Information on EC 2.7.11.19 - phosphorylase kinase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.7.11.19
-
RECOMMENDED NAME
GeneOntology No.
phosphorylase kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
show the reaction diagram
catalytic aspartate residue
-
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
show the reaction diagram
mechanism
-
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:phosphorylase-b phosphotransferase
Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis---glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b [5]. The gamma subunit of the tetrameric enzyme is the catalytic subunit.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dephosphophosphorylase kinase
-
-
-
-
DphK-gamma
Q9VYV7
-
EC 2.7.1.38
Q171G3
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
P34335
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
-
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
P46019
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
-
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
-
formerly
EC 2.7.1.38
-
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
P12798, P18688
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
A2WRR1
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
Q9W6R1
formerly, transferred to EC 2.7.11.19
EC 2.7.1.38
Q4S8G1
formerly, transferred to EC 2.7.11.19
glycogen phosphorylase b kinase
-
-
Glycogen phosphorylase kinase
-
-
-
-
kinase kinase/phosphatase/inhibitor-2
-
-
kinase, phosphorylase (phosphorylating)
-
-
-
-
PhK
Q171G3
-
PhK
-
-
PhK
P46019
-
PhK
P46020, Q16816
-
PhK
-
-
PhK
P12798, P18688
-
PhK
A2WRR1
-
PhK
Q64649
-
PhK
Q9W6R1
-
Phosphorylase b kinase
-
-
-
-
Phosphorylase b kinase
-
-
Phosphorylase b kinase
-
-
Phosphorylase b kinase
-
-
Phosphorylase b kinase
Q64649
-
phosphorylase B kinase GAMMA catalytic chain
Q9VYV7
-
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
Q16816
-
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
P07934
-
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
P00518
-
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
P13286
-
phosphorylase B kinase gamma catalytic chain, testis/liver
P31325
-
phosphorylase B kinase gamma catalytic chain, testis/liver isoform
P15735
-
phosphorylase B kinase gamma catalytic chain, testis/liver isoform
Q9DB30
-
phosphorylase kinase
-
-
phosphorylase kinase
-
-
phosphorylase kinase-b
-
-
PSK-C3
-
-
-
-
SkM Phk
Q64649
-
transmembrane Ser/Thr kinase KPI-2
-
-
KPI-2 kinase
-
-
additional information
-
formerly EC 2.7.1.38
CAS REGISTRY NUMBER
COMMENTARY
9001-88-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
alpha subunit
UniProt
Manually annotated by BRENDA team
blowfly
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
10 week old girl with severe hypertrophy of the septal and atrial walls, progressive ventricular wall thickening, girl died at the age of 5 month from aspiration pneumonia, decreased activity of phosphorylase kinase
-
-
Manually annotated by BRENDA team
gene PHKG1; the subunits of the muscle isozyme are encoded by different genes
SwissProt
Manually annotated by BRENDA team
liver isoform, alpha subunit; patients with XLG I, with a deficiency in phosphorylase kinase activity in peripheral blood cells and liver; and with XLG II, with normal in vitro PHK activity in peripheral blood cells and with variable activity in liver
UniProt
Manually annotated by BRENDA team
the subunits of the muscle isozyme are encoded by different genes
SwissProt
Manually annotated by BRENDA team
silk moth
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
beta subunit
UniProt
Manually annotated by BRENDA team
isozyme PhKalpha
-
-
Manually annotated by BRENDA team
New Zealand white (female)
-
-
Manually annotated by BRENDA team
New Zealand white (male)
-
-
Manually annotated by BRENDA team
New Zealand white rabbit
-
-
Manually annotated by BRENDA team
New Zealand white rabbits
-
-
Manually annotated by BRENDA team
hypothetical protein
UniProt
Manually annotated by BRENDA team
alpha subunit of the skeletal muscle enzyme
SwissProt
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
commercial baker's yeast
-
-
Manually annotated by BRENDA team
scorpion fish
-
-
Manually annotated by BRENDA team
i.e. Pacific dogfish or Squalus acanthias
-
-
Manually annotated by BRENDA team
alpha subunit
UniProt
Manually annotated by BRENDA team
fragment of the beta subunit
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
the phosphorylase kinase phosphorylates proteins and proteolytic fragments thereof, phosphorylation of multiple residues in the substrate sequence by mammary gland casein kinase
-
-
?
ATP + alphagammadelta subunit complex
ADP + activated alphagammadelta subunit complex
show the reaction diagram
-
autophosphorylation, by incorporation of phosphate into alpha subunit
-
-
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
show the reaction diagram
-
-
-
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
show the reaction diagram
-
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 + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
show the reaction diagram
-
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+-dependent transport ATPase
?
show the reaction diagram
-
rabbit
-
-
-
ATP + casein
?
show the reaction diagram
-
-
-
-
-
ATP + casein
?
show the reaction diagram
-
not
-
-
-
ATP + casein
?
show the reaction diagram
-
not
-
-
-
ATP + casein
?
show the reaction diagram
-
not
-
-
-
ATP + casein
?
show the reaction diagram
-
not
-
-
-
ATP + casein
?
show the reaction diagram
-
very poor substrate
-
-
-
ATP + casein
?
show the reaction diagram
-
rabbit
-
-
-
ATP + casein
?
show the reaction diagram
-
kappa-casein
-
-
-
ATP + glycogen phosphorylase
?
show the reaction diagram
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
regulatory enzyme in the activation cascade of glycogenolysis
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
the enzyme catalyzes the phosphorylation of inactive glycogen phosphorylase b on Ser-14 resulting in the formation of active glycogen phosphorylase a
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
show the reaction diagram
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
show the reaction diagram
-
the hexadecameric enzyme complex that catalyzes the phosphorylation and activation of glycogen phosphorylase b
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
show the reaction diagram
-
PhK catalyzes the Ca2+- and cAMP-dependent glycogen phosphorylase b phosphorylation and activation
-
-
?
ATP + glycogen S peptide
ADP + phosphorylated glycogen S peptide
show the reaction diagram
-
synthetic peptide corresponding to residues 5-18 of its convertible region
-
-
?
ATP + glycogen synthase
?
show the reaction diagram
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + glycogen synthase
?
show the reaction diagram
-
decreases activity of this substrate
-
-
-
ATP + glycogen synthase
?
show the reaction diagram
-
conversion to a glucose 6-phosphate dependent form
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
-
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
-
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
-
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
-
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
rabbit phosphorylase kinase
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
inactivation of skeletal muscle glycogen synthase in the presence or absence of EGTA
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
glycogen synthase a
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
phosphorylatable residue: Ser-7
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
at high concentration, from yeast
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
at high concentration, from rabbit skeletal muscle
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
at high concentration, from rabbit skeletal muscle
-
-
-
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
-
at the same rate as phosphorylase b
-
-
-
ATP + histone H1
?
show the reaction diagram
-
-
-
-
-
ATP + liver dephosphophosphorylase
?
show the reaction diagram
-
-
-
-
-
ATP + liver dephosphophosphorylase
?
show the reaction diagram
-
-
-
-
-
ATP + Lys-Arg-Glu-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Glu-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
?
show the reaction diagram
-
-
-
-
-
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
?
show the reaction diagram
-
-
-
-
-
ATP + Lys-Arg-Lys-Glu-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Glu-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Glu-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Glu-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
show the reaction diagram
-
-
-
-
ATP + Lys-Pro-Val-Thr-Arg-Glu-Ile-Ser-Ile-Arg-NH2
?
show the reaction diagram
-
i.e. S-peptide
-
-
-
ATP + melittin
ADP + phosphomelittin
show the reaction diagram
-
-
-
-
ATP + modified phosphorylase b
?
show the reaction diagram
-
modification at AMP-site
-
-
-
ATP + myelin basic protein
?
show the reaction diagram
-
-
-
-
-
ATP + myosin light chain kinase
?
show the reaction diagram
-
rabbit
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
-
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
-
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
not
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
in the presence of Mg2+ and Ca2+
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
presumably only in vitro
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
presumably only in vitro
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
presumably only in vitro
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
i.e. autophosphorylation and autoactivation
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
phosphorylation sites
-
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
ATP can be replaced by dATP or adenosine 5'-(3-thiotriphosphate) with 50% and 10% efficiency, respectively
-
-
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
-
phosphorylates alpha and beta, not gamma or delta subunits
-
-
-
ATP + peptides derived from glycogen synthase
?
show the reaction diagram
-
rabbit, overview
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
P46020, Q16816
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
r
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
best substrate
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
best substrate
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
yeast
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
liver (rat)
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-ATP complex
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
liver
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
binding studies with immobilized substrate
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
phosphorylase b from heart
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
incorporation of terminal phosphate of ATP into phosphorylase b
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
phosphorylation site: Ser-14
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
phosphorylation site: Ser-14
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
phosphorylation site: Ser-14
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
phosphorylation site: Ser-14
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
phosphorylation site: Ser-14
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
phosphorylation site located 14 residues from amino terminal
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
dogfish
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
rabbit skeletal muscle
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
human, rat
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme interacts with glycogen and phosphorylase b
-
-
?
ATP + phosphorylase b
?
show the reaction diagram
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
stimulates glycogenolysis in skeletal muscle
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
regulates conversion of inactive phosphorylase b into active phosphorylase a, vital process for short term energy supply to the cell, located at an interface between signalling and metabolic pathway
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
involved in glycogen metabolism regulation
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + phosphorylase b
ADP + phosphorylated phosphorylase b
show the reaction diagram
-
-, KPI-2 reacts with Ser residues either preceded by or followed by Pro residues, does not strictly require an adjacent Pro residue
-
-
?
ATP + protein
ATP + phosphoprotein
show the reaction diagram
P31325
in the presence of Ca2+/calmodulin, the isoform PhK-gamma T of the catalytic subunit is able to efficiently phosphorylate glycogen phosphorylase and convert it from an inactive to an active form
-
-
?
ATP + sarcolemmal Na+,K+ ATPase
?
show the reaction diagram
-
rabbit
-
-
-
ATP + sarcolemmal protein
?
show the reaction diagram
-
-
-
-
-
ATP + sarcoplasmic protein
?
show the reaction diagram
-
-
-
-
-
ATP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
?
show the reaction diagram
-
-
-
-
-
ATP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
?
show the reaction diagram
-
i.e. phosphorylase b peptide (5-18)
-
-
-
ATP + synthetic pentadecapeptide
?
show the reaction diagram
-
from amino-terminal of glycogen synthase, i.e. Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ser-Ser-Leu-Pro-Gly-Leu-Glu
-
-
-
ATP + synthetic peptides derived from glycogen synthase
?
show the reaction diagram
-
overview, phosphorylation at the same site as glycogen synthase
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
overview
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
overview
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
overview
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
overview
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
overview
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
overview
-
-
-
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
rabbit
-
-
-
ATP + synthetic tetradecapeptide
?
show the reaction diagram
-
i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
-
-
-
ATP + synthetic tetradecapeptide
?
show the reaction diagram
-
i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu, phosphorylation site: Ser between Ile and Val
-
-
-
ATP + synthetic tetradecapeptide
?
show the reaction diagram
-
substrate for holoenzyme and for catalytic gamma subunit
-
-
-
ATP + synthetic tetradecapeptide
?
show the reaction diagram
-
from amino-terminal of phosphorylase b
-
-
-
ATP + troponin I
ADP + phosphotroponin I
show the reaction diagram
-
-
-
-
-
ATP + troponin I
ADP + phosphotroponin I
show the reaction diagram
-
phosphorylation site
-
-
-
ATP + troponin I
ADP + phosphotroponin I
show the reaction diagram
-
phosphorylation site, phosphorylation site (Thr-residue)
-
-
-
ATP + troponin I
ADP + phosphotroponin I
show the reaction diagram
-
not rabbit or dogfish troponin I
-
-
-
ATP + troponin I
ADP + phosphotroponin I
show the reaction diagram
-
rabbit phosphorylase kinase
-
-
-
ATP + troponin T
ADP + phosphotroponin T
show the reaction diagram
-
-
-
-
ATP + troponin T
ADP + phosphotroponin T
show the reaction diagram
-
-
-
-
ATP + troponin T
ADP + phosphotroponin T
show the reaction diagram
-
not rabbit or dogfish troponin T
-
-
-
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
show the reaction diagram
-
phosphorylation is very slow, binds tightly to enzyme and acts as inhibitor for the phosphorylation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
-
-
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
P12798, P18688
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
Q9W6R1
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
P34335
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
A2WRR1
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
Q4S8G1
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
Q171G3
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
-
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
show the reaction diagram
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
-
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
-
-
?
GTP + phosphorylase b
GDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
GTP + phosphorylase b
GDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
GTP + phosphorylase b
GDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
GTP + phosphorylase b
GDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
GTP + phosphorylase b
GDP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-UTP complex
-
-
-
SDQEKRKQISVRGL + ATP
?
show the reaction diagram
-
artificial substrate
-
-
-
UTP + phosphorylase b
UDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
UTP + phosphorylase b
UDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
UTP + phosphorylase b
UDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
UTP + phosphorylase b
UDP + phosphorylase a
show the reaction diagram
-
not
-
-
-
UTP + phosphorylase b
UDP + phosphorylase a
show the reaction diagram
-
cosubstrate: Mg-UTP complex
-
-
-
UTP + phosphorylase b
UDP + phosphorylase a
show the reaction diagram
-
not (dogfish)
-
-
-
GTP + phosphorylase b
GDP + phosphorylase a
show the reaction diagram
-
not (dogfish)
-
-
-
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
troponin (whole complex) and histone IIAS are no substrates
-
-
-
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
?
-
-
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
?
-
-
histone II-A is no substrate
-
-
-
additional information
?
-
-
phosvitin is no substrate
-
-
-
additional information
?
-
-
phosvitin 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
?
-
-
no substrate is histone V-S
-
-
-
additional information
?
-
P13286
key enzyme in glycogen metabolism
-
-
-
additional information
?
-
Q9VYV7
enzyme is required in early embryonic processes, such as gastrulation and mesoderm formation
-
-
-
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
?
-
P46020, Q16816
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
-
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
?
-
-
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
?
-
-
the enzyme performs autophosphorylation
-
-
-
additional information
?
-
Q64649
the enzyme performs autophosphorylation
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
the enzyme complex regulates glycogenolysis, subunit PhKalpha is autophosphorylated
-
-
-
additional information
?
-
-
involved in the activation of phosphorylase
-
-
-
additional information
?
-
P46019
plays a regulatory role in a cascade of enzymatic reactions controlling glycogen breakdown
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
show the reaction diagram
-
-
-
-
?
ATP + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
show the reaction diagram
-
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 + Ca2+-ATPase
ADP + phospho-Ca2+-ATPase
show the reaction diagram
-
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 + glycogen phosphorylase
?
show the reaction diagram
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
regulatory enzyme in the activation cascade of glycogenolysis
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
show the reaction diagram
-
-
-
-
?
ATP + glycogen synthase
?
show the reaction diagram
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + glycogen synthase
?
show the reaction diagram
-
decreases activity of this substrate
-
-
-
ATP + glycogen synthase
?
show the reaction diagram
-
conversion to a glucose 6-phosphate dependent form
-
-
-
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
P46020, Q16816
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
-
the enzyme interacts with glycogen and phosphorylase b
-
-
?
ATP + phosphorylase b
?
show the reaction diagram
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
stimulates glycogenolysis in skeletal muscle
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
regulates conversion of inactive phosphorylase b into active phosphorylase a, vital process for short term energy supply to the cell, located at an interface between signalling and metabolic pathway
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
involved in glycogen metabolism regulation
-
-
-
ATP + phosphorylase b
?
show the reaction diagram
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
-
ATP + phosphorylase b
ADP + phosphorylated phosphorylase b
show the reaction diagram
-
-
-
-
?
ATP + protein
ATP + phosphoprotein
show the reaction diagram
P31325
in the presence of Ca2+/calmodulin, the isoform PhK-gamma T of the catalytic subunit is able to efficiently phosphorylate glycogen phosphorylase and convert it from an inactive to an active form
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
P12798, P18688
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
Q9W6R1
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
P34335
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
A2WRR1
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
Q4S8G1
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
Q171G3
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
-
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
show the reaction diagram
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
show the reaction diagram
-
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
-
-
?
additional information
?
-
P13286
key enzyme in glycogen metabolism
-
-
-
additional information
?
-
Q9VYV7
enzyme is required in early embryonic processes, such as gastrulation and mesoderm formation
-
-
-
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
?
-
P46020, Q16816
muscle-specific enzyme deficiency causes glycogen storage disease
-
-
-
additional information
?
-
-
protein kinases and protein phosphatases regulate enzyme activities in the cell, overview
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
the enzyme complex regulates glycogenolysis
-
-
-
additional information
?
-
-
involved in the activation of phosphorylase
-
-
-
additional information
?
-
P46019
plays a regulatory role in a cascade of enzymatic reactions controlling glycogen breakdown
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-deoxy-ADP
-
activation, can replace ADP
ADP
-
activation; can partially replace ATP in the activation of nonactivated enzyme
ADP
-
activation; allosteric effector; stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
allosteric effector; kinetics, 8 binding sites per hexadecamer
ATP
-
dependent on
ATP
-
activation of nonactivated enzyme by phosphorylation of subunits A and B, not C
ATP
-
by autophosphorylation or protein kinase phosphorylation; by phosphorylation of subunits alpha, beta not gamma; not alone, only in the presence of Mg2+ or Mn2+
ATP
P46020, Q16816
;
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; in the presence of Ca2+: 1 mol extrinsic calmodulin per mol alphabetagammadelta rabbit enzyme; no activation of bovine red skeletal muscle or rabbit cardiac enzymes; requirement
Calmodulin
-
allosteric effector; calmodulin containing enzyme i.e. tightly bound delta subunit; requirement
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit; in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation; requirement
Calmodulin
-
activation of nonactivated enzyme and alphagammadelta subunit complex; calmodulin containing enzyme i.e. tightly bound delta subunit; interacts with alpha subunit; requirement
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit; calmodulin containing enzyme in the absence of Ca2+; requirement; tightly bound molecule interacts with additional calmodulin in the presence of Ca2+
Calmodulin
-
no additional activation
Calmodulin
-
additional activation; no activation of phosphorylated or proteolytically modified enzyme by delta'-subunit
Calmodulin
-
additional activation
Calmodulin
-
activation of recombinant gamma subunit at pH 6.8, slightly at pH 8.2; additional activation
Calmodulin
-
mediates Ca2+-sensitivity of the enzyme, calmodulin is identical with the delta-subunit
Calmodulin
-
Ca2+-dependent binding, identical with the delta subunit
Calmodulin
Q64649
Ca2+-dependent binding, identical with the delta subunit
Calmodulin
P46020, Q16816
encoded by 3 different genes CALM1-3; encoded by 3 different genes CALM1-3
Calmodulin
-
identical with the delta subunit
Calmodulin
-
identical with the delta subunit
additional information
-
capable of binding FAD, binding of FAD suppresses self association of enzyme
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(NH4)2SO4
-
activation, 0.05-0.1 M, inhibits above 0.2 M
Ba2+
-
activation, can replace Ca2+ with 60% efficiency
Ba2+
-
activation, can replace Ca2+ with 26% efficiency
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+
-
allosteric mechanism; isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity; required for activity and activation; requirement; synergism with Mg2+
Ca2+
-
allosteric mechanism; isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity; required for activity and activation; synergism with Mg2+
Ca2+
-
allosteric mechanism; isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity; required for activity and activation; requirement; synergism with Mg2+
Ca2+
-
12 mol Ca2+ per mol (alphabetagammadelta)4; binding studies
Ca2+
-
required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme
Ca2+
-
requirement
Ca2+
-
stabilization, no absolute requirement for catalytic subunit gamma2
Ca2+
-
requirement
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction; requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
-
synergism with Mg2+
Ca2+
-
activation, 0.0001-0.001 mM, inhibits above 0.001 mM
Ca2+
-
Ca2+-independent activity: A0
Ca2+
-
Ca2+-independent activity: A0; required for activity and activation; stimulates autophosphorylation in micromolar range at pH 6.8, inhibits at millimolar range
Ca2+
-
requirement
Ca2+
-
requirement
Ca2+
-
requirement
Ca2+
-
stimulates phosphorylase b binding to enzyme, but to a considerable lesser extent than Mg2+
Ca2+
-
Ca2+-sensitivity of the enzyme is mediated by the delta-subunit which is identical with calmodulin
Ca2+
-
activates, dependent on, required for binding of calmodulin
Ca2+
Q64649
activates, dependent on, required for binding of calmodulin
Ca2+
-
dependent on, induces enzyme self-association and increases interaction with glycogen
Ca2+
-
activates, binding structure modeling, Ca2+-binding induces structural perturbation of the subunits and promotes redistribution of density throughout the lobes and bridges of the enzyme structure
Ca2+
-
dependent on
Ca2+
-
required for complex formation
Ca2+
-
activates, the four integral delta subunits of the phosphorylase kinase complex are identical to calmodulin and confer Ca2+ sensitivity to the enzyme, but bind independently of Ca2+, Ca2+ influences the conformational substates of the subunits, overview
Ca2+
-
is an obligatory allosteric activator absolutely required by the enzyme, Ca2+ activates PhK by binding to its nondissociable calmodulin subunits, it couples the cascade activation of glycogenolysis with muscle contraction, enzyme surface electrostatic properties of solvent accessible charged and polar groups are altered upon the binding of Ca2+ ions
Ca2+
-
Ca2+-dependent reaction
Ca2+
P46019
required, interacts with the delta subunit
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+
Q171G3
required
Ca2+
P34335
required
Ca2+
P12798, P18688
required; required
Ca2+
A2WRR1
required
Ca2+
Q9W6R1
required
Ca2+
Q4S8G1
required
Ca2+
-
required for activity
Ca2+
-
activated by Ca2+
Calcium
-
dependent on
Cd2+
-
can partially substitue Mg2+
Co2+
-
can partially substitue Mg2+
Co2+
-
activation, can replace Ca2+ with 10% efficiency
Fe3+
-
activation, can replace Ca2+ with 10% efficiency
Li+
-
activation
Li+
-
activation; can replace Ca2+ with 10% efficiency
Mg2+
-
-
Mg2+
-
-
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+
-
can replace Mn2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; not; requirement
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion; enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+; major role of Mg2+: cosubstrate in Mg2+-ATP complex; Mg2+ added in excess of ATP concentration stimulates; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
effect of Mg2+ on Ca2+-binding properties of nonactivated enzyme at pH 6.8; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement; synergism with Ca2+
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement; synergism with Ca2+
Mg2+
-
10 mM; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity and activation (by autophosphorylation); required for activity phosphorylation by (cAMP-dependent protein kinase); requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
10 mM; free Mg2+ inhibits activated enzyme; free Mg2+ stimulates (nonactivated enzyme); major role of Mg2+: cosubstrate in Mg2+-ATP complex; required for activity phosphorylation by (cAMP-dependent protein kinase); requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
greatly enhances affinity for phosphorylase b; major role of Mg2+: cosubstrate in Mg2+-ATP complex; requirement
Mg2+
-
dependent on, induces enzyme self-association and increases interaction with glycogen
Mg2+
-
required for complex formation and activity
Mg2+
-
induces association
Mn2+
-
can partially substitue Mg2+
Mn2+
-
optimal at ATP:Mg ratio of 1:1; requirement
Mn2+
-
requirement
Mn2+
-
can substitute for Mg2+; requirement
Mn2+
-
can substitute for Ca2+; requirement
Mn2+
-
can substitute for Mg2+ (less effective); requirement
Mn2+
-
can replace Ca2+ with 15% efficiency; requirement
Mn2+
-
at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+; can substitute for Mg2+; free Mn2+ inhibits; optimal at ATP:Mg ratio of 1:1; requirement
Mn2+
-
activation; stimulates activation by catalytic subunit of cAMP-dependent protein kinase
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status; nonactivated enzyme is activated by phosphorylation; requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
alphagammadelta complex undergoes autophosphorylation: up to 4.2 mol phosphate/mol complex incorporated into alpha subunit; gammadelta subunit complex cannot phosphorylate itself but phosphorylates and activates native enzyme, even in the presence of EGTA or protein kinase inhibitor; requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation; requirement, phosphate containing enzyme
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation; requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
20 mol/mol holoenzyme, phosphate content of subunits; requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
phosphate
-
requirement, phosphate containing enzyme
Sr2+
-
activation, can replace Ca2+ with 60% efficiency
Sr2+
-
activation, can replace Ca2+ with 45% efficiency
Mn2+
-
enhances enzyme/phosphorylase b interaction more effectively; requirement
additional information
-
Fe2+, Zn2+ or Ni2+
additional information
-
Fe2+, Zn2+ or Ni2+; no activation by Cu2+, Cd2+, Sn2+, Al3+
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
additional information
-
synopsis of activity by Ca2+/Mg2+ and phosphorylation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(D)-Arg-(D)-Leu-(D)-Ser-(D)-Leu
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
(D)-Leu-(D)-Ser-(D)-Leu-(D)-Arg
-
-
(D)-Leu-(D)-Ser-(D)-Tyr-(D)-Arg-(D)-Arg-(D)-Tyr-(D)-Ser-(D)-Leu
-
-
(NH4)2SO4
-
above 0.2 M, stimulates at 0.05-0.1 M
1,2-Dimethoxyethane
-
above 10% v/v, stimulates below
5'-adenylylimidodiphosphate
-
substrate-directed dead end inhibitor
Actin
-
inhibits activation of subunit gamma-troponin C or subunit gamma-calmodulin complexes
-
ADP
-
gammadelta subunit complex
ADP
-
gamma subunit
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
ATP
-
otherwise activating; total inhibition if ATP concentration exceeds that of divalent cation (i.e. Mg2+)
ATP
-
otherwise activating; total inhibition if ATP concentration exceeds that of divalent cation
ATP
-
free ATP, reversible
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
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
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
FAD
-
FAD at high concentrations completely inhibits the second stage of enzyme binding to glycogen particles containing glycogen phosphorylase b, the inhibitory effect of FAD is not complete and reaches a maximal value at FAD concentrations around 0.03 mM
glucose
-
less effective than glucose 6-phosphate, pH 8.2
glucose 6-phosphate
-
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
-
-
-
GTP
-
weak, with ATP as substrate
GTP
-
gammadelta subunit complex
heparin
-
depending on pH it inhibits or activates nonactivated enzyme
Hexametaphosphate
-
pH 8.2
Histone VIIS
-
gammadelta subunit complex
-
Ile-Ser-Val-Arg-Gly
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
ITP
-
weak, with ATP as substrate
ITP
-
not (gammadelta subunit complex)
K252a
-
microbial broth product, highly selective
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
Mg2+
-
in excess of ATP; nonactivated and activated enzyme
Mg2+
-
free Mg2+, only activated enzyme, reversible
Mg2+
-
in excess of ATP
MgADP-
-
product inhibition
Mn2+
-
free Mn2+
NaCl
-
100 mM NaCl suppresses effect of Ca2+ and Mg2+
NH4Cl
-
inhibits A1 and A2 activities by lowering of vmax, not A0
Phosphorylase b
-
high concentration
Phosphotetradecapeptide
-
product inhibition
-
poly-L-lysine
-
strong, activated and nonactivated enzyme, stimulates autophosphorylation
Polyaspartic acid
-
pH 8.2
Polyaspartic acid
-
pH 8.2
Polyaspartic acid
-
pH 8.2
proline
-
inhibits enzyme self-association and interaction with glycogen and phosphorylase b
protamine
-
pH 8.2
Protein phosphatase
-
rabbit (not dogfish) kinase
-
Protein phosphatase
-
type I, reverses autoactivation
-
quercetin
-
ATP does not reverse
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Asp-Val-Arg-Gly-Leu
-
substrate-directed dead end 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
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
Monospecific antibodies against alpha, beta and gamma subunits
-
mechanism, kinetic, anti-beta subunit reverses inhibition by anti-alpha at pH 6.8
-
additional information
-
autoregulation by a pseudosubstrate mechanism, overview
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
additional information
-
gamma subunit with autoinhibitory domains; regions of the gamma-subunit represented by PhK5 and PhK13 work in concert as regulatory subdomains that transduce Ca2+-induced conformational changes in the delta-subunit to the catalytic gamma-subunit through a pseudosubstrate autoinhibitory mechanism
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by spermidine, spermine, F-; no inhibition by UDPglucose
-
additional information
-
no inhibition by diethyldithiocarbamic acid, 2,2'-dipyridyl
-
additional information
-
no inhibition by 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
-
no inhibition by cAMP-binding protein
-
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
-
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
-
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
-
KPI-2 is inhibited in living cells by addition of nerve growth factor or serum
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,2-Dimethoxyethane
-
activation, 10% v/v, stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
adenosine 3',5'-monophosphate
-
i.e. cAMP, activation of nonactivated enzyme, not alone, only in the presence of Mg2+ or Mn2+; no enhancement or inhibition of this activation by various nucleotides and other compounds, overview
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
adenosine 3',5'-monophosphate
-
cAMP mediated activation
