex)
glyceraldehyde-3-phosphate dehydrogenase
-
-
-
glyceraldehyde-3-phosphate dehydrogenase
-
-
-
GTP
-
weak, with ATP as substrate
GTP
-
gammadelta subunit complex
indirubin
-
phosphorylase kinase ATP-binding site inhibitor
ITP
-
weak, with ATP as substrate
ITP
-
not (gammadelta subunit complex)
KCl
-
-
Mg2+
-
in excess of ATP; nonactivated and activated enzyme
Mg2+
-
in excess of ATP; nonactivated and activated enzyme
Mg2+
-
free Mg2+, only activated enzyme, reversible
Mn2+
-
free Mn2+
NaCl
-
0.1 M
NaCl
-
100 mM NaCl suppresses effect of Ca2+ and Mg2+
NH4Cl
-
inhibits A1 and A2 activities by lowering of vmax, not A0
Phenothiazin
-
blocks activation by extrinsic calmodulin
Phenothiazin
-
blocks activation by extrinsic calmodulin
Phenothiazin
-
blocks activation by extrinsic calmodulin
Phenothiazin
-
blocks activation by extrinsic calmodulin
Phenothiazin
-
blocks activation by extrinsic calmodulin
Phenothiazin
-
blocks activation by extrinsic calmodulin
Phenothiazin
-
blocks activation by extrinsic calmodulin
Polyaspartic acid
-
pH 8.2
Polyaspartic acid
-
pH 8.2
Polyaspartic acid
-
pH 8.2
Polyaspartic acid
-
pH 8.2
protamine
-
pH 8.2
Protein phosphatase
-
rabbit (not dogfish) kinase
-
Protein phosphatase
-
type I, reverses autoactivation
-
staurosporine
-
-
staurosporine
-
phosphorylase kinase ATP-binding site inhibitor
Synthetic peptide PhK13
derived from gamma subunit region, residues 302-326; kinetic; synergistic with PhK5
Synthetic peptide PhK13
-
calmodulin reverses; kinetic
Synthetic peptide PhK5
derived from gamma subunit region, residues 342-366; kinetic; synergistic with PhK13
Synthetic peptide PhK5
-
calmodulin reverses; kinetic
Trifluoperazine
-
nonspecific inactivation, at high concentrations, together with EGTA additive effect
Trifluoperazine
-
prevents activation by troponin C
additional information
-
-
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose
-
additional information
-
-
-
additional information
-
-
-
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
-
autoregulation by a pseudosubstrate mechanism, overview
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
additional information
-
-
-
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 troponin (rabbit)
-
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
-
no inhibition by cAMP-binding protein
-
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
-
-
-
additional information
-
-
-
additional information
-
no inhibition by cAMP-binding protein
-
additional information
-
-
-
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.
1,2-dimethoxyethane
-
activation, 10% v/v, stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
adenosine 3',5'-monophosphate
adenosine 3'-phosphate 5'-phosphosulfate
-
activation, can replace ADP to some extent
adenosine 5'-phosphosulfate
-
activation, can replace ADP to some extent
Artificial thin filaments
-
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Ca2+-dependent protease
-
Ca2+/calmodulin
-
the phosphorylase kinase is activated by both cAMP-dependent protein kinase and Ca2+/calmodulin
-
caspase-3
-
selective in vitro cleavage of the regulatory alpha-subunit increasing the enzyme activity 2fold
-
Catalytic subunit of cAMP-dependent protein kinase
-
Catalytic subunit of cGMP-dependent protein kinase
-
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
-
-
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
-
cAMP mediated activation
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
-
cAMP mediated activation
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
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
i.e. kinase-activating factor
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir
-
Ca2+-dependent protease
-
or Ca2+-activating factor
-
Calmodulin
-
-
Calmodulin
-
influences the conformational substrates of the subunits, overview
casein protein kinase
-
activation of nonactivated enzyme
-
casein protein kinase
-
activation of nonactivated enzyme
-
casein protein kinase
-
activation of nonactivated enzyme
-
casein protein kinase
-
activation of nonactivated enzyme
-
casein protein kinase
-
activation of nonactivated enzyme
-
casein protein kinase
-
activation of nonactivated enzyme
-
casein 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
-
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
-
and beta (not gamma)
-
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
-
not
-
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
-
alpha
-
Catalytic subunit of cAMP-dependent protein kinase
-
by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
Mn2+ stimulates
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation by enhancing vmax selectively for A2 activity
-
Catalytic subunit of cAMP-dependent protein kinase
-
kinetics
-
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
-
not
-
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
-
not
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
not
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
chymotrypsin
-
by limited proteolysis of alpha subunit, not gamma or delta subunits
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
glycogen
-
activation
glycogen
-
allosteric effector, mechanism
glycogen
-
effect on nonactivated and activated enzyme
glycogen
-
allosteric effector, mechanism
glycogen
-
allosteric effector, mechanism
glycogen
-
allosteric effector, mechanism
glycogen
-
allosteric effector, mechanism
glycogen
-
increases apparent affinity for phosphorylase b
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
glycogen
-
allosteric effector, mechanism
glycogen
-
allosteric effector, mechanism
glycogen
-
no significant effect on dogfish enzyme
heparin
-
activation
heparin
-
stimulates only holoenzyme, not subunit complexes
papain
-
proteolytic activation of nonactivated enzyme
-
papain
-
proteolytic activation of nonactivated enzyme
-
papain
-
proteolytic activation of nonactivated enzyme
-
papain
-
proteolytic activation of nonactivated enzyme
-
papain
-
proteolytic activation of nonactivated enzyme
-
papain
-
proteolytic activation of nonactivated enzyme
-
papain
-
proteolytic activation of nonactivated enzyme
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
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
-
not (liver enzyme)
-
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
-
troponin C
-
activation
-
troponin C
-
activation
-
troponin C
-
activation
-
troponin C
-
activation
-
troponin C
-
presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
troponin C
-
can replace extrinsic calmodulin
-
troponin C
-
activation
-
troponin C
-
presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
troponin C
-
can replace extrinsic calmodulin
-
troponin C
-
activation
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
increase of pH 6.8 activity, not pH 8.2 activity
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits
-
Trypsin
-
at low concentration
-
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
-
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
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits
-
additional information
-
autophosphorylation
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
the nonactivated enzyme (i.e. Dephospho-enzyme)
-
additional information
-
allosteric effectors, overview
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
the nonactivated enzyme (i.e. Dephospho-enzyme)
-
additional information
-
allosteric effectors, overview
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
the nonactivated enzyme (i.e. Dephospho-enzyme)
-
additional information
-
no autoactivation
-
additional information
-
allosteric effectors, overview
-
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
-
activation segment structure
-
additional information
-
autoregulation by a pseudosubstrate mechanism, overview
-
additional information
-
autophosphorylation
-
additional information
-
autophosphorylation
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
the nonactivated enzyme (i.e. Dephospho-enzyme)
-
additional information
-
allosteric effectors, overview
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation
-
additional information
-
autophosphorylation
-
additional information
-
autophosphorylation
-
additional information
-
autophosphorylation
-
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
-
phosphorylation by protein kinases
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
phosphorylation by protein kinases
-
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
-
allosteric effectors, overview
-
additional information
-
no activation by parvalbumin
-
additional information
-
no activation by parvalbumin
-
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
-
effect of molecular crowding
-
additional information
-
location of an allosteric activation switch in the multisubunit phosphorylase kinase complex, overview
-
additional information
-
trimethylamin N-oxide induces association
-
additional information
activation of phosphorylase kinase by physiological temperature
-
additional information
-
activation of phosphorylase kinase by physiological temperature
-
additional information
-
autophosphorylation
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
the nonactivated enzyme (i.e. Dephospho-enzyme)
-
additional information
-
allosteric effectors, overview
-
additional information
-
no activation by parvalbumin
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation
-
additional information
-
autophosphorylation
-
additional information
-
phosphorylation by protein kinases
-
additional information
-
phosphorylation by protein kinases
-
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 by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate
-
additional information
-
allosteric effectors, overview
-
additional information
-
no activation by parvalbumin
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
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0.0093
glycogen phosphorylase b
at pH 8.2 in the presence of calcium
0.9 - 1
Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
pH 8.2
0.002 - 0.37
phosphorylase b
2
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
-
activated enzyme, pH 8.2
1.2 - 3.5
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
0.3085 - 0.47
tetradecapeptide
additional information
additional information
-
0.018
ATP
-
-
0.018
ATP
-
phosphorylase b, truncated form of phosphorylase kinase gamma subunit
0.025
ATP
-
proteolytic fragment of phosphorylase kinase
0.03 - 0.037
ATP
-
pH 8.5
0.03 - 0.037
ATP
-
pH 8.5
0.03 - 0.037
ATP
-
pH 8.5
0.03 - 0.037
ATP
-
pH 8.5
0.03 - 0.037
ATP
-
pH 8.5
0.03 - 0.037
ATP
-
pH 8.5
0.03 - 0.037
ATP
-
pH 8.5
0.03 - 0.037
ATP
-
phosphorylase b
0.03 - 0.037
ATP
-
phosphorylase b
0.03 - 0.037
ATP
-
phosphorylase b
0.03 - 0.037
ATP
-
phosphorylase b
0.03 - 0.037
ATP
-
phosphorylase b
0.03 - 0.037
ATP
-
phosphorylase b
0.03 - 0.037
ATP
-
phosphorylase b
0.03 - 0.037
ATP
-
activated enzyme, pH 7.5
0.03 - 0.037
ATP
-
activated enzyme, pH 7.5
0.03 - 0.037
ATP
-
activated enzyme, pH 7.5
0.03 - 0.037
ATP
-
activated enzyme, pH 7.5
0.03 - 0.037
ATP
-
activated enzyme, pH 7.5
0.03 - 0.037
ATP
-
activated enzyme, pH 7.5
0.03 - 0.037
ATP
-
activated enzyme, pH 7.5
