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Information on EC 2.7.11.19 - phosphorylase kinase and Organism(s) Oryctolagus cuniculus and UniProt Accession P00518
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2.7.11.19 phosphorylase kinaseIUBMB Comments
Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis---glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b . The gamma subunit of the tetrameric enzyme is the catalytic subunit.
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Word Map
- 2.7.11.19
- calmodulin
-
camp-dependent
- amp
- phosphatases
- myosin
- glycogenosis
- casein
- autophosphorylation
-
holoenzyme
- alpha-subunits
- glucagon
- troponin
-
nonactivated
-
x-linked
-
calmodulin-dependent
- phosphoprotein
-
gamma-subunits
-
glycogenolytic
- mgatp
- hepatomegaly
-
calmodulin-binding
-
sarcoplasmic
-
cohen
- inhibitor-1
- phosphopeptide
-
hexadecameric
-
phosphorylatable
-
delta4
-
debranching
-
2.4.1.1
- trifluoperazine
-
bisbeta-aminoethyl
-
phosphatase-2a
-
amp-independent
- phosvitin
- amylo-1,6-glucosidase
-
cyclic-amp-dependent
-
kinase-catalyzed
-
3':5'-monophosphate
-
kinase-deficient
-
seryl
- gizzard
-
carlson
-
calmodulin-sepharose
-
delta-subunits
- medicine
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
phosphorylase kinase, phosphorylase b kinase, glycogen phosphorylase kinase, phkg1, phk alpha, dphk-gamma, glycogen phosphorylase b kinase, psk-c3, kpi-2 kinase, phosphorylase kinase beta, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
-
dephosphophosphorylase kinase
-
-
-
-
EC 2.7.1.38
Glycogen phosphorylase kinase
-
-
-
-
kinase, phosphorylase (phosphorylating)
-
-
-
-
PhK
Phosphorylase b kinase
PSK-C3
-
-
-
-
EC 2.7.1.38
-
formerly, transferred to EC 2.7.11.19
PhK
-
-
Phosphorylase b kinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 ATP + phosphorylase b = 2 ADP + phosphorylase a
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
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.
CAS REGISTRY NUMBER
COMMENTARY
9001-88-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
the enzyme catalyzes the phosphorylation of inactive glycogen phosphorylase b on Ser-14 resulting in the formation of active glycogen phosphorylase a
-
-
?
ATP + alphagammadelta subunit complex
ADP + activated alphagammadelta subunit complex
-
autophosphorylation, by incorporation of phosphate into alpha subunit
-
?
ATP + glycogen phosphorylase
?
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen phosphorylase
ADP + phosphorylated glycogen phosphorylase
-
-
-
-
?
ATP + glycogen S peptide
ADP + phosphorylated glycogen S peptide
-
synthetic peptide corresponding to residues 5-18 of its convertible region
-
-
?
ATP + Lys-Arg-Glu-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Glu-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + Lys-Arg-Lys-Glu-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Arg-Lys-Glu-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + Lys-Glu-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
ADP + Lys-Glu-Lys-Gln-Ile-(phospho)Ser-Val-Arg-Gly-Leu
-
-
-
?
ATP + peptides derived from glycogen synthase
?
-
rabbit, overview
-
-
?
ATP + synthetic pentadecapeptide
?
-
from amino-terminal of glycogen synthase, i.e. Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ser-Ser-Leu-Pro-Gly-Leu-Glu
-
-
?
ATP + synthetic peptides derived from glycogen synthase
?
-
overview, phosphorylation at the same site as glycogen synthase
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
-
overview
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
-
phosphorylation is very slow, binds tightly to enzyme and acts as inhibitor for the phosphorylation of glycogen phosphorylase b
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
rabbit muscle GP
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
regulatory enzyme in the activation cascade of glycogenolysis
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
the hexadecameric enzyme complex that catalyzes the phosphorylation and activation of glycogen phosphorylase b
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
PhK catalyzes the Ca2+- and cAMP-dependent glycogen phosphorylase b phosphorylation and activation
-
-
?
ATP + glycogen synthase
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen synthase
?
-
conversion to a glucose 6-phosphate dependent form
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
-
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
rabbit phosphorylase kinase
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
inactivation of skeletal muscle glycogen synthase in the presence or absence of EGTA
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
glycogen synthase a
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
phosphorylatable residue: Ser-7
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
at high concentration, from rabbit skeletal muscle
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
-
at the same rate as phosphorylase b
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
-
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
phosphorylates alpha and beta, not gamma or delta subunits
-
-
?
ATP + phosphorylase b
?
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
?
-
vital process for short term energy supply to the cell, located at an interface between signalling and metabolic pathway
-
-
?
ATP + phosphorylase b
?
-
involved in glycogen metabolism regulation
-
-
?
ATP + phosphorylase b
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
binding studies with immobilized substrate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
incorporation of terminal phosphate of ATP into phosphorylase b
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site located 14 residues from amino terminal
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
the enzyme interacts with glycogen and phosphorylase b
-
-
?
ATP + synthetic tetradecapeptide
?
-
i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu
-
-
?
ATP + synthetic tetradecapeptide
?
-
substrate for holoenzyme and for catalytic gamma subunit
-
-
?
ATP + synthetic tetradecapeptide
?
-
from amino-terminal of phosphorylase b
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
phosphorylation site (Thr-residue)
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
not rabbit or dogfish troponin I
-
-
?
ATP + troponin I
ADP + phosphotroponin I
-
rabbit phosphorylase kinase
-
-
?
ATP + troponin T
ADP + phosphotroponin T
-
not rabbit or dogfish troponin T
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
-
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
catalyzes phosphorylation and activation of glycogen phosphorylase b and hence plays a key role in the cascade system of regulation of glycogen metabolism
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
regulates energy production through its Ca2+-dependent activation of glycogen phosphorylase in the cascade activation of glycogenolysis, only known kinase that activates glycogen phosphorylase b
-
-
?
additional information
?
-
-
creatine phosphate, phosphoenolpyruvate, actin, parvalbumin, protamin, dogfish or rabbit myosin, adenosine 5'-(3-methyltriphosphate), 5'-adenylylimidodiphosphate (dogfish) are no substrates
-
-
?
additional information
?
-
-
no substrates are phosphorylase kinase gamma subunit
-
-
?
additional information
?
-
-
Lys-Gln-Ile-Ser-Val-Arg, Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Gly-Ser-Gly-Arg-Gly-Leu, Lys-Gln-Ile-Thr-Val-Arg, Arg-Lys-Gln-Ile-Thr-Val-Arg are no substrates
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
additional information
?
-
-
no spontaneous or MnSO4-induced dephosphorylation of activated enzyme
-
-
?
additional information
?
-
-
polylysine and polyarginine are no substrates
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation
-
-
?
additional information
?
-
-
interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle
-
-
?
additional information
?
-
-
key enzyme in regulating glycogenolytic flux in skeletal muscle in response to changing energy demands, phosphorylase kinase associates with the cytoskeletal organizing protein Cdc42-interacting protein 4, CIP4, in vivo in skeletal muscle, the cognate binding domain on CIP4 lies between residues 398 and 545, the interaction is independent of the SH3 domain
-
-
?
additional information
?
-
-
the enzyme complex regulates glycogenolysis
-
-
?
additional information
?
-
-
subunit PhKalpha is autophosphorylated
-
-
?
additional information
?
-
the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme
-
-
?
additional information
?
-
development of a highly sensitive and nonradioactive assay for phosphorylase kinase activity by measuring the enhanced glycogen phosphorylase activity towards a pyridylaminated maltohexaose, method evaluation, phosphate quantification by the FiskeSubbarow method, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + glycogen phosphorylase
?
-
conversion to an AMP-independent form, key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen phosphorylase
ADP + phosphorylated glycogen phosphorylase
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + phosphorylated glycogen phosphorylase b
-
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
-
?