adenosine 3',5'-monophosphate
-
-
adenosine 3'-phosphate 5'-phosphosulfate
-
activation, can replace ADP to some extent
adenosine 5'-phosphosulfate
-
activation, can replace ADP to some extent
Artificial thin filaments
-
activation, made by mixing actin, tropomyosin and troponin complex
-
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Ca2+-dependent protease
-
i.e. kinase-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
i.e. kinase-activating factor
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor
-
Ca2+-dependent protease
-
ir; or Ca2+-activating factor; proteolytic activation of nonactivated enzyme
-
Ca2+/calmodulin
-
the phosphorylase kinase is activated by both cAMP-dependent protein kinase and Ca2+/calmodulin
-
Calmodulin
-
influences the conformational substates of the subunits, overview
cAMP
-
dependent on
casein protein kinase
-
activation of nonactivated enzyme
-
caspase-3
-
selective in vitro cleavage of the regulatory alpha-subunit increasing the enzyme activity 2fold
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; and beta (not gamma); by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
not
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; or alphagammadelta subunit complex
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation by enhancing vmax selectively for A2 activity; alpha; and beta
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; alpha; and beta
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; and beta; by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; Mn2+ stimulates; subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme; kinetics
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cGMP-dependent protein kinase
-
not
-
Chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
Chymotrypsin
-
by limited proteolysis of alpha subunit, not gamma or delta subunits; proteolytic activation of nonactivated enzyme
-
Chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
glycogen
-
activation; pH-dependent
glycogen
-
no significant effect on dogfish enzyme
glycogen
-
activation; stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
glycogen
-
activation; effect on nonactivated and activated enzyme
glycogen
-
activation; increases apparent affinity for phosphorylase b
heparin
-
activation; pH-dependent
heparin
-
activation; pH-dependent
heparin
-
activation; pH-dependent
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
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Protein kinases
-
not (liver enzyme)
-
Protein kinases
-
not
-
Trimethylamine N-oxide
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Troponin
-
i.e. complex of troponin C, I and T, activation, as effective as troponin C, forms complex with beta subunit
-
Troponin C
-
activation; can replace extrinsic calmodulin; presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
Troponin C
-
activation; can replace extrinsic calmodulin
-
Trypsin
-
at low concentration; proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme; strong, by limited proteolysis of alpha and beta subunits; strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
accompanied by loss of absolute requirement for Ca2+, activates holoenzyme and alphagammadelta subunit complex, not gammadelta complex; proteolytic activation of nonactivated enzyme; strong, by limited proteolysis of alpha and beta subunits
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme; vmax enhancement of all three activities of the kinase: A0, A1 and A2
-
Trypsin
-
increase of pH 6.8 activity, not pH 8.2 activity; proteolytic activation of nonactivated enzyme
-
Trypsin
-
proteolytic activation of nonactivated enzyme; strong, by limited proteolysis of alpha and beta subunits; strong, by limited proteolysis of alpha and beta subunits (not gamma); strong, by limited proteolysis of alpha and beta subunits or delta subunits
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
heparin
-
activation; stimulates only holoenzyme, not subunit complexes
additional information
-
autoregulation by a pseudosubstrate mechanism, overview
-
additional information
-
activation segment structure
-
additional information
-
no activation by g poly-aspartic acid, hexametaphosphate, yeast nucleic acid, at pH 6.8; No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate; phosphorylation by protein kinases; the nonactivated enzyme is activated either by limited proteolysis
-
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; the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
allosteric effectors, overview; autophosphorylation; phosphorylation by protein kinases; the nonactivated enzyme (i.e. Dephospho-enzyme); the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation; phosphorylation by protein kinases; the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation; phosphorylation by protein kinases; the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
autophosphorylation; phosphorylation by protein kinases; the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
no activation by glucose 6-phosphate, UDPglucose, dogfish myosin, actin, tropomyosin, rabbit glycogen synthase; no activation by parvalbumin; No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate
-
additional information
-
no activation by parvalbumin; the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
phosphorylation by protein kinases; the nonactivated enzyme is activated either by limited proteolysis; three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
-
additional information
-
autophosphorylation; the nonactivated enzyme is activated either by limited proteolysis; three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
no stimulation of autophosphorylation by poly-L-alanine, poly-L-asparagine, putrescine, spermidine or spermine
-
additional information
-
no autoactivation; the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
hexadecamer of (alphabetagammadelta)4 with variable degree of activity depending on pH, metal ions, allosteric effectors, covalent modifications, etc.
-
additional information
-
no activation by g adenine, adenosine, 5'-AMP, 2',5'-ADP, 3',5'-ADP, adenosine 2':3'cyclicphosphate 5'-monophosphate, alpha,beta-methylene-ADP, adenosine 2'-phosphate 5'-phosphosulfate, adenosine 5'-diphosphoglucose, adenosine 5'-diphosphoribose, ADP-3'-diphosphate, adenylylimidodiphosphate, diadenosine diphosphate
-
additional information
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-
activated enzyme, pH 7.5; phosphorylase b
0.03
0.037
ATP
-
activated enzyme, pH 7.5; pH 8.5; phosphorylase b
0.03
0.037
ATP
-
activated enzyme, pH 7.5; pH 8.5; phosphorylase b
0.03
0.037
ATP
-
activated enzyme, pH 7.5; pH 8.5; phosphorylase b
0.03
0.037
ATP
-
phosphorylase b; 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
-
-
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
-
pH 8.2, nonactivated enzyme
0.22
-
ATP
-
bovine heart
0.22
-
ATP
-
S-peptide, activated enzyme, pH 6.8
0.24
-
ATP
-
nonactivated enzyme, pH 7.5
0.38
-
ATP
-
activated enzyme, pH 7.5
0.45
-
ATP
-
-
0.5
-
ATP
-
pH 8.2, alphagammadelta subunit complex
0.95
-
ATP
-
pH 8.2, gammadelta subunit complex
0.0093
-
glycogen phosphorylase b
-
at pH 8.2 in the presence of calcium
-
0.9
1
Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
pH 8.2
0.0098
-
Melittin
-
-
0.017
0.027
MgATP2-
-
autophosphorylation
0.07
-
MgATP2-
-
activated rabbit skeletal muscle enzyme, pH 8.2
0.07
-
MgATP2-
-
ATP (+ melittin)
0.08
-
MgATP2-
-
activated rabbit skeletal muscle enzyme, pH 6
0.08
-
MgATP2-
-
phosphorylase b, activated enzyme
0.08
-
MgATP2-
-
pH 8.2, gamma subunit or holoenzyme
0.08
-
MgATP2-
-
ATP (+ tetrapeptide)
0.098
-
MgATP2-
-
pH 8.2, gamma subunit or holoenzyme
0.1
-
MgATP2-
-
nonactivated rabbit skeletal muscle enzyme, pH 6
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
-
activated enzyme, pH 8.2
0.015
0.017
Phosphorylase b
-
bovine heart
0.015
0.017
Phosphorylase b
-
-
0.019
0.02
Phosphorylase b
-
-
0.0276
-
Phosphorylase b
-
holoenzyme
0.04
-
Phosphorylase b
-
before activation, pH 8.2
0.044
0.08
Phosphorylase b
-
holoenzyme
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
-
2
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
-
activated enzyme, pH 8.2
1.2
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
nonactivated enzyme, pH 8.2
3.5
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
activated enzyme, pH 8.2
0.3085
-
tetradecapeptide
-
-
0.47
-
tetradecapeptide
-
-
0.1
-
MgATP2-
-
dogfish phosphorylase b, pH 8.2, dogfish enzyme
additional information
-
additional information
-
random kinetic mechanism, reaction order can be influenced by the sort of substrate
-
additional information
-
additional information
-
pH-dependence of kinetic parameters
-
additional information
-
additional information
-
effects of holoenzyme dissociation; kinetic data for peptides derived from glycogen synthase; kinetic data for phosphorylase b; kinetic properties, overview; kinetic studies
-
additional information
-
additional information
-
kinetic studies
-
additional information
-
additional information
-
effects of holoenzyme dissociation; kinetic data for peptides derived from glycogen synthase; kinetic data for phosphorylase b; kinetic properties, overview; kinetic studies
-
additional information
-
additional information
-
kinetic data of holoenzyme and catalytically active proteolytic fragment
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetic data for phosphorylase b; kinetic properties, overview; pH-dependence of kinetic parameters
-
additional information
-
additional information
-
kinetic parameters of catalytically active gamma subunit at pH 6.8 and 8.5
-
additional information
-
additional information
-
kinetic properties of subunit complexes at pH 6.8 and 8.5
-
additional information
-
additional information
-
effect of isolated delta subunit on kinetic parameters of nonactivated holoenzyme and alphagammadelta complex
-
additional information
-
additional information
-
kinetic properties of covalently modified and nonmodified phosphorylase kinase
-
additional information
-
additional information
-
influence on kinetic parameters, glycogen decreases Km-values for phosphorylase b
-
additional information
-
additional information
-
kinetic data for peptides derived from glycogen synthase; kinetic data for phosphorylase b
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
influence of anti-subunit antibodies
-
additional information
-
additional information
-
kinetic parameters for different enzyme forms
-
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
-
kinetics of phosphorylase kinase-glycogen complex formation
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
97
-
ATP
-
at pH 8.2 in the presence of calcium
134
-
glycogen phosphorylase b
-
at pH 8.2 in the presence of calcium
-
0.0983
-
Melittin
-
-
57.1
-
Phosphorylase b
-
-
91.4
-
Phosphorylase b
-
nonactivated enzyme
99
-
Phosphorylase b
-
alphagammadelta subunit complex
104
-
Phosphorylase b
-
gammadelta subunit complex
23.6
-
tetradecapeptide
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00045
-
glyceraldehyde-3-phosphate dehydrogenase
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.53
-
-
-
2.8
-
-
dogfish
3.68
-
-
-
8.3
-
-
-
10.9
-
-
truncated form of phosphorylase kinase gamma subunit
16.4
-
-
hind limb
19.6
-
-
brest
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
Q64649
activity of purified native and recombinant enzymes and subunit subcomplexes at different pH
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
nonactivated enzyme
6.8
7
-
assay at
6.8
-
P46020, Q16816
enzyme assay at pH 6.8
6.8
-
-
assay at, substrate glycogen phosphorylase b
7
-
-
liver enzyme
7
-
-
above, activated enzyme
7
-
-
nonactivated enzyme
7.4
-
-
assay at
7.6
-
-
above, nonactivated rabbit enzyme
8.2
-
P46020, Q16816
enzyme assay at pH 8.2
8.3
-
-
assay at, substrate glycogen S peptide
8.5
-
-
-
8.8
-
-
-
9.3
-
-
-
9.5
-
-
muscle enzyme
additional information
-
-
-
additional information
-
-
nonactivated kinase activity ratios at pH 6.8/8.2: between 0.01-0.05, activated kinase activity ratio: about 0.6; pI: 5.77 (nonactivated rabbit enzyme)
additional information
-
-
activity ratios at pH 6.8/8.2: 0.01-0.02 (phosphorylase kinase a), 0.36 (phosphorylase kinase sa), 0.67 (phosphorylase kinase a')
additional information
-
-
-
additional information
-
-
pI: 5.77 (nonactivated rabbit enzyme)
additional information
-
-
-
additional information
-
-
influence of activation by protein kinase on pH-activity profile
additional information
-
-
pH-dependence of partial activities A1 and A2
additional information
-
-
pH-activity profiles of alphagammadelta and gammadelta subunit complexes
additional information
-
-
nonactivated enzyme has only low activity at pH 6.8
additional information
-
-
activity ratios pH 6.8/8.2 of nonactivated enzyme: 0.07 (in the presence of 0.05-0.07 M Ca2+) and 0.23 (after calmodulin addition)
additional information
-
-
pH 6.8/8.2 activity ratios: 0.58
additional information
-
-
0.3-0.5
additional information
-
-
0.5-0.6 (gamma subunit)
additional information
-
-
activated enzyme has a higher pH-optimum than nonactivated enzyme
additional information
-
P46020, Q16816
enzyme assay at pH 6.8 and pH 8.2
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
11.5
-
about half-maximal activity at pH 6 and 11.5, liver enzyme
6.2
7.6
-
about half-maximal activity at pH 6.2 and 7.6, nonactivated enzyme
6.2
8
-
progressive increase of activity, about half-maximal activity at pH 7.4
6.2
8.8
-
progressive increase of activity
6.2
9.3
-
progressive increase of activity from 10% to 100% of maximal activity, with half-maximal activity at pH 7
6.2
9.5
-
about half-maximal activity at pH 6.2 and about 70% of maximal activity at pH 9.5
6.5
8.5
-
progressive increase of activity, biphasic with dogfish phosphorylase b as substrate: then about half-maximal activity at pH 7.2-7.6 (dogfish activated enzyme)
6.6
9.1
-
about half-maximal activity at pH 6.6 and 9.1, activity increases up to pH 8, sharp drop above 9
6.8
8.2
-
activity increases dramatically when the pH is raised from 6.8 to 8.2
6.8
8.5
-
about half-maximal activity at pH 6.8 and maximal activity at pH 8.5, activated rabbit enzyme
7.2
9
-
70% of maximal activity at pH 7.2 and and 9
8.1
8.5
-
about half-maximal activity at pH 8.1 and maximal activity at pH 8.5, nonactivated rabbit enzyme
9
10
-
about half-maximal activity at pH 9 and 10, muscle enzyme
additional information
-
Q64649
activity of purified native and recombinant enzymes and subunit subcomplexes at different pH, the latter show higher activity at pH 6.8, while the native enzyme shows higher activity at pH 8.2
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
22
-
-
assay at room temperature
26
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
autophosphorylation reaction at
30
-
Q64649
autophosphorylation reaction at
30
-
-
assay at
37
-
-
assay at
additional information
-
-
reaction and conformation temperature dependence, overview
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
P46019
peripheral blood cells
Manually annotated by BRENDA team
-
differentiated muscle myoblasts
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
-
soleus muscle
Manually annotated by BRENDA team
P46020, Q16816
muscle isoform; muscle isoform
Manually annotated by BRENDA team
-
muscle cells
Manually annotated by BRENDA team
-
postmortem tissue, 8fold increase in glycogen concentration and no detectable phosphorylase kinase activity
Manually annotated by BRENDA team
-
from back and leg
Manually annotated by BRENDA team
-
papillary
Manually annotated by BRENDA team
additional information
-
isozyme distribution in different tissues
Manually annotated by BRENDA team
additional information
-
-
Manually annotated by BRENDA team
additional information
-
tissue distribution in dogfish
Manually annotated by BRENDA team
additional information
-
isozyme distribution in different tissues
Manually annotated by BRENDA team
additional information
-
isozyme distribution in different tissues
Manually annotated by BRENDA team
additional information
-
PhK shows a wide tissue distribution, expression of subunits, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
together with other enzymes of glycogen metabolism linked together on glycogen particles
-
Manually annotated by BRENDA team
-
due to protein-protein interactions in glycogen particles the proteins behave differently from those in cytosol; organelle-like particles
-
Manually annotated by BRENDA team
-
of sarcoplasmic reticulum
Manually annotated by BRENDA team
-
KPI-2 is a transmembrane protein
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
29000
-
-
Saccharomyces cerevisiae, gel filtration
86000
-
-
rabbit, catalytically active gammagamma subunit complex, gel filtration
130000
-
-
gel filtration
205000
-
-
rabbit, trypsinized or chymotrypsinized enzyme form, gel filtration
243000
-
-
rabbit, alphagammadelta complex, gel filtration
1000000
-
-
rat
1220000
-
-
rabbit, HPLC gel filtration
1260000
-
-
rabbit, gel filtration
1300000
-
-
rabbit, gel filtration
1300000
-
-
rat, gel filtration
1300000
-
-
bovine, sucrose density gradient centrifugation
1300000
-
-
dogfish, gel filtration or sedimentation velocity analysis
1300000
-
-
rat, gel filtration
1320000
-
-
chicken, gel filtration
1330000
-
-
analytical ultracentrifugation; rabbit, nonactivated enzyme
1330000
-
-
analytical ultracentrifugation
additional information
-
-
amino acid composition; 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
additional information
-
-
amino acid composition
additional information
-
-
MW of trypsinized enzyme
additional information
-
-
mechanism and structure
additional information
-
-
amino acid sequence in regulatory domain of gamma subunit
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 44673, calculation from amino acid sequence
dimer
-
2 * 45000, rabbit, catalytically active gammagamma subunit, SDS-PAGE
heterotetramer
-
x-ray crystallography
hexadecamer
-
alpha4beta4gamma4delta4, alpha and beta subunits are regulatory, delta is calmodulin, and the gamma subunit is catalytic
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
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
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
-
alpha4beta4gamma4delta4
hexadecamer
Q64649
(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
-
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 * alpha + 4 * beta + 4 * gamma + 4 * delta
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
-
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
Q171G3
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
P34335
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
P12798, P18688
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory; 4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
A2WRR1
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
Q9W6R1
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
oligomer
P46020, Q16816
;
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
hexadecamer
Q4S8G1
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
additional information
-
the enzyme has an open, active conformation and a closed, inactive conformation
additional information
-
phosphorylase kinase is a multisubunit protein kinase with molecular weight above 1000000 Da
additional information
-
gamma subunit; homology with catalytic subunit of cAMP dependent protein kinase
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
-
partial amino acid composition of subunits
additional information
-
spatial arrangement of subunits; subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity; the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
-
delta subunits
additional information
-
spatial arrangement of subunits
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
-
molecular interaction and subunit structure
additional information
-
amino acid composition of alpha; delta subunits; gamma
additional information
-
amino acid composition of alpha; beta; gamma
additional information
-
gamma' subunit is not identical with rabbit skeletal muscle gamma subunit
additional information
-
alpha'; amino acid sequence of alpha, beta
additional information
-
composed of 3 regulatory and 1 catalytic subunit
additional information
-
chicken gamma and alpha' subunits compared to that of rabbit red muscle enzyme
additional information
-
amino acid sequence of alpha, beta; gamma subunit; structure/function relationships of subunits
additional information
-
alpha and beta subunits are regulatory subunits controlled by phosphorylation and proteolysis, Ca2+-sensitivity is conferred to delta subunit; the catalytic gamma subunit contains a kinase domain and a calmodulin binding domain
additional information
-
the delta subunit is identical with calmodulin
additional information
Q64649
the delta subunit is identical with calmodulin
additional information
-
self-association is induced by Mg2+ and Ca2+, kinetics
additional information
-
calmodulin is identical with the delta subunit
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
-
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
-
conformational substates of PhK subunit bound or unbound to calmodulin and Ca2+, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
the phosphorylase kinase is activated by cAMP-dependent protein kinase
phosphoprotein
-
autophosphorylation, the site often depends more on structure than on primary sequence
phosphoprotein
-
subunit PhKalpha is autophosphorylated
proteolytic modification
-
specific cleavage of caspase-3 at a specific cleavage site within the alpha-subunit at residue 46 in the sequence DWMD*G
phosphoprotein
Q64649
regulation by de-/phosphorylation performed by cAMP-dependent protein kinase, EC 2.7.11.11
proteolytic modification
-
specific cleavage of caspase-3 at a specific cleavage site within the alpha-subunit in vivo
additional information
-
the native and the recombinant enzyme performs autophosphorylation of its alpha and beta subunits
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallization of PhK in active conformation
-
crystal structures of the catalytic core, residues 1-298, of the gamma-subunit, the binary complex with Mn2+/beta-gamma-imidoadenosine 5'-triphosphate to a resolution of 2.6 A and the binary complex with Mg2+/ADP to a resolution of 3.0 A
-
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, i.e. Phkgammatrnc, in the presence of Mg-ATP, X-ray data
-
structure of a truncated form of the gamma-subunit of phosphorylase kinase in a ternary complex with a non-hydrolysable ATP analogue, adenylylimidodiphosphate, and a heptapeptide substrate related in sequence to both the natural substrate and to the optimal peptide substrate
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
-
below, rapid irreversible inactivation
6.8
-
-
PhK is almost inactive at pH 6.8
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h stable
30
-
-
at least 30 min
37
-
-
50% loss of nonactivated enzyme activity within 15 min, 50% loss of alphagammadelta subunit complex activity within 7 min, 90% loss of gammadelta subunit complex activity within 5 min
40
-
-
t1/2: 3 min, in 10% ethylene glycol, pH 8
45
-
-
t1/2: 1 min, in 10% ethylene glycol, pH 8
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
About 70% loss of activity during centrifugation for 5 h on a glycerol density gradient
-
Delta-Subunit remains tightly bound to alphagammadelta subunit complex even in the presence of 8 M urea
-
Effects of protein concentration, buffer and ATP on stability and dissociation behaviour of trypsin-activated enzyme
-
In the presence of ATP nonactivated enzyme does not dissociate into catalytically active subunits as trypsin-activated enzyme does
-
Inactive gamma subunit after reverse-phase HPLC can be reactivated by dilution into ice-cold, pH 8.2, Ca2+/calmodulin containing buffer
-
Incubation of nonactivated enzyme with 100 mM ATP at 0C dissociates the 23 S enzyme to active 7.5 S and 14 S subunits, with LiBr it produces 5 S subunits
-
isoelectric focusing inactivates
-
Nonactivated or protein kinase-activated enzyme stable in the cold, not trypsin-activated enzyme
-
Rabbit muscle enzyme is subject to pressure denaturation leading to the formation of polydisperse aggregates
-
unstable in dilute solutions
-
Unstable in the presence of Mg2+
-
With strong tendency to aggregate, unstable in high concentrations of ammonium sulfate for prolonged periods
-
unstable in dilute solutions
-
5%, w/v, glycerol stabilizes
-
Ca2+-free enzyme is unstable
-
