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EC Tree
IUBMB 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.
The taxonomic range for the selected organisms is: Mus musculus 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
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phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
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dephosphophosphorylase kinase
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-
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EC 2.7.1.38
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formerly, transferred to EC 2.7.11.19
Glycogen phosphorylase kinase
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-
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kinase, phosphorylase (phosphorylating)
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-
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phosphorylase B kinase gamma catalytic chain, testis/liver isoform
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Phosphorylase b kinase
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Phosphorylase b kinase
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phospho group transfer
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ATP:phosphorylase-b phosphotransferase
Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis---glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b [5]. The gamma subunit of the tetrameric enzyme is the catalytic subunit.
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ATP + a protein
ADP + a phosphoprotein
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-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
ATP + glycogen synthase
ADP + phosphoglycogen synthase
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-
-
-
?
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp
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-
-
-
?
ATP + Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
ADP + Lys-Arg-Lys-Gln-Ile-(phospho)Ser-Val-Asp-Gly-Ile
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-
-
-
?
ATP + Lys-Pro-Val-Thr-Arg-Glu-Ile-Ser-Ile-Arg-NH2
?
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i.e. S-peptide
-
-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
ATP + phosphorylase b
?
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involved in glycogenolysis
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
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
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-
-
-
?
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
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i.e. phosphorylase b peptide (5-18)
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-
?
ATP + synthetic peptides derived from phosphorylase b
?
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overview
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-
?
ATP + troponin I
ADP + phosphotroponin I
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phosphorylation site
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-
?
glyceraldehyde-3-phosphate dehydrogenase + ATP
?
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phosphorylation is very slow, binds tightly to enzyme and acts as inhibitor for the phosphorylation of glycogen phosphorylase b
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-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
additional information
?
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ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
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-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
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key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
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-
?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
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presumably only in vitro
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?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
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i.e. autophosphorylation and autoactivation
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?
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
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phosphorylation sites
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-
?
ATP + phosphorylase b
ADP + phosphorylase a
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-
-
-
?
ATP + phosphorylase b
ADP + phosphorylase a
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cosubstrate: Mg-ATP complex
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-
?
ATP + phosphorylase b
ADP + phosphorylase a
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main reaction
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-
?
ATP + phosphorylase b
ADP + phosphorylase a
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phosphorylation site: Ser-14
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-
?
ATP + phosphorylase b
ADP + phosphorylase a
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rabbit skeletal muscle
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-
?
ATP + phosphorylase b
ADP + phosphorylase a
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ATP can be replaced by 8-azido-ATP and its 2',3'-dialdehyde derivative, not by any other natural nucleotide triphosphate
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-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
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?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
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phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
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-
?
additional information
?
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substrate specificity
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-
?
additional information
?
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gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
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-
?
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ATP + a protein
ADP + a phosphoprotein
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-
-
-
?
ATP + glycogen phosphorylase b
ADP + glycogen phosphorylase a
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key enzyme in conversion of glycogen to glucose in skeletal muscle, regulation of enzyme activity during apoptosis, overview
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-
?
ATP + phosphorylase b
?
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involved in glycogenolysis
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-
?
ATP + phosphorylase b
ADP + phosphorylase a
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-
-
-
?
glycogen phosphorylase b + ATP
glycogen phosphorylase a + ADP
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phosphorylates and activates glycogen phosphorylase b, couples muscle contraction with glycogen breakdown
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-
?
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ADP
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activation
ADP
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stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
ADP
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allosteric effector
ATP
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ATP
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by autophosphorylation or protein kinase phosphorylation
ATP
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not alone, only in the presence of Mg2+ or Mn2+
ATP
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by phosphorylation of subunits alpha, beta not gamma
Calmodulin
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requirement
Calmodulin
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allosteric effector
Calmodulin
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additional activation
Calmodulin
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activation of recombinant gamma subunit at pH 6.8, slightly at pH 8.2
Calmodulin
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calmodulin containing enzyme i.e. tightly bound delta subunit
Calmodulin
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identical with the delta subunit
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Ca2+
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requirement
Ca2+
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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+
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synergism with Mg2+
Ca2+
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allosteric mechanism
Ca2+
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required for activity and activation
Ca2+
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Ca2+-dependent reaction
Li+
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activation
Mg2+
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Mg2+
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enzyme catalyzes its own phosphorylation (i.e. alpha and beta subunits, not gammadelta subunit complex) in the presence of MgATP2- and Ca2+
Mg2+
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synergism with Ca2+
Mg2+
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Mg2+ added in excess of ATP concentration stimulates
Mg2+
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allosteric effector, rabbit delta-subunit has two Mg2+/Ca2+-binding sites that can bind either ion
Mg2+
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major role of Mg2+: cosubstrate in Mg2+-ATP complex
Mg2+
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required for activity phosphorylation by (cAMP-dependent protein kinase)
phosphate
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contains 7.18-19 mol per mol (alphabetagammadelta)4 depending on phosphorylation status
phosphate
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requirement, phosphate containing enzyme
phosphate
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nonactivated enzyme is activated by phosphorylation
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glyceraldehyde-3-phosphate dehydrogenase
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Lys-Pro-Val-Thr-Arg-Glu-Ile-Val-Ile-Arg-NH2
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i.e. V-peptide
Phenothiazin
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blocks activation by extrinsic calmodulin
Polyaspartic acid
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pH 8.2
VIRDPYALPPLRRLIDAYAFRI
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autoregulatory pseudosubstrate sequence of the gamma subunit, residues 333-354
additional information
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additional information
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no inhibition by UDPglucose
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additional information
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no inhibition by glucose 1-phosphate (gammadelta subunit complex)
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additional information
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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
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additional information
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synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