0.03 - 0.037
ATP
-
recombinant gamma subunit, pH 8.2
0.042
ATP
at pH 8.2 in the presence of calcium
0.14 - 0.22
ATP
-
at different phosphorylase b concentrations
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
0.22
ATP
-
S-peptide, activated enzyme, pH 6.8
0.22
ATP
-
pH 8.2, nonactivated enzyme
0.24
ATP
-
nonactivated enzyme, pH 7.5
0.38
ATP
-
activated enzyme, pH 7.5
0.5
ATP
-
pH 8.2, alphagammadelta subunit complex
0.95
ATP
-
pH 8.2, gammadelta subunit complex
0.017 - 0.027
MgATP2-
-
autophosphorylation
0.07
MgATP2-
-
activated rabbit skeletal muscle enzyme, pH 8.2
0.07
MgATP2-
-
activated rabbit skeletal muscle enzyme, pH 8.2
0.07
MgATP2-
-
ATP (+ melittin)
0.08
MgATP2-
-
pH 8.2, gamma subunit or holoenzyme
0.08
MgATP2-
-
ATP (+ tetrapeptide)
0.08
MgATP2-
-
phosphorylase b, activated enzyme
0.08
MgATP2-
-
activated rabbit skeletal muscle enzyme, pH 6
0.08
MgATP2-
-
activated rabbit skeletal muscle enzyme, pH 6
0.098
MgATP2-
-
pH 8.2, gamma subunit or holoenzyme
0.1
MgATP2-
-
nonactivated rabbit skeletal muscle enzyme, pH 6
0.1
MgATP2-
-
dogfish phosphorylase b, pH 8.2, dogfish enzyme
0.2 - 2.3
peptides
-
from phosphorylase b, synthetic
0.7 - 3.5
peptides
-
from glycogen synthase, synthetic
0.002 - 0.0025
phosphorylase b
-
in the presence of glycogen
0.01
phosphorylase b
-
pH 7.5, in the presence of glycogen
0.014
phosphorylase b
-
recombinant gamma subunit, pH 6.8
0.015 - 0.017
phosphorylase b
-
-
0.015 - 0.017
phosphorylase b
-
bovine heart
0.015 - 0.017
phosphorylase b
-
activated enzyme, pH 8.2
0.019 - 0.02
phosphorylase b
-
-
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.019 - 0.02
phosphorylase b
-
pH 7, activated enzyme
0.0276
phosphorylase b
-
holoenzyme
0.04
phosphorylase b
-
before activation, pH 8.2
0.044 - 0.08
phosphorylase b
-
holoenzyme
0.07 - 0.24
phosphorylase b
-
-
0.07 - 0.24
phosphorylase b
-
-
0.07 - 0.24
phosphorylase b
-
-
0.07 - 0.24
phosphorylase b
-
-
0.07 - 0.24
phosphorylase b
-
-
0.07 - 0.24
phosphorylase b
-
-
0.07 - 0.24
phosphorylase b
-
-
0.0824
phosphorylase b
-
gamma subunit
0.084
phosphorylase b
-
from rabbit, pH 8.2, dogfish enzyme
0.094
phosphorylase b
-
pH 8.2, gammadelta subunit complex
0.11
phosphorylase b
-
pH 8.2, alphagammadelta subunit complex
0.12
phosphorylase b
-
pH 7.5
0.125
phosphorylase b
-
before activation, pH 7.5
0.14
phosphorylase b
-
before activation, pH 7.5
0.19
phosphorylase b
-
nonactivated enzyme, pH 8.2
0.25
phosphorylase b
-
pH 7.6
0.25
phosphorylase b
-
pH 8.2, nonactivated enzyme
0.27
phosphorylase b
-
nonactivated enzyme
0.37
phosphorylase b
-
nonactivated enzyme, pH 7
0.21
S-peptide
-
recombinant gamma subunit, pH 8.2
-
0.28
S-peptide
-
recombinant gamma subunit, pH 6.8
-
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
0.3085
tetradecapeptide
-
-
0.47
tetradecapeptide
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
kinetic studies
-
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
-
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
-
influence of Ca2+
-
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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0.00029
6'-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6,5-dichloroindirubin
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
0.05
6-bromoindirubin
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
0.05
6-chloroindirubin
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
0.05
6-fluoroindirubin
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
0.05
6-vinylindirubin
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
0.05
7-bromoindirubin
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
0.05
7-carboxylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00045
glyceraldehyde-3-phosphate dehydrogenase
Oryctolagus cuniculus
-
-
-
0.00021
indirubin 3'-oxime
Oryctolagus cuniculus
-
pH not spefified 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
0.000144
indirubin-3'-oxime
Oryctolagus cuniculus
-
30°C, pH 8.2
0.0000184
KT5720
Oryctolagus cuniculus
-
30°C, pH 8.2
0.00000037
staurosporine
Oryctolagus cuniculus
-
30°C, pH 8.2
0.05
indirubin
Oryctolagus cuniculus
-
30°C, pH 8.2
0.05
indirubin
Oryctolagus cuniculus
-
pH not spefified in the publication, 30°C
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1220000
-
HPLC gel filtration
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
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
1299000
-
calculated from sequence, hexadecameric complex
1305000
-
mass spectrometry, hexadecameric complex
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
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
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
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
205000
-
trypsinized or chymotrypsinized enzyme form, gel filtration
243000
-
alpha/gamma/delta complex, gel filtration
44000
-
2 * 69000 + 2 * 44000, rabbit, proteolytic form, SDS-PAGE
44643
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
44667
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
44669
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
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
69000
-
2 * 69000 + 2 * 44000, rabbit, proteolytic form, SDS-PAGE
86000
-
catalytically active gammagamma subunit complex, gel filtration
125000
-
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
-
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
gel filtration
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
1300000
-
-
1300000
-
rat, gel filtration
1300000
-
rat, gel filtration
1300000
-
calculated from amino acid sequence
1300000
-
dogfish, gel filtration or sedimentation velocity analysis
1300000
-
dogfish, gel filtration or sedimentation velocity analysis
1300000
-
bovine, sucrose density gradient centrifugation
1330000
-
analytical ultracentrifugation
1330000
-
nonactivated enzyme
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
-
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
x * 44673, calculation from amino acid sequence
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
-
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
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amino acid composition
additional information
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amino acid composition
additional information
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amino acid composition
additional information
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amino acid composition
additional information
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amino acid composition
additional information
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mechanism and structure
additional information
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amino acid sequence in regulatory domain of gamma subunit
additional information
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MW of trypsinized enzyme
additional information
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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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dimer
-
2 * 45000, rabbit, catalytically active gammagamma subunit, SDS-PAGE
heterotetramer
x-ray crystallography
?
x * 125000, about, beta-subunit
?
x * 44673, calculation from amino acid sequence
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
-
alpha4beta4gamma4delta4
hexadecamer
-
4 * alpha + 4 * beta + 4 * gamma + 4 * delta
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta
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
-
(alphabetagammadelta)4
hexadecamer
(alphabetagammadelta)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
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
(alphabetagammadelta)4
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
oligomer
-
tetramer
-
2 * 69000 + 2 * 44000, rabbit, proteolytic form, SDS-PAGE
tetramer
-
the enzyme forms a (alphabetagammadelta)4 complex, location of an allosteric activation switch in the multisubunit phosphorylase kinase complex, overview
additional information
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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
-
spatial arrangement of subunits
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
-
spatial arrangement of subunits
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
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gamma' subunit is not identical with rabbit skeletal muscle gamma subunit
additional information
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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
-
spatial arrangement of subunits
additional information
-
chicken gamma and alpha' subunits compared to that of rabbit red muscle enzyme
additional information
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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
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
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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
-
spatial arrangement of subunits
additional information
-
spatial arrangement of subunits
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
-
molecular interaction and subunit structure
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
-
gamma subunit
additional information
gamma subunit
additional information
-
gamma subunit
additional information
-
alpha and beta subunits are regulatory subunits controlled by phosphorylation and proteolysis, Ca2+-sensitivity is conferred to delta subunit
additional information
-
spatial arrangement of subunits
additional information
-
spatial arrangement of subunits
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
-
structure/function relationships of subunits
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
-
partial amino acid composition of subunits
additional information
-
delta subunits
additional information
-
delta subunits
additional information
-
alpha'
additional information
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amino acid composition of alpha
additional information
-
amino acid composition of alpha
additional information
-
amino acid composition of alpha
additional information
-
amino acid sequence of alpha, beta
additional information
-
amino acid sequence of alpha, beta
additional information
-
gamma
additional information
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gamma
additional information
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gamma
additional information
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beta
additional information
-
beta
additional information
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calmodulin is identical with the delta subunit
additional information
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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
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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
-
spatial arrangement of subunits
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
-
spatial arrangement of subunits
additional information
-
spatial arrangement of subunits
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
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