2 ATP + glycogen phosphorylase b
2 ADP + glycogen phosphorylase a
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
-
regulatory enzyme in the activation cascade of glycogenolysis
-
-
?
ATP + glycogen synthase
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + glycogen synthase
?
-
conversion to a glucose 6-phosphate dependent form
-
-
?
ATP + phosphorylase b
?
-
i.e. EC 2.4.1.1 or glycogen phosphorylase
-
-
?
ATP + phosphorylase b
?
-
stimulates glycogenolysis in skeletal muscle
-
-
?
ATP + phosphorylase b
?
-
regulates conversion of inactive phosphorylase b into active phosphorylase a
-
-
?
ATP + phosphorylase b
?
-
vital process for short term energy supply to the cell, located at an interface between signalling and metabolic pathway
-
-
?
ATP + phosphorylase b
?
-
involved in glycogen metabolism regulation
-
-
?
ATP + phosphorylase b
?
-
key enzyme of neural and hormonal control of glycogen metabolism
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
the enzyme interacts with glycogen and phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
catalyzes phosphorylation and activation of glycogen phosphorylase b
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
catalyzes phosphorylation and activation of glycogen phosphorylase b and hence plays a key role in the cascade system of regulation of glycogen metabolism
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
regulates energy production through its Ca2+-dependent activation of glycogen phosphorylase in the cascade activation of glycogenolysis, only known kinase that activates glycogen phosphorylase b
-
-
?
additional information
?
-
-
interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle
-
-
?
additional information
?
-
-
key enzyme in regulating glycogenolytic flux in skeletal muscle in response to changing energy demands, phosphorylase kinase associates with the cytoskeletal organizing protein Cdc42-interacting protein 4, CIP4, in vivo in skeletal muscle, the cognate binding domain on CIP4 lies between residues 398 and 545, the interaction is independent of the SH3 domain
-
-
?
additional information
?
-
-
the enzyme complex regulates glycogenolysis
-
-
?
additional information
?
-
the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
capable of binding FAD, binding of FAD suppresses self association of enzyme
-
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
-
can partially replace ATP in the activation of nonactivated enzyme
ATP
-
-
ATP
-
activation of nonactivated enzyme by phosphorylation of subunits A and B, not C
Calmodulin
-
calmodulin containing enzyme i.e. tightly bound delta subunit
Calmodulin
-
no activation of phosphorylated or proteolytically modified enzyme by delta'-subunit
Calmodulin
-
activation of nonactivated enzyme and alphagammadelta subunit complex
Calmodulin
-
in the presence of Ca2+: 1 mol extrinsic calmodulin per mol alphabetagammadelta rabbit enzyme
Calmodulin
-
tightly bound molecule interacts with additional calmodulin in the presence of Ca2+
Calmodulin
-
in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation
Calmodulin
-
no activation of bovine red skeletal muscle or rabbit cardiac enzymes
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ba2+
Ca2+
Li+
Mg2+
Mn2+
phosphate
Sr2+
additional information
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+
-
-
Ca2+
-
irreversible activation of nonactivated kinase by preincubation together with a separate kinase-activating factor independent of cAMP, kinetics
Ca2+
-
required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Ca2+
-
stabilization, no absolute requirement for catalytic subunit gamma2
Ca2+
-
delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction
Ca2+
-
stimulates autophosphorylation in micromolar range at pH 6.8, inhibits at millimolar range
Ca2+
-
requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
-
stimulates phosphorylase b binding to enzyme, but to a considerable lesser extent than Mg2+
Ca2+
-
activates, binding structure modeling, Ca2+-binding induces structural perturbation of the subunits and promotes redistribution of density throughout the lobes and bridges of the enzyme structure
Ca2+
-
dependent on, induces enzyme self-association and increases interaction with glycogen
Ca2+
-
activates, the four integral delta subunits of the phosphorylase kinase complex are identical to calmodulin and confer Ca2+ sensitivity to the enzyme, but bind independently of Ca2+, Ca2+ influences the conformational substrates of the subunits, overview
Ca2+
-
is an obligatory allosteric activator absolutely required by the enzyme, Ca2+ activates PhK by binding to its nondissociable calmodulin subunits, it couples the cascade activation of glycogenolysis with muscle contraction, enzyme surface electrostatic properties of solvent accessible charged and polar groups are altered upon the binding of Ca2+ ions
Ca2+
-
induces association, obligatory allosteric activator, binds to an integral, nondissociable molecule of calmodulin (delta-subunit), and thus reveals the protein kinase activity of the catalytic gamma-subunit, which in the absence of Ca2+ ions is constrained by the regulatory alpha- and beta-subunits
Mg2+
-
requirement
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
effect of Mg2+ on Ca2+-binding properties of nonactivated enzyme at pH 6.8
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
Mg2+
-
required for activity phosphorylation by (cAMP-dependent protein kinase)
Mg2+
-
dependent on, induces enzyme self-association and increases interaction with glycogen
Mg2+
-
activator, changes in the physicochemical properties of the enzyme induced by Mg2+ under nonactivating (pH 6.8) and activating (pH 8.2) conditions are investigated by circular dichroism spectroscopy, zeta potential analyses, dynamic light scattering, second derivative UV absorption, negative stain electron microscopy, and differential chemical crosslinking. The effects of the activator Mg2+ on some of the properties of the enzyme measured by these techniques are quite different at the two pH values.
Mn2+
-
stimulates activation by catalytic subunit of cAMP-dependent protein kinase
Mn2+
-
at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
-
alphagammadelta complex undergoes autophosphorylation: up to 4.2 mol phosphate/mol complex incorporated into alpha subunit
phosphate
-
requirement, phosphate containing enzyme
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492116, 492117, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492131, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492141, 492142, 492145, 492146, 492147, 492149, 492150, 492152, 492154, 492155
phosphate
-
gammadelta subunit complex cannot phosphorylate itself but phosphorylates and activates native enzyme, even in the presence of EGTA or protein kinase inhibitor
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
additional information
-
synopsis of activity by Ca2+/Mg2+ and phosphorylation
additional information
Ca2+ and Mg2+ induce self-aggregation of PhK at 37°C
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(D)-Arg-(D)-Leu-(D)-Ser-(D)-Leu
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
actin
-
inhibits activation of subunit gamma-troponin C or subunit gamma-calmodulin complexes
betaine
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Calcineurin
-
i.e. calmodulin-binding protein, blocks activation by calmodulin
-
Calmodulin
-
inhibits cAMP-dependent protein kinase mediated activation of phosphorylase kinase, kinetics
FAD
-
FAD at high concentrations completely inhibits the second stage of enzyme binding to glycogen particles containing glycogen phosphorylase b, the inhibitory effect of FAD is not complete and reaches a maximal value at FAD concentrations around 0.03 mM
Ile-Ser-Val-Arg-Gly
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu as substrate
Melittin
-
model calmodulin-binding peptide, mechanism, kinetic, phosphorylase b as substrate
Monospecific antibodies against alpha, beta and gamma subunits
-
mechanism, kinetic, anti-beta subunit reverses inhibition by anti-alpha at pH 6.8
-
poly-L-lysine
-
strong, activated and nonactivated enzyme, stimulates autophosphorylation
proline
-
inhibits enzyme self-association and interaction with glycogen and phosphorylase b
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Asp-Val-Arg-Gly-Leu
-
substrate-directed dead end inhibitor
Trimethylamine N-oxide
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
VIRDPYALRPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 332-353
ATP
-
total inhibition if ATP concentration exceeds that of divalent cation (i.e. Mg2+)
ATP
enzyme PhK shows substrate inhibition at high ATP concentration above 3 mM
DTNB
-
only gradual loss of activity after more than 10 min, pH-dependent
EGTA
-
alphagammadelta and gammadelta subunit complexes less sensitive than holoenzyme
glucose 6-phosphate
-
Mg2+ protects, phosphorylase b as substrate, mechanism, kinetics
glucose 6-phosphate
-
no inhibition with modified phosphorylase b or a tetradecapeptide as substrate
Synthetic peptide PhK13
derived from gamma subunit region, residues 302-326
Synthetic peptide PhK5
derived from gamma subunit region, residues 342-366
