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Information on EC 2.7.11.17 - Ca2+/calmodulin-dependent protein kinase

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EC Tree
IUBMB Comments
Requires calmodulin and Ca2+ for activity. A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light chains and the microtubule-associated tau protein. Not identical with EC 2.7.11.18 (myosin-light-chain kinase) or EC 2.7.11.26 (tau-protein kinase).
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This record set is specific for:
UNIPROT: Q13555
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
caldesmon, cam kinase ii, camkiv, cam kinase, calcium/calmodulin-dependent protein kinase ii, calmodulin-dependent protein kinase, camkk2, calcium/calmodulin-dependent protein kinase, ca2+/calmodulin-dependent protein kinase, camk ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+/calmodulin-dependent protein kinase IIgamma
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calcium-calmodulin-dependent protein kinase II
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CaMK IIgamma
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CaMKIIdeltaA
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CaMKIIgamma
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CAKI
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-
-
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caldesmon
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-
-
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Calspermin
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-
-
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CAM kinase-GR
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-
-
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CMPK
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-
-
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kinase, caldesmon (phosphorylating)
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-
-
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kinase, microtubule-associated protein 2 (phosphorylating)
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-
-
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MAP kinase
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-
-
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MAP-2 kinase
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-
-
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MAP-2 protein serine kinase
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-
-
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microtubule associated protein kinase
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-
-
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microtubule-associated protein 2 kinase
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-
-
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peripheral plasma membrane protein CaMGUK
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
show the reaction diagram
sequential reaction mechanism in which all substrates bind to enzyme before any product is released. Binding of phospholamban to the enzyme decreases the affinity of the enzyme toward ATP
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:protein phosphotransferase (Ca2+/calmodulin-dependent)
Requires calmodulin and Ca2+ for activity. A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light chains and the microtubule-associated tau protein. Not identical with EC 2.7.11.18 (myosin-light-chain kinase) or EC 2.7.11.26 (tau-protein kinase).
CAS REGISTRY NUMBER
COMMENTARY hide
141467-21-2
-
93229-57-3
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97350-82-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + biotinylated Thr-Arg-Ser-Ala-Ile-Arg-Arg-Ala-Ser-Thr-Ile-Glu-Met-Pro-Gln-Gln-Ala-Arg-Gln
ADP + biotinylated Thr-Arg-Ser-Ala-Ile-Arg-Arg-Ala-Ser-phospho-Thr-Ile-Glu-Met-Pro-Gln-Gln-Ala-Arg-Gln
show the reaction diagram
biotinylated phospholamban Thr17 peptide substrate
-
-
?
ATP + phospholamban
ADP + phosphorylated phospholamban
show the reaction diagram
-
-
-
?
ATP + STAT3
ADP + phosphorylated STAT3
show the reaction diagram
-
-
-
?
additional information
?
-
CaMKIIgamma is activated by autophosphorylation
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-
?
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 + phospholamban
ADP + phosphorylated phospholamban
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
dependent on
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
product inhibition is best fit with an ordered Bi Bi mechanism in which phospholamban is the first substrate to bind and ADP is the last product to be released. Competitive inhibition versus ATP, uncompetitive inhibition versus phospholamban, isoenzyme CaMK IIgamma
biotinylated Thr-Arg-Ser-Ala-Ile-Arg-Arg-Ala-Ser-Thr-Ile-Glu-Met-Pro-Gln-Gln-Ala-Arg-Gln
product inhibition is best fit with an ordered Bi Bi mechanism in which phospholamban is the first substrate to bind and ADP is the last product to be released. Competitive inhibition versus phospholamban and ATP, isoenzyme CaMK IIgamma
imatinib
downregulates CaMKIIgamma autophosphorylation/activation
KN-93
inhibits CaMKII activity by blocking its interaction with the Ca2+/calmodulin complex
additional information
not inhibited by AG490, JAK3 inhibitor, PP1, PD98059, U0126, SB203580, wortmannin, LY294002, c-Jun NH2-terminal kinase inhibitor II, Raf 1 inhibitor, pho kinase inhibitor, RO-31-8220, Go6983, cucurbitacin I, Gleevec, and AMPK inhibitor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0128
ATP
pH 7.6, 25°C, isoenzyme CaMK IIgamma
0.0084
biotinylated Thr-Arg-Ser-Ala-Ile-Arg-Arg-Ala-Ser-Thr-Ile-Glu-Met-Pro-Gln-Gln-Ala-Arg-Gln
pH 7.6, 25°C, isoenzyme CaMK IIgamma
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.8
ATP
pH 7.6, 25°C, isoenzyme CaMK IIgamma
9.8
biotinylated Thr-Arg-Ser-Ala-Ile-Arg-Arg-Ala-Ser-Thr-Ile-Glu-Met-Pro-Gln-Gln-Ala-Arg-Gln
pH 7.6, 25°C, isoenzyme CaMK IIgamma
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
all CaMKII isoenzymes are implicated in a wide variety of cellular processes, which include a critical regulatory role in actin cytoskeletal assembly. All isoforms inhibit polymerization of actin in the order of decreasing effictivenes: CaMKIIbeta, CaMKIIgamma, CaMKIIdelta, CaMKIIalpha. Ca2+/CaM activation of all kinase isoforms produces a robust increase in actin polymerization that surpasses the rates of polymerization in the absence of kinase inhibition. The delta isoform of CaMKII bundles F-actin filaments
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KCC2G_HUMAN
558
0
62607
Swiss-Prot
other Location (Reliability: 1), Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in the LXSN retroviral expression vector M28248
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Si, J.; Collins, S.J.
Activated Ca2+/calmodulin-dependent protein kinase IIgamma is a critical regulator of myeloid leukemia cell proliferation
Cancer Res.
68
3733-3742
2008
Homo sapiens (Q13555)
Manually annotated by BRENDA team
Huynh, Q.K.; Pagratis, N.
Kinetic mechanisms of Ca++/calmodulin dependent protein kinases
Arch. Biochem. Biophys.
506
130-136
2011
Homo sapiens (Q13554), Homo sapiens (Q13555), Homo sapiens (Q13557), Homo sapiens (Q9UQM7)
Manually annotated by BRENDA team
Hoffman, L.; Farley, M.M.; Waxham, M.N.
Calcium-calmodulin-dependent protein kinase II isoforms differentially impact the dynamics and structure of the actin cytoskeleton
Biochemistry
52
1198-1207
2013
Rattus norvegicus (P08413), Rattus norvegicus (P11275), Homo sapiens (Q13555), Homo sapiens (Q13557)
Manually annotated by BRENDA team