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Information on EC 2.7.11.19 - phosphorylase kinase and Organism(s) Bos taurus
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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: Bos taurus
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
dephosphophosphorylase kinase
-
-
-
-
Glycogen phosphorylase kinase
-
-
-
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kinase, phosphorylase (phosphorylating)
-
-
-
-
Phosphorylase b kinase
-
-
-
-
PSK-C3
-
-
-
-
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 + 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 + phosphorylase b
ADP + phosphorylase a
-
cosubstrate: Mg-ATP complex
-
-
?
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
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
stimulates phosphorylase conversion and autophosphorylation, 8 mol ADP per mol (alphabetagammadelta)4
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
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
phosphate
-
alpha and beta subunits are phosphorylated by protein kinases or autophosphorylation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
otherwise activating; total inhibition if ATP concentration exceeds that of divalent cation
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Catalytic subunit of cGMP-dependent protein kinase
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activation of nonactivated enzyme
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Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
adenosine 3',5'-monophosphate
-
cf. catalytic subunit of cAMP-dependent protein kinase
Catalytic subunit of cAMP-dependent protein kinase
-
activation of nonactivated enzyme
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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
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Catalytic subunit of cAMP-dependent protein kinase
-
by phosphorylation of alpha'
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Catalytic subunit of cAMP-dependent protein kinase
-
subunits, in the presence of ATP and Mg2+
-
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
additional information
additional information
-
influence on kinetic parameters, glycogen decreases Km-values 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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
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). PHKG2_BOVIN
406
0
46542
Swiss-Prot
other Location (Reliability: 1)
A0A3Q1M0J3_BOVIN
500
0
56264
TrEMBL
other Location (Reliability: 2)
Q29RI2_BOVIN
387
0
44837
TrEMBL
other Location (Reliability: 2)
A0A3Q1M4X9_BOVIN
399
0
45596
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
125000
-
4 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
130000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
134000
-
4 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
140000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, 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)
18000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
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)
46000
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
48000
-
4 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexadecamer
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 * 134000 + 4 * 125000 + 4 * 48000 + 4 * ?, (alphabetagammadelta)4, SDS-PAGE, the forth subunit is comigrating with calmodulin
hexadecamer
-
2 major isozymes in muscle: (alphabetagammadelta)4 and (alpha'betagammadelta)4
hexadecamer
-
4 * 140000 + 4 * 130000 + 4 * 46000 + 4 * 18000, (alphabetagammadelta)4, SDS-PAGE
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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Frozen in liquid N2, in 50 mM beta-glycerophosphate, pH 7, 2 mM EDTA, 1 mM DTT, 10% sucrose, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Cooper, R.H.; Sul, H.S.; McCullough, T.E.; Walsh, D.
Purification and properties of the cardiac isoenzyme of phosphorylase kinase
J. Biol. Chem.
255
11794-11801
1980
Bos taurus
Killilea, S.D.; Ky, N.M.
Purification and partial characterization of bovine heart phosphorylase kinase
Arch. Biochem. Biophys.
221
333-342
1983
Bos taurus
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