Trifluoperazine
-
nonspecific inactivation, at high concentrations, together with EGTA additive effect
additional information
-
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
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
-
phosphorylase kinase alpha and beta subunits suppress catalytic activity of gamma subunit in holoenzyme
-
additional information
gamma subunit with autoinhibitory domains
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex)
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex)
-
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex)
-
additional information
-
no inhibition by diethyldithiocarbamic acid, 2,2'-dipyridyl
-
additional information
-
inhibition study with modified gamma subunit
-
additional information
-
no inhibition by CTP, caffeine, cAMP, cGMP, IMP, glucose 6-phosphate (gammadelta subunit complex)
-
additional information
-
effect of molecular crowding, osmolytes inhibit complex formation with substrate phosphorylase b
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
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
-
evaluation of indirubin analogues as phosphorylase kinase inhibitors, structure-activity relationship analysis, docking, overview. The inhibitory effects arises from binding at the kinase domain, i.e. gamma-subunit
-
additional information
loss of activity through proteolysis only by ficin digestion
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,2-dimethoxyethane
-
activation, 10% v/v, stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
adenosine 3'-phosphate 5'-phosphosulfate
-
activation, can replace ADP to some extent
adenosine 5'-phosphosulfate
-
activation, can replace ADP to some extent
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
caspase-3
-
selective in vitro cleavage of the regulatory alpha-subunit increasing the enzyme activity 2fold
-
poly-L-arginine
-
strong, phosphorylase kinase as substrate, i.e. autophosphorylation
poly-L-lysine
-
strong, only with phosphorylase kinase as substrate, i.e. autophosphorylation, inhibits activity of activated and nonactivated enzyme with other substrates
Trimethylamine N-oxide
-
stimulates enzyme self-association and interaction with glycogen, prevents complex formation with phosphorylase b
Troponin
-
i.e. complex of troponin C, I and T, activation, as effective as troponin C, forms complex with beta subunit
-
adenosine 3',5'-monophosphate
-
i.e. cAMP, activation of nonactivated enzyme, not alone, only in the presence of Mg2+ or Mn2+
adenosine 3',5'-monophosphate
-
no enhancement or inhibition of this activation by various nucleotides and other compounds, overview
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
Ca2+-dependent protease
-
proteolytic activation of nonactivated enzyme
-
Calmodulin
-
influences the conformational substrates of the subunits, overview
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
or alphagammadelta subunit complex
-
Catalytic subunit of cAMP-dependent protein kinase
-
and beta
-
Catalytic subunit of cAMP-dependent protein kinase
-
by phosphorylation of alpha'
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation by enhancing vmax selectively for A2 activity
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
chymotrypsin
-
by limited proteolysis of alpha subunit, not gamma or delta subunits
-
glycogen
-
stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex
glycogen
significantly stimulates the enzyme PhK. GPb molecules located on the glycogen surface might serve as good connecting molecules between PhK and glycogen and, consequently, promote indirect binding of PhK to the glycogen surface. Under conditions of high ionic strength and high ATP concentration in the body, direct binding of PhK to glycogen is reported to be very weak. The ternary PhK-GPbn-glycogen complex produces active GPa very efficiently compared with PhK, either alone or in the binary complex, i.e. the PhK-GPb complex. The effect is inhibited by gamma-cyclodextrin
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
troponin C
-
presumably key event in vivo, coupling glycogenolysis and muscle contraction
-
Trypsin
-
proteolytic activation of nonactivated enzyme
-
Trypsin
-
accompanied by loss of absolute requirement for Ca2+, activates holoenzyme and alphagammadelta subunit complex, not gammadelta complex
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits
-
Trypsin
-
vmax enhancement of all three activities of the kinase: A0, A1 and A2
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits or delta subunits
-
additional information
-
hexadecamer of (alphabetagammadelta)4 with variable degree of activity depending on pH, metal ions, allosteric effectors, covalent modifications, etc.
-
additional information
-
no activation by g adenine, adenosine, 5'-AMP, 2',5'-ADP, 3',5'-ADP, adenosine 2':3'cyclicphosphate 5'-monophosphate, alpha,beta-methylene-ADP, adenosine 2'-phosphate 5'-phosphosulfate, adenosine 5'-diphosphoglucose, adenosine 5'-diphosphoribose, ADP-3'-diphosphate, adenylylimidodiphosphate, diadenosine diphosphate
-
additional information
-
the nonactivated enzyme (i.e. Dephospho-enzyme)
-
additional information
-
no activation by glucose 6-phosphate, UDPglucose, dogfish myosin, actin, tropomyosin, rabbit glycogen synthase
-
additional information
-
no activation of nonactivated enzyme by renin (with or without Ca2+), thrombin (with or without Ca2+), phospholipase D from Clostridium perfringens or phospholipase from Crotalus adamanteus
-
additional information
-
no activation by g poly-aspartic acid, hexametaphosphate, yeast nucleic acid, at pH 6.8
-
additional information
-
no stimulation of autophosphorylation by poly-L-alanine, poly-L-asparagine, putrescine, spermidine or spermine
-
additional information
-
No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate
-
additional information
-
No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
-
additional information
-
three separate activities can be characterized by their response to Ca2+, Mg2+, NH4Cl and pH: A0, A1 and A2
-
additional information
-
location of an allosteric activation switch in the multisubunit phosphorylase kinase complex, overview
-
additional information
activation of phosphorylase kinase by physiological temperature
-
additional information
-
activation of phosphorylase kinase by physiological temperature
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0093
glycogen phosphorylase b
at pH 8.2 in the presence of calcium
0.018
ATP
-
phosphorylase b, truncated form of phosphorylase kinase gamma subunit
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
kinetic properties, overview
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic parameters of catalytically active gamma subunit at pH 6.8 and 8.5
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
kinetic parameters for different enzyme forms
-
additional information
additional information
-
kinetic properties of covalently modified and nonmodified phosphorylase kinase
-
additional information
additional information
-
effect of isolated delta subunit on kinetic parameters of nonactivated holoenzyme and alphagammadelta complex
-
additional information
additional information
-
influence of anti-subunit antibodies
-
additional information
additional information
-
kinetic data of holoenzyme and catalytically active proteolytic fragment
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic properties of subunit complexes at pH 6.8 and 8.5
-
additional information
additional information
-
kinetics of phosphorylase kinase-glycogen complex formation
-
additional information
additional information
the rate of product formation by the basal activity of PhK is not linear
-
additional information
additional information
-
the rate of product formation by the basal activity of PhK is not linear
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
134
glycogen phosphorylase b
at pH 8.2 in the presence of calcium
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00029
6'-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00082
6,5-dichloroindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0002
6,5-dichloroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00233
6,6'-dibromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-5-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00036
6-bromo-5-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-5-nitroindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0012
6-bromo-5-nitroindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.001
6-bromo-5-nitroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-N-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
6-bromo-N-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00033
6-bromoindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00034
6-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00023
6-chloroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00022
6-fluoroindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00033
6-iodoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00113
6-methoxindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0007
6-methoxindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00054
6-vinylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00055
6-vinylindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromo-N-methylindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.01
7-bromoindirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.05
7-bromoindirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.0018
7-bromoindirubin-3'-oxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
0.00017
indirubin-3'-acetoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
-
0.00034
indirubin-3'-methoxime
Oryctolagus cuniculus
-
pH not specified in the publication, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
8.2
additional information
additional information
-
nonactivated kinase activity ratios at pH 6.8/8.2: between 0.01-0.05, activated kinase activity ratio: about 0.6
additional information
-
pH-activity profiles of alphagammadelta and gammadelta subunit complexes
additional information
-
activity ratios pH 6.8/8.2 of nonactivated enzyme: 0.07 (in the presence of 0.05-0.07 M Ca2+) and 0.23 (after calmodulin addition)
additional information
-
activity ratios at pH 6.8/8.2: 0.01-0.02 (phosphorylase kinase a), 0.36 (phosphorylase kinase sa), 0.67 (phosphorylase kinase a')
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 9.5
-
about half-maximal activity at pH 6.2 and about 70% of maximal activity at pH 9.5
6.6 - 9.1
-
about half-maximal activity at pH 6.6 and 9.1, activity increases up to pH 8, sharp drop above 9
6.8 - 8.2
-
activity increases dramatically when the pH is raised from 6.8 to 8.2
6.8 - 8.5
-
about half-maximal activity at pH 6.8 and maximal activity at pH 8.5, activated rabbit enzyme
8.1 - 8.5
-
about half-maximal activity at pH 8.1 and maximal activity at pH 8.5, nonactivated rabbit enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
activation of phosphorylase kinase by physiological temperature
additional information
-
reaction and conformation temperature dependence, overview
30
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
the activity at pH 6.8 of nonphosphorylated PhK predictably increases, but between 30°C and 40°C, there is a dramatic jump in activity, resulting in the nonactivated enzyme having a far greater activity at body temperature than was previously realized. Both stimulation (by ADP and phosphorylation) and inhibition (by phosphate) were considerably less pronounced at 40°C than at 30°C. The probable underlying mechanism for the dramatic increase in PhK's activity between 30°C and 40°C is an abrupt change in the conformations of the regulatory beta and catalytic gamma subunits between these two temperatures. Activity profiles, overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
492092, 492094, 492095, 492096, 492097, 492098, 492099, 492100, 492101, 492102, 492103, 492104, 492105, 492106, 492108, 492109, 492110, 492111, 492112, 492113, 492114, 492118, 492120, 492122, 492123, 492124, 492125, 492128, 492130, 492133, 492135, 492136, 492137, 492138, 492139, 492140, 492145, 492149, 492152, 492154, 492155, 661075, 662670, 662844, 663335, 663347, 671763, 672305, 677034, 691329, 702389, 740880, 761263, 762340, 762341
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
due to protein-protein interactions in glycogen particles the proteins behave differently from those in cytosol
-
-
together with other enzymes of glycogen metabolism linked together on glycogen particles
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
the enzyme plays a key role in the cascade system for regulating glycogen metabolism
metabolism
-
the enzyme phosphorylates and activates glycogen phosphorylase in the cascade activation of glycogenolysis
physiological function
the enzyme regulates glycogenolysis in skeletal muscle
physiological function
-
the phosphorylase kinase enzyme complex regulates glycogenolysis
physiological function
glycogen phosphorylase, EC 2.4.1.1, exists in two interconvertible forms, GPa (phosphorylated form, high activity) and GPb (nonphosphorylated form, low activity). Phosphorylase kinase catalyses the phosphorylation of GPb and plays a key role in the cascade system for regulating glycogen metabolism
physiological function
the enzyme is a Ca2+-dependent regulatory enzymethat catalyzes phosphorylation and activation of glycogen phosphorylase b
physiological function
-
the enzyme plays a key role in the neural and hormonal regulation of glycogenolysis in skeletal muscle
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PHKG1_RABIT
387
0
44803
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
-
4 * alpha + 4 * 125000 (beta) + 4 * gamma + 4 * delta, beta-gamma-conjugate 1700000 Da, SDS-PAGE
125084
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
125200
125602
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
125660
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
130000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
1300000
1330000
138325
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
138400
138792
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
139358
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
145000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
16680
-
4 * 118000-145000 + 4 * 108000-128000 + 4 * 44673 + 4 * 16680, (alphabetagammadelta)4, rabbit, SDS-PAGE, 2 isozymes that differ in size of the largest subunit (alpha: 118000-145000 and alpha: 133000-140000)
16696
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
16700
16784
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
16787
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
17000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
17700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 17700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits
44643
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
44667
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
44669
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
44673
-
4 * 118000-145000 + 4 * 108000-128000 + 4 * 44673 + 4 * 16680, (alphabetagammadelta)4, rabbit, SDS-PAGE, 2 isozymes that differ in size of the largest subunit (alpha: 118000-145000 and alpha: 133000-140000)
44700
45000
86000
-
catalytically active gammagamma subunit complex, gel filtration
additional information
125200
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
125200
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 17700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits
138400
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
138400
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 17700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits
16700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
44700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
44700
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 17700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits
45000
-
2 * 45000, rabbit, catalytically active gammagamma subunit, SDS-PAGE
45000
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
additional information
-
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 45000, rabbit, catalytically active gammagamma subunit, SDS-PAGE
hexadecamer
tetramer
additional information
hexadecamer
-
4 * 118000-145000 + 4 * 108000-128000 + 4 * 44673 + 4 * 16680, (alphabetagammadelta)4, rabbit, SDS-PAGE, 2 isozymes that differ in size of the largest subunit (alpha: 118000-145000 and alpha': 133000-140000)
hexadecamer
-
4 * 145000 + 4 * 130000 + 4 * 45000 + 4 * 17000, (alphabetagammadelta)4, rabbit, SDS-PAGE
hexadecamer
-
2 major isozymes in muscle: (alphabetagammadelta)4 and (alpha'betagammadelta)4
hexadecamer
-
tertiary and secondary structure of PhK measured in presence or absence of Ca2+, conformational changes induced by Ca2+, surface electrostatic properties of solvent accessible charged and polar groups are altered upon the binding of Ca2+ ions, overview
hexadecamer
-
4 * alpha + 4 * 125000 (beta) + 4 * gamma + 4 * delta, beta-gamma-conjugate 1700000 Da, SDS-PAGE
hexadecamer
4 * alpha + 4 * beta + 4 * gamma + 4 * delta, gamma subunit is the catalytic subunit, alpha, beta and delta subunits are regulatory
hexadecamer
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits, delta subunit is calmodulin
hexadecamer
-
alpha,beta, gamma,delta, 4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 17700, catalytic gamma subunit is controlled by its regulatory alpha and beta, and delta subunits
hexadecamer
-
4 * 138325 (alpha), 4 * 125084 (beta), 4 * 44643 (gamma), 4 * 16696 (delta), (alphabetagammadelta)4, calculated from sequence, the phosphorylase kinase enzyme complex is composed of four copies each of four distinct subunits (alpha, beta, gamma and delta). The catalytic protein kinase subunit within this complex is gamma, and its activity is regulated by the three remaining subunits, which are targeted by allosteric activators from neuronal, metabolic, and hormonal signaling pathways. The network of contacts among subunits differs significantly between the nonactivated and phospho-activated conformers of the enzyme, with the latter revealing new interprotomeric contact patterns for the beta subunit, the predominant subunit responsible for activation of the enzyme complex by phosphorylation
hexadecamer
-
4 * 138792 (alpha), 4 * 125602 (beta), 4 * 44667 (gamma), 4 * 16787 (delta), (alphabetagammadelta)4, non-activated enzyme, mass spectrometry
hexadecamer
-
4 * 139358 (alpha), 4 * 125660 (beta), 4 * 44669 (gamma), 4 * 16784 (delta), (alphabetagammadelta)4, phospho-activated enzyme, mass spectrometry
hexadecamer
the beta subunit is helical and forms the 4-bridged core in the (alphabetagammadelta)4 kinase complex. Activity of the catalytic gamma subunit is regulated by allosteric activators targeting the regulatory alpha beta and delta subunits
hexadecamer
(alphabetagammadelta)4 , 4 x 138400, alpha-subunit, + 4 * 125200, beta-subunit, + 4 * 44700, gamma-subunit, + 4 * 16700, delta-subunit, about, mass spectrometry
hexadecamer
-
4 * 138400 + 125200 + 4 * 66700 + 4 * 16700, calculated from amino acid sequence
hexadecamer
-
4 * 138400 + 4 * 125200 + 4 * 44700 + 4 * 16700, calculated from amino acid sequence
tetramer
-
the enzyme forms a (alphabetagammadelta)4 complex, location of an allosteric activation switch in the multisubunit phosphorylase kinase complex, overview
additional information
-
composed of 3 regulatory and 1 catalytic subunit
additional information
-
the delta subunit is firmly bound to holoenzyme whereas delta' subunit (i.e. calmodulin) is bound only in the presence of Ca2+
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
alpha and beta subunits are regulatory subunits controlled by phosphorylation and proteolysis, Ca2+-sensitivity is conferred to delta subunit
additional information
-
the catalytic gamma subunit contains a kinase domain and a calmodulin binding domain
additional information
-
homology with catalytic subunit of cAMP dependent protein kinase
additional information
homology with catalytic subunit of cAMP dependent protein kinase
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
-
calmodulin is identical with the delta subunit
additional information
-
calmodulin is identical with the delta subunit, determination and analysis of enzyme three-dimensional structure with a resolution of 25 A by cryoelectron microscopy
additional information
-
calmodulin is identical with the delta subunit, X-ray light-scattering structure modeling of unactivated enzyme or enzyme after structural changes induced by Ca2+-binding, structure analysis, overview
additional information
-
self-association is induced by Mg2+ and Ca2+, kinetics
additional information
-
conformational substrates of PhK subunit bound or unbound to calmodulin and Ca2+, overview
additional information
Ca2+and Mg2+ions induce the self-association of PhK. Effects of arginine on protein-protein interactions in the enzyme polymer: arginine induces aggregation of Ca2+-free enzyme PhK. But when studying Ca2+, Mg2+-induced aggregation of PhK at 37°C, the protective effect of arginine is demon-strated, disruption of PhK hexadecameric structure occurs under the action of arginine. Although HspB6 and HspB5 suppress aggregation of PhK they do not block the disruption effect of arginine with respect to both forms of PhK (Ca2+-free and Ca2+, Mg2+-bound conformers). Aggregation of PhK induced by 0.5 M Arg is significantly suppressed in the presence of 1 M trimethylamine N-oxide dihydrate (TMAO)
additional information
mass spectrometric analysis of surface-exposed regions in the hexadecameric phosphorylase kinase complex, overview. Phosphorylase kinase is a 1.3 MDa (alphabetagammadelta)4 enzyme complex, in which alphabetagammadelta protomers associate in D2 symmetry to form two large octameric lobes that are interconnected by four bridges. The alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme. Enzyme structure analysis by mass spectrometry, small-angle X-ray scattering, and transmission electron microscopy
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
-
specific cleavage of caspase-3 at a specific cleavage site within the alpha-subunit at residue 46 in the sequence DWMD*G
additional information
phosphoprotein
-
autophosphorylation results in a 40fold activation of phosphorylase conversion at pH 6.8
phosphoprotein
the phoshorylase kinase i phosphorylated and activated
phosphoprotein
when PhK is phosphorylated, the alpha subunit is cleaved in the same loop regions (656-748 and 967-1015). A new region (627-662) proximal to the former loop is observed. Additionally, two new regions near the C-terminus of alpha appear, as well as a peptide corresponding to residues 1103-1113 and one of residues 1217-1224. Cys1234 is modified only in the phosphorylated complex. The entire C-terminus from residues 1217 to 1237 may be more exposed in the activated conformer
phosphoprotein
-
the enzyme is activated by phosphorylation of its alpha and beta subunits
phosphoprotein
-
the enzyme is activated by phosphorylation of Ser26 on beta subunit by cAMP-dependent protein kinase
additional information
-
the native and the recombinant enzyme performs autophosphorylation of its alpha and beta subunits
additional information
loss of activity through proteolysis only by ficin digestion
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the catalytic core, residues 1-298, of the gamma-subunit, the binary complex with Mn2+/beta-gamma-imidoadenosine 5'-triphosphate to a resolution of 2.6 A and the binary complex with Mg2+/ADP to a resolution of 3.0 A
structure of a truncated form of the gamma-subunit of phosphorylase kinase in a ternary complex with a non-hydrolysable ATP analogue, adenylylimidodiphosphate, and a heptapeptide substrate related in sequence to both the natural substrate and to the optimal peptide substrate
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, i.e. Phkgammatrnc, in the presence of Mg-ATP, X-ray data
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of PhKbeta subunit deletion mutants
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h stable
37
-
50% loss of nonactivated enzyme activity within 15 min, 50% loss of alphagammadelta subunit complex activity within 7 min, 90% loss of gammadelta subunit complex activity within 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
About 70% loss of activity during centrifugation for 5 h on a glycerol density gradient
-
Delta-Subunit remains tightly bound to alphagammadelta subunit complex even in the presence of 8 M urea
-
Effects of protein concentration, buffer and ATP on stability and dissociation behaviour of trypsin-activated enzyme
-
In the presence of ATP nonactivated enzyme does not dissociate into catalytically active subunits as trypsin-activated enzyme does
-
Inactive gamma subunit after reverse-phase HPLC can be reactivated by dilution into ice-cold, pH 8.2, Ca2+/calmodulin containing buffer
-
Incubation of nonactivated enzyme with 100 mM ATP at 0°C dissociates the 23 S enzyme to active 7.5 S and 14 S subunits, with LiBr it produces 5 S subunits
-
Nonactivated or protein kinase-activated enzyme stable in the cold, not trypsin-activated enzyme
-
Rabbit muscle enzyme is subject to pressure denaturation leading to the formation of polydisperse aggregates
-
With strong tendency to aggregate, unstable in high concentrations of ammonium sulfate for prolonged periods
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50 mM sodium glycerophosphate, 0.1% v/v 2-mercaptoethanol, pH 7, 2 mM EDTA, 50% v/v glycerol, at least 1 year
-
-80°C in 50 mM HEPES buffer (pH 6.8, 10% w/v sucrose, and 0.2 mM EDTA)
-
0-4°C, in 5-20% glycerol, 70% loss of activity within 5 h, more rapid inactivation in 5-20% sucrose
-
0°C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 30% loss of activity within 4 h
-
20 °C, 25 mM Na-glycerol phosphate buffer, pH 7.05, 1 mM EDTA, 0.5 mM 2-mercaptoetanol, 50% glycerol, stored for 3 weeks
-
20°C, 2 mg enzyme/ml, trypsin-activated enzyme, with or without ATP, 4 h
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic subunit (i.e. gamma subunit, from holoenzyme by dissociation)
-
native enzyme from skeletal muscle by anion exchange chromatography to homogeneity
-
native enzyme from skeletal muscle, recombinant enzyme subunit subcomplexes from Sf9 insect cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit
alpha, gamma, delta-trimer, complex is shown to be unable to phosphorylate glyceraldehyde-3-phosphate dehydrogenase
-
cooverexpression with the beta subunit of the rabbit enzyme with the rat holoenzyme and rat alphagammadelta and gammadelta subunit complexes in Spodoptera frugiperda Sf9 cells via the baculovirus infection system, resulting in formation of subunit subcomplexes, overview
-
expressed as a N-terminal GST fusion, expressed in B834 (DE3)pLyS cells at 18°C
-
rabbit muscle phosphorylase kinase catalytic domain of catalytic subunit, expressed in Escherichia coli
-
two hybrid rabbit DNA library screening using the yeast strain EGY48 and a C-terminal fragment of isozyme PhKalpha, expression of the enzyme and interaction partners in C2C12 cells
-
two-hybrid plasmid construction of fusions containing the PhK beta subunit and its deletion mutants and expression in a yeast two-hybrid system
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kemp, B.E.; Pearson, R.B.; House, M.
Pseudosubstrate-based peptide inhibitors
Methods Enzymol.
201
287-304
1991
Oryctolagus cuniculus, Homo sapiens, Mus musculus
da Cruz e Silva, E.F.; Cohen, P.T.
Isolation and sequence analysis of a cDNA clone encoding the entire catalytic subunit of phosphorylase kinase
FEBS Lett.
220
36-42
1987
Oryctolagus cuniculus (P00518), Oryctolagus cuniculus
Dasgupta, M.; Blumenthal, D.K.
Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory
J. Biol. Chem.
270
22283-22289
1995
Oryctolagus cuniculus, Oryctolagus cuniculus (P00518)
Dasgupta, M.; Honeycutt, T.; Blumenthal, D.K.
The gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin
J. Biol. Chem.
264
17156-17163
1989
Oryctolagus cuniculus (P00518)
Lowe, E.D.; Noble, M.E.; Skamnaki, V.T.; Oikonomakos, N.G.; Owen, D.J.; Johnson, L.N.
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition
EMBO J.
16
6646-6658
1997
Oryctolagus cuniculus (P00518)
Owen, D.J.; Noble, M.E.; Garman, E.F.; Papageorgiou, A.C.; Johnson, L.N.
Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product
Structure
3
467-482
1995
Oryctolagus cuniculus (P00518), Oryctolagus cuniculus
Reimann, E.M.; Titani, K.; Ericsson, L.H.; Wade, R.D.; Fischer, E.H.; Walsh, K.A.
Homology of the gamma subunit of phosphorylase b kinase with cAMP-dependent protein kinase
Biochemistry
23
4185-4192
1984
Oryctolagus cuniculus, Oryctolagus cuniculus (P00518)
Krebs, E.G.; Fischer, E.H.
Phosphorylase b-to-a converting enzyme of rabbit skeletal muscle
Biochim. Biophys. Acta
20
150-157
1956
Oryctolagus cuniculus
Krebs, E.G.; Love, D.S.; Bratvold, G.E.; Trayser, K.A.; Meyer, W.L.; Fischer, E.H.
Purification and properties of rabbit skeletal muscle phosphorylase b kinase
Biochemistry
3
1022-1033
1964
Oryctolagus cuniculus
Meyer, W.L.; Fischer, E.H.; Krebs, E.G.
Activation of skeletal muscle phosphorylase b kinase by calcium ion
Biochemistry
3
1033-1039
1964
Oryctolagus cuniculus
Graves, D.J.; Hayakawa, T.; Horvitz, R.A.; Beckman, E.; Krebs, E.G.
Studies on the subunit structure of trypsin-activated phosphorylase kinase
Biochemistry
12
580-585
1973
Oryctolagus cuniculus
Hayakawa, T.; Perkins, J.P.; Walsh, D.A.; Krebs, E.G.
Physiochemical properties of rabbit skeletal muscle phosphorylase kinase
Biochemistry
12
567-573
1973
Oryctolagus cuniculus
Hayakawa, T.; Perkins, J.P.; Krebs, E.G.
Studies of the subunit structure of rabbit skeletal muscle phosphorylase kinase
Biochemistry
12
574-580
1973
Oryctolagus cuniculus
Tu, J.I.; Graves, D.J.
Inhibition of the phosphorylase kinase catalyzed reaction by glucose-6-P
Biochem. Biophys. Res. Commun.
53
59-65
1973
Oryctolagus cuniculus
Yeoman, S.J.; Cohen, P.
The hormonal control of activity of skeletal muscle phosphorylase kinase. Phosphorylation of the enzyme at two sites in vivo in response to adrenalin
Eur. J. Biochem.
51
93-104
1975
Oryctolagus cuniculus
Pickett-Gies, C.A.; Walsh, D.A.
Phosphorylase kinase
The Enzymes, 3rd. Ed. (Boyer, P. D. , Krebs, E. G. , eds. )
17
395-456
1986
Bos taurus, Saccharomyces cerevisiae, Cavia porcellus, Gallus gallus, Oryctolagus cuniculus, Mus musculus, Rattus norvegicus, Squalus acanthias
-
Kilimann, M.; Heilmeyer, L.M.G.
The effect of Mg2+ on the Ca2+-binding properties of non-activated phosphorylase kinase
Eur. J. Biochem.
73
191-197
1977
Oryctolagus cuniculus
Cohen, P.; Burchell, A.; Foulkes, J.G.; Cohen, P.T.W.; Vanaman, T.C.; Nairn, A.C.
Identification of the Ca2+-dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase
FEBS Lett.
92
287-293
1978
Oryctolagus cuniculus
Sakai, K.; Matsumura, S.; Okimura, Y.; Yamamura, H.; Nishizuka, Y.
Liver glycogen phosphorylase kinase. Partial purification and characterization
J. Biol. Chem.
254
6631-6637
1979
Oryctolagus cuniculus
Vandenheede, J.R.; De Wulf, H.; Merlevede, W.
Liver phosphorylase b kinase. Cyclic-AMP-mediated activation and properties of the partially purified rat-liver enzyme
Eur. J. Biochem.
101
51-58
1979
Oryctolagus cuniculus, Rattus norvegicus
Carlson, G.M.; Bechtel, P.J.; Graves, D.J.
Chemical and regulatory properties of phosphorylase kinase and cyclic AMP-dependent protein kinase
Adv. Enzymol. Relat. Areas Mol. Biol.
50
41-115
1979
Calliphoridae, Oryctolagus cuniculus, Mus musculus, Squalus acanthias
Skuster, J.R.; Chan, K.F.J.; Graves, D.J.
Isolation and properties of the catalytically active gamma subunit of phosphorylase b kinase
J. Biol. Chem.
255
2203-2210
1980
Oryctolagus cuniculus
Pocinwong, S.; Blum, H.; Malencik, D.; Fisher, E.H.
Phosphorylase kinase from dogfish skeletal muscle. Purification and properties
Biochemistry
20
7219-7226
1981
Oryctolagus cuniculus, Squalus acanthias
Cohen, P.; Klee, C.B.; Picton, C.; Shenolikar, S.
Calcium control of muscle phosphorylase kinase through the combined action of calmodulin and troponin
Ann. N. Y. Acad. Sci.
356
151-161
1980
Oryctolagus cuniculus, Rattus norvegicus
King, M.M.; Carslon, G.M.
Synergistic effect of Ca2+ and Mg2+ in promoting an activity of phosphorylase kinase that is insensitive to ethylene glycol bis(beta-aminoethyl ether)-N,N-tetraacetic acid
Arch. Biochem. Biophys.
209
517-523
1981
Oryctolagus cuniculus
King, M.M.; Carslon, G.M.
Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions
J. Biol. Chem.
256
11058-11064
1981
Oryctolagus cuniculus
Chan, K.F.J.; Graves, D.J.
Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexes
J. Biol. Chem.
257
5948-5955
1982
Oryctolagus cuniculus
Chan, K.F.J.; Graves, D.J.
Rabbit skeletal muscle phosphorylase kinase. Interactions between subunits and influence of calmodulin on different complexes
J. Biol. Chem.
257
5956-5961
1982
Oryctolagus cuniculus
Kilimann, M.W.; Heilmeyer, L.M.G.
Multiple activities on phosphorylase kinase. 1. Characterization of three partial activities by their response to calcium ion, magnesium ion, pH, and ammonium chloride and effect of activation by phosphorylation and proteolysis
Biochemistry
21
1727-1734
1982
Oryctolagus cuniculus
Kilimann, M.W.; Heilmeyer, L.M.G.
Multiple activities on phosphorylase kinase. 2. Different specificities toward the protein substrates phosphorylase b, troponin, and phosphorylase kinase
Biochemistry
21
1735-1739
1982
Oryctolagus cuniculus
Chan, K.F.J.; Graves, D.J.
Isolation and physicochemical properties of active complexes of rabbit muscle phosphorylase kinase
J. Biol. Chem.
257
5939-5947
1982
Oryctolagus cuniculus
Picton, C.; Shenolikar, S.; Grand, R.; Cohen, P.
Calmodulin as an integral subunit of phosphorylase kinase from rabbit skeletal muscle
Methods Enzymol.
102
219-227
1983
Oryctolagus cuniculus
Cohen, P.
Phosphorylase kinase from rabbit skeletal muscle
Methods Enzymol.
99
243-250
1983
Oryctolagus cuniculus
Sul, H.S.; Dirden, B.; Angelos, K.L.; Hallenbeck, P.; Walsh, D.
Cardiac phosphorylase kinase: preparation and properties
Methods Enzymol.
99
250-259
1983
Bos taurus, Oryctolagus cuniculus
Chan, K.F.J.; Graves, D.J.
Separation of the subunits of muscle phosphorylase kinase
Methods Enzymol.
99
259-267
1983
Oryctolagus cuniculus
Graves, D.J.
Use of peptide substrates to study the specificity of phosphorylase kinase phosphorylation
Methods Enzymol.
99
268-278
1983
Oryctolagus cuniculus
Negami, A.; Sakai, K.; Kobayashi, T.; Tabuchi, H.; Nakamura, S.; Yamamura, H.
Two diverse effects of poly(L-lysine) on rabbit skeletal muscle phosphorylase kinase: stimulation of autophosphorylation and inhibition of its activity
FEBS Lett.
166
335-338
1984
Oryctolagus cuniculus
Crabb, J.W.; Heilmeyer, L.M.G.
High performance liquid chromatography purification and structural characterization of the subunits of rabbit muscle phosphorylase kinase
J. Biol. Chem.
259
6346-6350
1984
Oryctolagus cuniculus
Srivastava, A.K.
Inhibition of phosphorylase kinase, and tyrosine protein kinase activities by quercetin
Biochem. Biophys. Res. Commun.
131
1-5
1985
Oryctolagus cuniculus
Jennissen, H.P.; Petersen-von Gehr, J.K.H.; Botzet, G.
Activation and inhibition of phosphorylase kinase by monospecific antibodies against preparatively isolated alpha, beta and gamma subunits
Eur. J. Biochem.
147
619-630
1985
Oryctolagus cuniculus
Kee, S.M.; Graves, D.J.
Properties of the gamma subunit of phosphorylase kinase
J. Biol. Chem.
262
9448-9453
1987
Oryctolagus cuniculus
Paudel, H.K.; Carlson, G.M.
Inhibition of the catalytic subunit of phosphorylase kinase by its alpha/beta subunits
J. Biol. Chem.
262
11912-11915
1987
Oryctolagus cuniculus
Cox, D.E.; Meinke, M.H.; Edstrom, R.D.
Mechanism of calmodulin inhibition of cAMP-dependent protein kinase activation of phosphorylation kinase
Arch. Biochem. Biophys.
259
350-362
1987
Oryctolagus cuniculus
Crabb, J.W.; Harris, W.R.; Johnson, C.M.; Sotiroudis, T.G.; Kuhn, C.C.; Heilmeyer, L.M.G.
Electrophoretic purification of the alpha and beta subunits of phosphorylase kinase and evidence in support of the deduced amino acid sequences
Electrophoresis
11
133-140
1990
Oryctolagus cuniculus
Elliott, L.H.; Wilkinson, S.E.; Sedgwick, A.D.; Hill, C.H.; Lawton, G.; Davis, P.D.; Nixon, J.S.
K252a is a potent and selective inhibitor of phosphorylase kinase
Biochem. Biophys. Res. Commun.
171
148-154
1990
Oryctolagus cuniculus
Farrar, Y.J.K.; Carlson, G.M.
Kinetic characterization of the calmodulin-activated catalytic subunit of phosphorylase kinase
Biochemistry
30
10274-10279
1991
Oryctolagus cuniculus
Beleta, J.; Benedicto, P.; Gella, F.J.
Regulatory properties of rabbit liver phosphorylase kinase
Int. J. Biochem.
22
453-460
1990
Oryctolagus cuniculus
Beleta, J.; Benedicto, P.; Aymerich, P.; Gella, F.J.
Purification and characterization of native and proteolytic forms of rabbit liver phosphorylase kinase
Int. J. Biochem.
22
443-451
1990
Oryctolagus cuniculus
Paudel, H.K.; Carlson, G.M.
Functional and structural similarities between the inhibitory region of troponin I coded by exon VII and the calmodulin-binding regulatory region of the catalytic subunit of phosphorylase kinase
Proc. Natl. Acad. Sci. USA
87
7285-7289
1990
Oryctolagus cuniculus
Heilmeyer, L.M.G.
Molecular basis of signal integration in phosphorylase kinase
Biochim. Biophys. Acta
1094
168-174
1991
Oryctolagus cuniculus
Paudel, H.K.; Xu, Y.H.; Jarrett, H.W.; Carlson, G.M.
The model calmodulin-binding peptide melittin inhibits phosphorylase kinase by interacting with its catalytic center
Biochemistry
32
11865-11872
1993
Oryctolagus cuniculus
Cheng, A.; Fitzgerald, T.J.; Carlson, G.M.
Adenosine 5-diphosphate as an allosteric effector of phosphorylase kinase from rabbit skeletal muscle
J. Biol. Chem.
260
2535-2542
1985
Oryctolagus cuniculus
Huang, C.Y.F.; Yuan, C.J.; Blumenthal, D.K.; Graves, D.J.
Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit
J. Biol. Chem.
270
7183-7188
1995
Oryctolagus cuniculus
Owen, D.J.; Papageorgiou, A.C.; Garman, E.F.; Noble, M.E.M.; Johnson, L.N.
Expression, purification and crystallisation of phosphorylase kinase catalytic domain
J. Mol. Biol.
246
374-381
1995
Oryctolagus cuniculus
Kee, S.M.; Graves, D.J.
Isolation and properties of the active gamma subunit of phosphorylase kinase
J. Biol. Chem.
261
4732-4737
1986
Oryctolagus cuniculus
Xu, Y.H.; Wilkinson, D.A.; Carlson, G.M.
Divalent cations but not other activators enhance phosphorylase kinases affinity for glycogen phosphorylase
Biochemistry
35
5014-5021
1996
Oryctolagus cuniculus
Kumar, P.; Brushia, R.J.; Hoye, E.; Walsh, D.A.
Baculovirus-mediated overexpression of the phosphorylase b kinase holoenzyme and alpha gamma delta and gamma delta subcomplexes
Biochemistry
43
10247-10254
2004
Oryctolagus cuniculus, Rattus norvegicus (Q64649)
Chebotareva, N.A.; Andreeva, I.E.; Makeeva, V.F.; Livanova, N.B.; Kurganov, B.I.
Effect of molecular crowding on self-association of phosphorylase kinase and its interaction with phosphorylase b and glycogen
J. Mol. Recognit.
17
426-432
2004
Oryctolagus cuniculus
Hilder, T.L.; Carlson, G.M.; Haystead, T.A.; Krebs, E.G.; Graves, L.M.
Caspase-3 dependent cleavage and activation of skeletal muscle phosphorylase b kinase
Mol. Cell. Biochem.
275
233-242
2005
Oryctolagus cuniculus, Mus musculus
Priddy, T.S.; MacDonald, B.A.; Heller, W.T.; Nadeau, O.W.; Trewhella, J.; Carlson, G.M.
Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering
Protein Sci.
14
1039-1048
2005
Oryctolagus cuniculus
Nadeau, O.W.; Gogol, E.P.; Carlson, G.M.
Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase
Protein Sci.
14
914-920
2005
Oryctolagus cuniculus
Archila, S.; King, M.A.; Carlson, G.M.; Rice, N.A.
The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle
Biochem. Biophys. Res. Commun.
345
1592-1599
2006
Oryctolagus cuniculus
Makeeva, V.F.; Chebotareva, N.A.; Andreeva, I.E.; Livanova, N.B.; Kurganov, B.I.