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adenosine 3',5'-monophosphate
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cf. catalytic subunit of cAMP-dependent protein kinase
Ca2+-dependent protease
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casein protein kinase
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activation of nonactivated enzyme
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Catalytic subunit of cAMP-dependent protein kinase
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Catalytic subunit of cGMP-dependent protein kinase
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activation of nonactivated enzyme
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chymotrypsin
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proteolytic activation of nonactivated enzyme
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papain
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proteolytic activation of nonactivated enzyme
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Protein kinases
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activation of nonactivated enzyme, phosphorylation sites, mechanism
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troponin C
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activation
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Ca2+-dependent protease
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proteolytic activation of nonactivated enzyme
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Ca2+-dependent protease
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ir
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Ca2+-dependent protease
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or Ca2+-activating factor
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Catalytic subunit of cAMP-dependent protein kinase
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activation of nonactivated enzyme
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Catalytic subunit of cAMP-dependent protein kinase
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ATP cannot be replaced by 5'-AMP, 3'-AMP, 2',3'-AMP, CMP, CDP, CTP, UMP, UDP, UTP, GMP, GDP, GTP, IMP, IDP, ITP
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Catalytic subunit of cAMP-dependent protein kinase
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subunits, in the presence of ATP and Mg2+
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glycogen
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activation
glycogen
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allosteric effector, mechanism
heparin
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activation
Proteases
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Proteases
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proteolytic activation of nonactivated enzyme, mechanism
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Trypsin
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proteolytic activation of nonactivated enzyme
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Trypsin
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strong, by limited proteolysis of alpha and beta subunits (not gamma)
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Trypsin
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strong, by limited proteolysis of alpha and beta subunits
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additional information
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autophosphorylation
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additional information
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autophosphorylation
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additional information
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phosphorylation by protein kinases
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additional information
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phosphorylation by protein kinases
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additional information
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the nonactivated enzyme (i.e. Dephospho-enzyme)
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additional information
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allosteric effectors, overview
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additional information
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the nonactivated enzyme is activated either by limited proteolysis
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additional information
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the nonactivated enzyme is activated either by limited proteolysis
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0.9 - 1
Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
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pH 8.2
0.014 - 0.24
phosphorylase b
2
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp
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activated enzyme, pH 8.2
1.2 - 3.5
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
additional information
additional information
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0.03 - 0.037
ATP
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pH 8.5
0.03 - 0.037
ATP
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phosphorylase b
0.03 - 0.037
ATP
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activated enzyme, pH 7.5
0.03 - 0.037
ATP
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recombinant gamma subunit, pH 8.2
0.2
ATP
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Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, nonactivated enzyme, pH 8.2
0.22
ATP
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S-peptide, activated enzyme, pH 6.8
0.014
phosphorylase b
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recombinant gamma subunit, pH 6.8
0.019 - 0.02
phosphorylase b
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pH 7, activated enzyme
0.07 - 0.24
phosphorylase b
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-
0.19
phosphorylase b
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nonactivated enzyme, pH 8.2
0.21
S-peptide
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recombinant gamma subunit, pH 8.2
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0.28
S-peptide
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recombinant gamma subunit, pH 6.8
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1.2
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
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nonactivated enzyme, pH 8.2
3.5
Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp-Gly-Ile
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activated enzyme, pH 8.2
additional information
additional information
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kinetic studies
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additional information
additional information
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pH-dependence of kinetic parameters
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additional information
additional information
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kinetic properties, overview
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additional information
additional information
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kinetic properties, overview
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additional information
additional information
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kinetic data for phosphorylase b
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additional information
additional information
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kinetic data for phosphorylase b
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additional information
additional information
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effects of holoenzyme dissociation
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additional information
additional information
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kinetic data for peptides derived from glycogen synthase
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additional information
additional information
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kinetic parameters for recombinant wild-type gamma subunit and its mutant form
-
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additional information
additional information
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Ki values of the pseudosubstrates in nano- to micromolar range
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10.9
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truncated form of phosphorylase kinase gamma subunit
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additional information
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-
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SwissProt
brenda
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brenda
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differentiated muscle myoblasts
brenda
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muscle cells
brenda
additional information
-
isozyme distribution in different tissues
brenda
-
brenda
skeletal muscle
brenda
-
-
brenda
-
from back and leg
brenda
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-
-
-
brenda
-
-
brenda
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PHKG1_MOUSE
388
0
44960
Swiss-Prot
other Location (Reliability: 2 )
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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
-
amino acid composition
additional information
-
amino acid sequence in regulatory domain of gamma subunit
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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
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subunit alpha in isozymes that occur primarily in cells relying on glycolytic activity and alpha' in tissues with higher oxidative than glycolytic activity
additional information
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spatial arrangement of subunits
additional information
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spatial arrangement of subunits
additional information
-
the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
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proteolytic modification
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specific cleavage of caspase-3 at a specific cleavage site within the alpha-subunit in vivo
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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
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recombinant gamma-subunit, as expressed in Sf-9 cells
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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
-
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Kemp, B.E.; Pearson, R.B.; House, M.
Pseudosubstrate-based peptide inhibitors
Methods Enzymol.
201
287-304
1991
Oryctolagus cuniculus, Homo sapiens, Mus musculus
brenda
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)
brenda
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
brenda
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
brenda
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)
brenda
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
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brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda