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Information on EC 2.7.11.22 - cyclin-dependent kinase and Organism(s) Plasmodium falciparum and UniProt Accession Q07785

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IUBMB Comments
Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.
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This record set is specific for:
Plasmodium falciparum
UNIPROT: Q07785
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The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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ATP
+
a [protein]-(L-serine/L-threonine)
=
ADP
+
a [protein]-(L-serine/L-threonine) phosphate
+
a [protein]-(L-serine/L-threonine)
=
+
a [protein]-(L-serine/L-threonine) phosphate
Synonyms
cyclin-dependent kinase, cdk, p34cdc2, cdkl5, cdc2 kinase, cyclin-dependent kinase 5, cyclin-dependent kinase 2, cdc28, cyclin-dependent kinase 4, cyclin-dependent kinase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cell division control protein 2 homolog
-
Cyclin-dependent kinase pef1
-
-
-
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cyclin-dependent protein kinase
-
-
PHO85 homolog
-
-
-
-
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
active site amino acid sequences of PK5 and mrk
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:cyclin phosphotransferase
Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.
CAS REGISTRY NUMBER
COMMENTARY hide
150428-23-2
-
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
ADP + phosphorylated casein
show the reaction diagram
-
-
-
?
ATP + histone H1
ADP + phosphorylated histone H1
show the reaction diagram
-
-
-
?
ATP + C-terminal domain of RNA polymerase II
ADP + phosphorylated C-terminal domain of RNA polymerase II
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
autophosphorylation of Pfmrk, can not phosphorylate PfPK5
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyclin-1
-
regulatory subunit
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3Z)-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
-
IC50 for mrk is 0.0040 mM, and for PK5 0.15 mM, only weak inhibition of parasite strains D6 and W2 growth
(3Z)-3-[2-(4-bromophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
IC50 for mrk is 0.0035 mM, and for PK5 0.13 mM, only weak inhibition of parasite strains D6 and W2 growth
(3Z)-5-bromo-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
-
IC50 for mrk is 0.0031 mM, and for PK5 0.12 mM, only weak inhibition of parasite strains D6 and W2 growth
(3Z)-5-bromo-3-[2-(4-fluorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
IC50 for mrk is 0.0014 mM, and for PK5 0.19 mM, only weak inhibition of parasite strains D6 and W2 growth
(3Z)-5-bromo-3-[2-(4-methylphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
-
IC50 for mrk is 0.0029 mM, and for PK5 0.12 mM, only weak inhibition of parasite strains D6 and W2 growth
oxindole-based compounds
-
highly selective for mrk, IC50 of mrk is 0.0015 mM, low cross-reactivity with PK5 and human CDK1
-
additional information
-
molecular modeling of inhibitor-enzyme interactions
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyclin
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stimulates, does not affect autophosphorylation
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PfMAT1
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stimulates Pfmrk kinase activity in a cyclin-dependent manner, does not affect autophosphorylation
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.004
(3Z)-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
Plasmodium falciparum
-
IC50 for mrk is 0.0040 mM, and for PK5 0.15 mM, only weak inhibition of parasite strains D6 and W2 growth
0.0035
(3Z)-3-[2-(4-bromophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Plasmodium falciparum
-
IC50 for mrk is 0.0035 mM, and for PK5 0.13 mM, only weak inhibition of parasite strains D6 and W2 growth
0.0031
(3Z)-5-bromo-3-(2-oxo-2-phenylethylidene)-1,3-dihydro-2H-indol-2-one
Plasmodium falciparum
-
IC50 for mrk is 0.0031 mM, and for PK5 0.12 mM, only weak inhibition of parasite strains D6 and W2 growth
0.0014
(3Z)-5-bromo-3-[2-(4-fluorophenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Plasmodium falciparum
-
IC50 for mrk is 0.0014 mM, and for PK5 0.19 mM, only weak inhibition of parasite strains D6 and W2 growth
0.0029
(3Z)-5-bromo-3-[2-(4-methylphenyl)-2-oxoethylidene]-1,3-dihydro-2H-indol-2-one
Plasmodium falciparum
-
IC50 for mrk is 0.0029 mM, and for PK5 0.12 mM, only weak inhibition of parasite strains D6 and W2 growth
0.0015
oxindole-based compounds
Plasmodium falciparum
-
highly selective for mrk, IC50 of mrk is 0.0015 mM, low cross-reactivity with PK5 and human CDK1
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
present in approximately constant amounts throughout the intra-erythrocytic asexual reproductive stage of the life cycle
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F143L
-
4-10fold increase in Pfmrk activity, significant kinase activity in the absence of either cyclin or PfMAT1
S138K
-
4-10fold increase in Pfmrk activity, significant kinase activity in the absence of either cyclin or PfMAT1
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged mrk, His6-tagged PK5, and GST-tagged cyclin-1 from Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of His6-tagged mrk and His6-tagged PK5 in Escherichia coli, co-expression with GST-tagged cyclin-1
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
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the enzyme is a target for drug development in human malaria treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ross-Macdonald, P.B.; Graeser, R.; Kappes, B.; Franklin, R.; Williamson, D.H.
Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite Plasmodium falciparum
Eur. J. Biochem.
220
693-701
1994
Plasmodium falciparum (Q07785), Plasmodium falciparum
Manually annotated by BRENDA team
Woodard, C.L.; Li, Z.; Kathcart, A.K.; Terrell, J.; Gerena, L.; Lopez-Sanchez, M.; Kyle, D.E.; Bhattacharjee, A.K.; Nichols, D.A.; Ellis, W.; Prigge, S.T.; Geyer, J.A.; Waters, N.C.
Oxindole-based compounds are selective inhibitors of Plasmodium falciparum cyclin dependent protein kinases
J. Med. Chem.
46
3877-3882
2003
Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
Chen, Y.; Jirage, D.; Caridha, D.; Kathcart, A.K.; Cortes, E.A.; Dennull, R.A.; Geyer, J.A.; Prigge, S.T.; Waters, N.C.
Identification of an effector protein and gain-of-function mutants that activate Pfmrk, a malarial cyclin-dependent protein kinase
Mol. Biochem. Parasitol.
149
48-57
2006
Plasmodium falciparum
Manually annotated by BRENDA team