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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: Rattus norvegicus 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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Glycogen phosphorylase kinase
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kinase, phosphorylase (phosphorylating)
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phosphorylase B kinase gamma catalytic chain, testis/liver
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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 + glycogen synthase
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decreases activity of this substrate
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?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
ATP + phosphorylase b
ADP + phosphorylase a
ATP + protein
ADP + phosphoprotein
in the presence of Ca2+/calmodulin, the isoform PhK-gamma T of the catalytic subunit is able to efficiently phosphorylate glycogen phosphorylase and convert it from an inactive to an active form
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ATP + synthetic peptides derived from phosphorylase b
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overview
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additional information
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ATP + casein
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?
ATP + casein
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very poor substrate
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?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
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?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
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inactivation of skeletal muscle glycogen synthase in the presence or absence of EGTA
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?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
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at high concentration, from rabbit skeletal muscle
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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 + phosphorylase b
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involved in glycogenolysis
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?
ATP + phosphorylase b
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stimulates glycogenolysis in skeletal muscle
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ATP + phosphorylase b
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regulates conversion of inactive phosphorylase b into active phosphorylase a
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?
ATP + phosphorylase b
ADP + phosphorylase a
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best substrate
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?
ATP + phosphorylase b
ADP + phosphorylase a
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liver (rat)
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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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liver
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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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?
additional information
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key enzyme in glycogen metabolism
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?
additional information
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histone H2B is no substrate
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?
additional information
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histone II-A is no substrate
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?
additional information
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phosvitin is no substrate
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additional information
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gammadelta complex catalyzes EGTA-insensitive phosphorylation of holoenzyme
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additional information
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no spontaneous or MnSO4-induced dephosphorylation of activated enzyme
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additional information
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no substrate is histone V-S
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additional information
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the enzyme performs autophosphorylation
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ATP + glycogen synthase
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decreases activity of this substrate
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ATP + protein
ADP + phosphoprotein
in the presence of Ca2+/calmodulin, the isoform PhK-gamma T of the catalytic subunit is able to efficiently phosphorylate glycogen phosphorylase and convert it from an inactive to an active form
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?
additional information
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key enzyme in glycogen metabolism
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?
ATP + phosphorylase b
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involved in glycogenolysis
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?
ATP + phosphorylase b
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stimulates glycogenolysis in skeletal muscle
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?
ATP + phosphorylase b
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regulates conversion of inactive phosphorylase b into active phosphorylase a
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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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calmodulin containing enzyme i.e. tightly bound delta subunit
Calmodulin
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in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation
Calmodulin
Ca2+-dependent binding, identical with the delta subunit
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Ca2+
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Ca2+
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activation, 0.0001-0.001 mM, inhibits above 0.001 mM
Ca2+
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required for efficient substrate binding of active and nonactivated enzyme and for maximal catalysis of active enzyme
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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delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction
Ca2+
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allosteric mechanism
Ca2+
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requirement (trypsin activation leads to loss of absolute requirement)
Ca2+
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required for activity and activation
Ca2+
activates, dependent on, required for binding of calmodulin
Mg2+
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requirement
Mg2+
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free Mg2+ inhibits activated enzyme
Mg2+
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free Mg2+ stimulates (nonactivated enzyme)
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)
Mg2+
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required for activity and activation (by autophosphorylation)
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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Antibodies to delta subunit of phosphorylase kinase
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Antibodies to rat testis calmodulin
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calmodulin or troponin (the latter at high concentrations) reverses
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ATP
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free ATP, reversible
Phenothiazin
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blocks activation by extrinsic calmodulin
additional information
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EGTA
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Mg2+
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in excess of ATP
Mg2+
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free Mg2+, only activated enzyme, reversible
Mg2+
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nonactivated and activated enzyme
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adenosine 3',5'-monophosphate
Artificial thin filaments
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activation, made by mixing actin, tropomyosin and troponin complex
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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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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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Proteases
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proteolytic activation of nonactivated enzyme, mechanism
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Protein kinases
