Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.11.19 - phosphorylase kinase and Organism(s) Rattus norvegicus and UniProt Accession P13286

for references in articles please use BRENDA:EC2.7.11.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Rattus norvegicus
UNIPROT: P13286
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
-
dephosphophosphorylase kinase
-
-
-
-
Glycogen phosphorylase kinase
-
-
-
-
kinase, phosphorylase (phosphorylating)
-
-
-
-
Phosphorylase b kinase
phosphorylase B kinase gamma catalytic chain, testis/liver
-
PSK-C3
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9001-88-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + casein
?
show the reaction diagram
ATP + glycogen synthase
?
show the reaction diagram
-
decreases activity of this substrate
-
-
?
ATP + glycogen synthase
ADP + phosphoglycogen synthase
show the reaction diagram
ATP + nonactivated phosphorylase kinase
ADP + activated phosphorylase kinase
show the reaction diagram
ATP + phosphorylase b
?
show the reaction diagram
ATP + phosphorylase b
ADP + phosphorylase a
show the reaction diagram
ATP + protein
ADP + phosphoprotein
show the reaction diagram
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
-
-
?
ATP + synthetic peptides derived from phosphorylase b
?
show the reaction diagram
-
overview
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + glycogen synthase
?
show the reaction diagram
-
decreases activity of this substrate
-
-
?
ATP + phosphorylase b
?
show the reaction diagram
ATP + protein
ADP + phosphoprotein
show the reaction diagram
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
-
-
?
additional information
?
-
key enzyme in glycogen metabolism
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Antibodies to delta subunit of phosphorylase kinase
-
-
-
Antibodies to rat testis calmodulin
-
calmodulin or troponin (the latter at high concentrations) reverses
-
ATP
-
free ATP, reversible
Mn2+
-
free Mn2+
Phenothiazin
-
blocks activation by extrinsic calmodulin
additional information
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
adenosine 3',5'-monophosphate
Artificial thin filaments
-
activation, made by mixing actin, tropomyosin and troponin complex
-
Ca2+-dependent protease
-
casein protein kinase
-
activation of nonactivated enzyme
-
Catalytic subunit of cAMP-dependent protein kinase
-
Catalytic subunit of cGMP-dependent protein kinase
-
chymotrypsin
-
proteolytic activation of nonactivated enzyme
-
glycogen
papain
-
proteolytic activation of nonactivated enzyme
-
Proteases
-
proteolytic activation of nonactivated enzyme, mechanism
-
Protein kinases
-
activation of nonactivated enzyme, phosphorylation sites, mechanism
-
troponin C
-
Trypsin
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.05
ATP
0.07 - 0.1
MgATP2-
0.019 - 0.24
phosphorylase b
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
nonactivated enzyme
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 7.6
-
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
soleus muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHKG1_RAT
388
0
45015
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1000000
-
rat
1300000
-
rat, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexadecamer
alpha4beta4gamma4delta4, alpha and beta subunits are regulatory, delta is calmodulin, and the gamma subunit is catalytic
hexadecamer
(alphabetagammadelta)4
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
regulation by de-/phosphorylation performed by cAMP-dependent protein kinase, EC 2.7.11.11
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in dilute solutions
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 0.25 M sucrose, 0.1 M Tris-HCl, 0.5 mM DTT, pH 7.4, 50% glycerol, several weeks
-
-70°C, in 20 mM triethanolamine-HCl, pH 7.5, 20% v/v glycerol, 1 mM DTT, 0.02% NaN3, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant holoenzyme and enzyme subunit subcomplexes from Sf9 insect cells
to near homogeneity from glycogen-rich pellet, from 1000 rats
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chrisman, T.D.; Jordan, J.E.; Exton, J.H.
Purification of rat liver phosphorylase kinase
J. Biol. Chem.
257
10798-10804
1982
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team