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Information on EC 2.7.11.19 - phosphorylase kinase and Organism(s) Mus musculus and UniProt Accession P07934
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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: Mus musculus
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, psk-c3, glycogen phosphorylase b kinase, kpi-2 kinase, phosphorylase kinase beta, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
-
dephosphophosphorylase kinase
-
-
-
-
Glycogen phosphorylase kinase
-
-
-
-
kinase, phosphorylase (phosphorylating)
-
-
-
-
Phosphorylase b kinase
PSK-C3
-
-
-
-
Phosphorylase b kinase
-
-
-
-
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 + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp
-
-
-
-
?
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp-Gly-Ile
-
-
-
-
?
ATP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
ADP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp
-
-
-
-
?
ATP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
ADP + Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp-Gly-Ile
-
i.e. phosphorylase b peptide (5-18)
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
-
phosphorylation is very slow, binds tightly to enzyme and acts as inhibitor for the phosphorylation of glycogen phosphorylase b
-
-
?
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 + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
presumably only in vitro
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
i.e. autophosphorylation and autoactivation
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
-
phosphorylation sites
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
phosphorylation site: Ser-14
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
rabbit skeletal muscle
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
-
ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
additional information
?
-
-
gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
-
-
?
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 b
ADP + glycogen phosphorylase a
-
key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
-
phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
Calmodulin
-
activation of recombinant gamma subunit at pH 6.8, slightly at pH 8.2
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Li+
Mg2+
phosphate
Ca2+
-
isolated delta-subunit from rabbit has 4 Ca2+-binding sites of which 2 are lost at high ionic strength and 2 Mg2+/Ca2+-binding sites that can bind either ion, treatment of gammadelta-subunit complex with EGTA with following centrifugation leads to Ca2+-independent catalytic activity
Mg2+
-
enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
-
allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
-
major role of Mg2+: cosubstrate in Mg2+-ATP complex
phosphate
-
contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
VIRDPYALPPLRRLIDAYAFRI
-
autoregulatory pseudosubstrate sequence of the gamma subunit, residues 333-354
additional information
-
no inhibition by glucose 1-phosphate (gammadelta subunit complex)
-
additional information
-
after treatment of differentiated C2C12 muscle myoblasts with apoptosis inducers staurosporine, N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine, doxorubicin, or UV radiation the enzyme alpha-subunit disappears
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
Catalytic subunit of cGMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
-
Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
Trypsin
-
strong, by limited proteolysis of alpha and beta subunits (not gamma)
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
additional information
-
the nonactivated enzyme is activated either by limited proteolysis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
ATP
-
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, nonactivated enzyme, pH 8.2
1.2
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
nonactivated enzyme, pH 8.2
3.5
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
-
activated enzyme, pH 8.2
additional information
additional information
-
pH-dependence of kinetic parameters
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
kinetic data for phosphorylase b
-
additional information
additional information
-
effects of holoenzyme dissociation
-
additional information
additional information
-
kinetic data for peptides derived from glycogen synthase
-
additional information
additional information
-
kinetic parameters for recombinant wild-type gamma subunit and its mutant form
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki values of the pseudosubstrates in nano- to micromolar range
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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_MOUSE
388
0
44960
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
additional information
additional information
-
amino acid sequence in regulatory domain of gamma subunit
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
-
subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
specific cleavage of caspase-3 at a specific cleavage site within the alpha-subunit in vivo
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a B2 repeat insertion generates alternate structures of the mouse muscle gamma-phosphorylase kinase gene
additional information
-
a B2 repeat insertion generates alternate structures of the mouse muscle gamma-phosphorylase kinase gene
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
Bender, P.K.; Emerson, C.P., Jr.
Skeletal muscle phosphorylase kinase catalytic subunit mRNAs are expressed in heart tissue but not in liver
J. Biol. Chem.
262
8799-8805
1987
Mus musculus (P07934)
Chamberlain, J.S.; VanTuinen, P.; Reeves, A.A.; Philip, B.A.; Caskey, C.T.
Isolation of cDNA clones for the catalytic gamma subunit of mouse muscle phosphorylase kinase: expression of mRNA in normal and mutant Phk mice
Proc. Natl. Acad. Sci. USA
84
2886-2890
1987
Mus musculus (P07934), Mus musculus
Maichele, A.J.; Farwell, N.J.; Chamberlain, J.S.
A B2 repeat insertion generates alternate structures of the mouse muscle gamma-phosphorylase kinase gene
Genomics
16
139-149
1993
Mus musculus (P07934), Mus musculus
Kawai, J.; Shinagawa, A.; Shibata, K.; Yoshino, M.; Itoh, M.; et al.
Functional annotation of a full-length mouse cDNA collection
Nature
409
685-690
2001
Mus musculus (Q9DB30)
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
-
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
Lanciotti, R.A.; Bender, P.K.
Baculovirus-directed expression of the gamma-subunit of phosphorylase kinase: purification and calmodulin dependence
Biochem. J.
299
183-189
1994
Mus musculus
Lanciotti, R.A.; Bender, P.K.
The gamma subunit of phosphorylase kinase contains a pseudosubstrate sequence
Eur. J. Biochem.
230
139-145
1995
Mus musculus
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
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
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