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activation of nonactivated enzyme, phosphorylation sites, mechanism
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adenosine 3',5'-monophosphate
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cAMP mediated activation
adenosine 3',5'-monophosphate
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cf. catalytic subunit of cAMP-dependent protein kinase
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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at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each
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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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Catalytic subunit of cGMP-dependent protein kinase
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not
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Catalytic subunit of cGMP-dependent protein kinase
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activation of nonactivated enzyme
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glycogen
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activation
glycogen
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allosteric effector, mechanism
troponin C
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activation
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troponin C
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presumably key event in vivo, coupling glycogenolysis and muscle contraction
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troponin C
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can replace extrinsic calmodulin
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Trypsin
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proteolytic activation of nonactivated enzyme
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Trypsin
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accompanied by loss of absolute requirement for Ca2+, activates holoenzyme and alphagammadelta subunit complex, not gammadelta complex
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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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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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no activation by parvalbumin
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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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0.019 - 0.24
phosphorylase b
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
0.07
MgATP2-
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activated rabbit skeletal muscle enzyme, pH 8.2
0.08
MgATP2-
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activated rabbit skeletal muscle enzyme, pH 6
0.1
MgATP2-
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nonactivated rabbit skeletal muscle enzyme, pH 6
0.019 - 0.02
phosphorylase b
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pH 7, activated enzyme
0.07 - 0.24
phosphorylase b
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additional information
additional information
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additional information
additional information
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kinetic studies
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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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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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influence of Ca2+
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additional information
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additional information
activity of purified native and recombinant enzymes and subunit subcomplexes at different pH
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7
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nonactivated enzyme
7
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above, activated enzyme
additional information
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activated enzyme has a higher pH-optimum than nonactivated enzyme
additional information
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influence of activation by protein kinase on pH-activity profile
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6.2 - 7.6
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about half-maximal activity at pH 6.2 and 7.6, nonactivated enzyme
additional information
activity of purified native and recombinant enzymes and subunit subcomplexes at different pH, the latter show higher activity at pH 6.8, while the native enzyme shows higher activity at pH 8.2
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30
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assay at
30
autophosphorylation reaction at
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SwissProt
brenda
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soleus muscle
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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together with other enzymes of glycogen metabolism linked together on glycogen particles
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brenda
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PHKG1_RAT
388
0
45015
Swiss-Prot
other Location (Reliability: 2 )
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1300000
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rat, gel filtration
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hexadecamer
alpha4beta4gamma4delta4, alpha and beta subunits are regulatory, delta is calmodulin, and the gamma subunit is catalytic
hexadecamer
(alphabetagammadelta)4
additional information
subunit composition of alpha4beta4gamma4delta4, in which the alpha and beta subunits are regulatory, delta is calmodulin, and the gamma subunit is catalytic
additional information
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the delta subunit is firmly bound to holoenzyme whereas delta' subunit (i.e. calmodulin) is bound only in the presence of Ca2+
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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the delta subunit is very similar to calmodulin but a tightly bound integral component of holoenzyme
additional information
the delta subunit is identical with calmodulin
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phosphoprotein
regulation by de-/phosphorylation performed by cAMP-dependent protein kinase, EC 2.7.11.11
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unstable in dilute solutions
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-20°C, in 0.25 M sucrose, 0.1 M Tris-HCl, 0.5 mM DTT, pH 7.4, 50% glycerol, several weeks
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-70°C, in 20 mM triethanolamine-HCl, pH 7.5, 20% v/v glycerol, 1 mM DTT, 0.02% NaN3, stable
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recombinant holoenzyme and enzyme subunit subcomplexes from Sf9 insect cells
to near homogeneity from glycogen-rich pellet, from 1000 rats
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nucleotide sequence of cDNA encoding the catalytic subunit
PhK-gamma T isoform of phosphorylase kinase catalytic subunit
subcloning of subunits in Escherichia coli, overexpression of the soluble holoenzyme and of soluble trimeric alphagammadelta and dimeric gammadelta subunit subcomplexes, as well as coexpression with the beta subunit of the rabbit enzyme also resulting in subunit complex formation, in Spodoptera frugiperda Sf9 cells via the baculovirus infection system
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Cawley, K.C.; Akita, C.G.; Angelos, K.L.; Walsh, D.A.
Characterization of the gene for rat phosphorylase kinase catalytic subunit
J. Biol. Chem.
268
1194-1200
1993
Rattus norvegicus (P13286)
brenda
Cawley, K.C.; Ramachandran, C.; Gorin, F.A.; Walsh, D.A.
Nucleotide sequence of cDNA encoding the catalytic subunit of phosphorylase kinase from rat soleus muscle
Nucleic Acids Res.
16
2355-2356
1988
Rattus norvegicus (P13286)
brenda
Calalb, M.B.; Fox, D.T.; Hanks, S.K.
Molecular cloning and enzymatic analysis of the rat homolog of "PhK-gamma T," an isoform of phosphorylase kinase catalytic subunit
J. Biol. Chem.
267
1455-1463
1992
Rattus norvegicus (P31325)
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
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
brenda
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
brenda
Chrisman, T.D.; Jordan, J.E.; Exton, J.H.
Purification of rat liver phosphorylase kinase
J. Biol. Chem.
257
10798-10804
1982
Rattus norvegicus
brenda
Chrisman, T.D.; Sobo, G.E.; Exton, J.H.
The Mg2+ requirements of nonactivated and activated rat liver phosphorylase kinase. Inhibition of the activated form by free Mg2+
FEBS Lett.
167
295-300
1984
Rattus norvegicus
brenda
Doorneweerd, D.D.; Tan, A.W.H.; Nuttall, F.Q.
Liver phosphorylase kinase: characterization of two interconvertible forms and partial purification of phosphorylase kinase a
Mol. Cell. Biochem.
47
45-53
1982
Rattus norvegicus
brenda
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)
brenda