Rapid irreversible inactivation during desalting by gel filtration or dialysis at ionic strength below 0.1, sucrose, glycerol, salts, SH-compounds or reagents does not stabilize, glycogen, glucose, glucose 1-phosphate, glucose 6-phosphate, mono-, di- and trinucleotides or divalent metal ions and protease inhibitors do not protect
-
Tends to aggregate upon standing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, several months
-
Frozen in liquid N2, in 50 mM beta-glycerophosphate, pH 7, 2 mM EDTA, 1 mM DTT, 10% sucrose, stable
-
-20C, in 50 mM sodium glycerophosphate, 0.1% v/v 2-mercaptoethanol, pH 7, 2 mM EDTA, 50% v/v glycerol, at least 1 year
-
-20C, partially purified, at least 2 months
-
-25C, in 50% ethylene glycol, at least 1 month
-
-80C, 50 mM Hepes, pH 6.8, 0.2 mM EDTA, 10% sucrose
-
0-4C, in 5-20% glycerol, 70% loss of activity within 5 h, more rapid inactivation in 5-20% sucrose
-
0C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 30% loss of activity within 4 h
-
0C, in 10% ethylene glycol, at least 1 week
-
20 C, 25 mM Na-glycerol phosphate buffer, pH 7.05, 1 mM EDTA, 0.5 mM 2-mercaptoetanol, 50% glycerol, stored for 3 weeks
-
20C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h
-
Frozen, at least 6 months
-
-20C, in 0.25 M sucrose, 0.1 M Tris-HCl, 0.5 mM DTT, pH 7.4, 50% glycerol, several weeks
-
-70C, in 20 mM triethanolamine-HCl, pH 7.5, 20% v/v glycerol, 1 mM DTT, 0.02% NaN3, stable
-
-15C, 3 mg dogfish enzyme/ml, in 0.1 M glycerophosphate, 2 mM EDTA, pH 7, 0.3 M NaCl or in 0.1 M glycerophosphate, 2 mM EDTA, 10% sucrose, 1 mM ATP, pH 7, 1 mM DTT, about 50% loss of activity within 1 week
-
-15C, partially purified dogfish enzyme, lyophilized, almost indefinitely
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
heart
-
nonactivated enzyme; to near homogeneity
-
to near homogeneity
-
to near homogeneity
-
recombinant c-Myc-/His6-tagged full-length KPI-2 from Sf9 cells by nickel affinity and ion exchange chromatography, and gel filtration
-
recombinant gamma-subunit, as expressed in Sf-9 cells
-
2 isozymes separable by calmodulin affinity chromatography; isolation of denatured subunits; overview
-
active gamma subunit from inactive form by reverse-phase HPLC)
-
alpha, alpha' and beta subunits by preparative SDS-PAGE
-
as in vivo activated phosphorylase sa
-
as nonactivated enzyme; to near homogeneity (phosphorylase b is a persistent contaminant)
-
by affinity chromatography on calmodulin-Sepharose 4B; catalytically active alphagammadelta complexes; catalytically active gammadelta complexes
-
catalytic subunit (i.e. gamma subunit, from holoenzyme by dissociation)
-
catalytic subunit as expressed in Escherichia coli
-
catalytically active alphagammadelta complexes
-
catalytically active proteolytic product of holoenzyme; liver; to near homogeneity
-
DEAE Toyopearl 650M column chromatography
-
delta subunit
-
from protein-glycogen complex; to near homogeneity
-
from skeletal muscle
-
homogenous alpha, beta and gamma subunits
-
isolation of denatured subunits (from nonactivated enzyme)
-
native and proteolytically generated enzyme forms
-
native enzyme from psoas muscle
-
native enzyme from skeletal muscle by anion exchange chromatography to homogeneity
-
native enzyme from skeletal muscle, recombinant enzyme subunit subcomplexes from Sf9 insect cells
-
from sarcoplasmic reticular membranes of femoral muscle
-
recombinant holoenzyme and enzyme subunit subcomplexes from Sf9 insect cells
Q64649
to near homogeneity from glycogen-rich pellet, from 1000 rats
-
from sarcoplasmic reticular membranes of spinal muscle
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNA sequence and predicted primary structure of the gamma M subunit
Q16816
DNA sequence determination and structural analysis, genetic organization, the subunits of the muscle isozyme are encoded by different genes, subunit alpha is encoded by gene PHKA1, genes PHKA1, PHKB1, PHKG1, CALM1, CALM2, and CALM3 are involved, relation to several pseudogenes; DNA sequence determination and structural analysis, genetic organization, the subunits of the muscle isozyme are encoded by different genes, subunit gamma is encoded by gene PHKG1, genes PHKA1, PHKB1, PHKG1, CALM1, CALM2, and CALM3 are involved, relation to several pseudogenes
P46020, Q16816
expression of c-Myc-/His6-tagged full-length KPI-2 and minimal kinase fold, residues 137-407 plus an additional C-terminal segment in HEK-293 cells and in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system
-
PhK isozymes, DNA sequence and genomic localization determination and analysis, genetic organization, the genes encoding the alpha, beta, and gamma subunits of PhK undergo extensive transcriptional processing, e.g. exon 6 of PhKG1 is a 3' composite terminal exon due to the presence of weak polyadenylation and cleavage site in intron 6
-
isolation of cDNA clones for the catalytic gamma subunit of mouse muscle phosphorylase kinase
-
mouse catalytic gamma subunit, Baculovirus-directed expression in Sf9 insect cells
-
alpha, gamma, delta-trimer, complex is shown to be unable to phosphorylate glyceraldehyde-3-phosphate dehydrogenase
-
cooverexpression with the beta subunit of the rabbit enzyme with the rat holoenzyme and rat alphagammadelta and gammadelta subunit complexes in Spodoptera frugiperda Sf9 cells via the baculovirus infection system, resulting in formation of subunit subcomplexes, overview
-
isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit
-
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, expressed in Escherichia coli
-
two hybrid rabbit DNA library screening using the yeast strain EGY48 and a C-terminal fragment of isozyme PhKalpha, expression of the enzyme and interaction partners in C2C12 cells
-
two-hybrid plasmid construction of fusions containing the PhK beta subunit and its deletion mutants and expression in a yeast two-hybrid system
-
nucleotide sequence of cDNA encoding the catalytic subunit
-
PhK-gamma T isoform of phosphorylase kinase catalytic subunit
P31325
subcloning of subunits in Escherichia coli, overexpression of the soluble holoenzyme and of soluble trimeric alphagammadelta and dimeric gammadelta subunit subcomplexes, as well as coexpression with the beta subunit of the rabbit enzyme also resulting in subunit complex formation, in Spodoptera frugiperda Sf9 cells via the baculovirus infection system
Q64649
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D299V
P46020, Q16816
naturally occurring mutation in gene PHKB, encoding subunit beta, missense mutation leads to enzyme deficiency in vivo; naturally occurring mutation in gene PHKB, encoding subunit beta, missense mutation leads to enzyme deficiency in vivo
DELTA189-190
P46019
naturally occurring mutation in XLG II patient, increased activity blood cells
Q1169X
P46019
naturally occurring mutation in XLG I patient, CAG codon is replaced by a TAG stop codon, very low activity in blood cells
Q657K
P46020, Q16816
naturally occurring heterozygous single amino acid replacement in gene PHKB, might not be significant for enzyme deficiency disease, patient shows low enzyme activity; naturally occurring heterozygous single amino acid replacement in gene PHKB, might not be significant for enzyme deficiency disease, patient shows low enzyme activity
R295H
P46019
naturally occurring mutation in XLG I and XLG II patients, very low activity in blood cells and liver
R384T
-
naturally occurring mutation
E1125K
P46019
naturally occurring mutation in XLG I patient, low activity in blood cells
additional information
-
regulatory enzyme of glycogen metabolism, mutations in the testis/liver isoform of the phosphorylase kinase gamma subunit cause autosomal liver glycogenosis. Mutation V106E, G189E and D215N are responsible for autosomal form of Phk deficiency
Y770C
P46020, Q16816
naturally occurring heterozygous single amino acid replacement in gene PHKB, might not be significant for enzyme deficiency disease, patient shows low enzyme activity; naturally occurring heterozygous single amino acid replacement in gene PHKB, might not be significant for enzyme deficiency disease, patient shows low enzyme activity
additional information
-
a B2 repeat insertion generates alternate structures of the mouse muscle gamma-phosphorylase kinase gene
additional information
-
construction of PhKbeta subunit deletion mutants