Interaction of phosphorylase kinase from rabbit skeletal muscle with flavin adenine dinucleotide
Biochemistry (Moscow)
71
652-657
2006
Oryctolagus cuniculus
Nadeau, O.W.; Anderson, D.W.; Yang, Q.; Artigues, A.; Paschall, J.E.; Wyckoff, G.J.; McClintock, J.L.; Carlson, G.M.
Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides
J. Mol. Biol.
365
1429-1445
2007
Oryctolagus cuniculus
Priddy, T.S.; Price, E.S.; Johnson, C.K.; Carlson, G.M.
Single molecule analyses of the conformational substrates of calmodulin bound to the phosphorylase kinase complex
Protein Sci.
16
1017-1023
2007
Oryctolagus cuniculus
Priddy, T.S.; Middaugh, C.R.; Carlson, G.M.
Electrostatic changes in phosphorylase kinase induced by its obligatory allosteric activator Ca2+
Protein Sci.
16
517-527
2007
Oryctolagus cuniculus
Boulatnikov, I.G.; Nadeau, O.W.; Daniels, P.J.; Sage, J.M.; Jeyasingham, M.D.; Villar, M.T.; Artigues, A.; Carlson, G.M.
The regulatory beta subunit of phosphorylase kinase interacts with glyceraldehyde-3-phosphate dehydrogenase
Biochemistry
47
7228-7236
2008
Oryctolagus cuniculus, Mus musculus
Chebotareva, N.A.; Meremyanin, A.V.; Makeeva, V.F.; Livanova, N.B.; Kurganov, B.I.
Cooperative self-association of phosphorylase kinase from rabbit skeletal muscle
Biophys. Chem.
133
45-53
2008
Oryctolagus cuniculus
Nadeau, O.W.; Wyckoff, G.J.; Paschall, J.E.; Artigues, A.; Sage, J.; Villar, M.T.; Carlson, G.M.
CrossSearch, a user-friendly search engine for detecting chemically cross-linked peptides in conjugated proteins
Mol. Cell. Proteomics
7
739-749
2008
Oryctolagus cuniculus
Liu, W.; Priddy, T.S.; Carlson, G.M.
Physicochemical changes in phosphorylase kinase associated with its activation
Protein Sci.
17
2111-2119
2008
Oryctolagus cuniculus
Carriere, C.; Mornon, J.; Venien-Bryan, C.; Boisset, N.; Callebaut, I.
Calcineurin B-like domains in the large regulatory alpha /beta subunits of phosphorylase kinase
Proteins Struct. Funct. Bioinform.
71
1597-1606
2008
Oryza sativa (A2WRR1), Oryctolagus cuniculus (P12798), Oryctolagus cuniculus (P18688), Caenorhabditis elegans (P34335), Aedes aegypti (Q171G3), Tetraodon nigroviridis (Q4S8G1), Takifugu rubripes (Q9W6R1)
Chebotareva, N.A.; Meremyanin, A.V.; Makeeva, V.F.; Eronina, T.B.; Kurganov, B.I.
Glycogen phosphorylase b and phosphorylase kinase binding to glycogen under molecular crowding conditions. Inhibitory effect of FAD
Biochemistry
74
562-568
2009
Oryctolagus cuniculus
Venien-Bryan, C.; Jonic, S.; Skamnaki, V.; Brown, N.; Bischler, N.; Oikonomakos, N.G.; Boisset, N.; Johnson, L.N.
The structure of phosphorylase kinase holoenzyme at 9.9 A resolution and location of the catalytic subunit and the substrate glycogen phosphorylase
Structure
17
117-127
2009
Oryctolagus cuniculus (P00518)
Nadeau, O.W.; Lane, L.A.; Xu, D.; Sage, J.; Priddy, T.S.; Artigues, A.; Villar, M.T.; Yang, Q.; Robinson, C.V.; Zhang, Y.; Carlson, G.M.
Structure and location of the regulatory beta subunits in the (alphabetagammadelta)4 phosphorylase kinase complex
J. Biol. Chem.
287
36651-36661
2012
Oryctolagus cuniculus (P12798)
Lane, L.A.; Nadeau, O.W.; Carlson, G.M.; Robinson, C.V.
Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (alphabetagammadelt)4 phosphorylase kinase complex
Mol. Cell. Proteomics
11
1768-1776
2012
Oryctolagus cuniculus
Liu, W.; Nadeau, O.W.; Sage, J.; Carlson, G.M.
Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg2+
Protein Sci.
22
444-454
2013
Oryctolagus cuniculus
Hayes, J.; Skamnaki, V.; Archontis, G.; Lamprakis, C.; Sarrou, J.; Bischler, N.; Skaltsounis, A.; Zographos, S.; Oikonomakos, N.
Kinetics, in silico docking, molecular dynamics, and MM-GBSA binding studies on prototype indirubins, KT5720, and staurosporine as phosphorylase kinase ATP-binding site inhibitors: The role of water molecules examined
Proteins
79
703-719
2011
Oryctolagus cuniculus
Rimmer, M.A.; Artigues, A.; Nadeau, O.W.; Villar, M.T.; Vasquez-Montes, V.; Carlson, G.M.
Mass spectrometric analysis of surface-exposed regions in the hexadecameric phosphorylase kinase complex
Biochemistry
54
6887-6895
2015
Oryctolagus cuniculus (P18688 AND P12798), Oryctolagus cuniculus New Zealand White (P18688 AND P12798)
Herrera, J.E.; Thompson, J.A.; Rimmer, M.A.; Nadeau, O.W.; Carlson, G.M.
Activation of phosphorylase kinase by physiological temperature
Biochemistry
54
7524-7530
2015
Oryctolagus cuniculus (P18688 AND P12798), Oryctolagus cuniculus, Oryctolagus cuniculus New Zealand White (P18688 AND P12798)
Eronina, T.B.; Chebotareva, N.A.; Sluchanko, N.N.; Mikhaylova, V.V.; Makeeva, V.F.; Roman, S.G.; Kleymenov, S.Y.; Kurganov, B.I.
Dual effect of arginine on aggregation of phosphorylase kinase
Int. J. Biol. Macromol.
68
225-232
2014
Oryctolagus cuniculus (P18688 AND P12798)
Miyagawa, D.; Makino, Y.; Sato, M.
Sensitive, nonradioactive assay of phosphorylase kinase through measurement of enhanced phosphorylase activity towards fluorogenic dextrin
J. Biochem.
159
239-246
2016
Oryctolagus cuniculus (P18688 AND P12798)
Begum, J.; Skamnaki, V.T.; Moffatt, C.; Bischler, N.; Sarrou, J.; Skaltsounis, A.L.; Leonidas, D.D.; Oikonomakos, N.G.; Hayes, J.M.
An evaluation of indirubin analogues as phosphorylase kinase inhibitors
J. Mol. Graph. Model.
61
231-242
2015
Oryctolagus cuniculus, Oryctolagus cuniculus New Zealand White
Thompson, J.A.; Carlson, G.M.
The regulatory alpha and beta subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase
Biochem. Biophys. Res. Commun.
482
221-225
2017
Oryctolagus cuniculus
Chebotareva, N.A.; Eronina, T.B.; Roman, S.G.; Mikhaylova, V.V.; Kleymenov, S.Y.; Kurganov, B.I.
Kinetic regime of Ca2+ and Mg2+-induced aggregation of phosphorylase kinase at 40C
Int. J. Biol. Macromol.
138
181-187
2019
Oryctolagus cuniculus
Rimmer, M.A.; Nadeau, O.W.; Yang, J.; Artigues, A.; Zhang, Y.; Carlson, G.M.
The structure of the large regulatory alpha subunit of phosphorylase kinase examined by modeling and hydrogen-deuterium exchange
Protein Sci.
27
472-484
2018
Oryctolagus cuniculus
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