Information on EC 2.7.4.14 - UMP/CMP kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.7.4.14
-
RECOMMENDED NAME
GeneOntology No.
UMP/CMP kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + UMP = ADP + UDP
show the reaction diagram
-
-
-
-
ATP + UMP = ADP + UDP
show the reaction diagram
formation of a ternary complex, addition of substrates is random
-
ATP + UMP = ADP + UDP
show the reaction diagram
reaction proceeds by a sequential mechanism, a ternary complex of the enzyme with both substrates is formed as the central intermediate in the reaction
-
ATP + UMP = ADP + UDP
show the reaction diagram
reaction mechanism is sequential and nonequilibrium in nature, substrates bind to the enzyme in a random order, substrate binding is cooperative
-
ATP + UMP = ADP + UDP
show the reaction diagram
the mechanism is analogous to the phosphoryl transfer mechanism in cAMP-dependent protein kinase that phosphorylates the hydroxyl groups of serine residues
-
ATP + UMP = ADP + UDP
show the reaction diagram
random bi-bi mechanism
-, O04905
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
phospho group transfer
-
-
PATHWAY
KEGG Link
MetaCyc Link
CMP phosphorylation
-
pyrimidine deoxyribonucleotide phosphorylation
-
UTP and CTP de novo biosynthesis
-
Pyrimidine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
ATP:CMP(UMP) phosphotransferase
This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP:UMP-CMP phosphotransferase
-
-
-
-
CMP kinase
-
-
-
-
CMPK
-
-
-
-
CMPK
-
-
CTP:CMP phosphotransferase
-
-
-
-
cytidine monophosphate kinase
-
-
-
-
cytidine monophosphate kinase
-
-
cytidylate kinase
-
-
-
-
cytidylate kinase
-
-
cytidylate kinase
P30085
-
deoxycytidine kinase
-
-
MssA protein
-
-
-
-
nucleoside monophosphate kinase
-
-
nucleoside monophosphate kinase
Q5EBM0
-
P25
-
-
-
-
pyrimidine nucleoside monophosphate kinase
-
-
-
-
UCK
-
-
-
-
UCK
P30085
-
UMP-CMP kinase
-
-
-
-
UMP-CMP kinase
-
-
UMP-CMP kinase
P30085
-
UMP-CMP kinase 2
Q5EBM0
-
UMP-CMPK2
Q5EBM0
-
UMP/CMP kinase
-
-
-
-
UMP/CMP kinase
P20425
-
UMP/CMP kinase
-
-
UMPK
-
-
-
-
uridine monophosphate/cytidine monophosphate kinase
P20425
-
kinase, cytidylate (phosphorylating)
-
-
-
-
additional information
P20425
the enzyme belongs to the family of nucleoside monophosphate, NMP, kinases. These enzymes not only show high sequence and structure similarities but also share the alpha/beta-fold, a very common protein topology
additional information
Q5EBM0
mitochondrial UMP-CMPK2 belongs to a distinct nucleoside monophosphate kinase family, closer to thymidylate kinase than to cytosolic UMP-CMP kinase
CAS REGISTRY NUMBER
COMMENTARY
37278-21-0
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (S)-1-(3-hydroxy-2-phosphonylmethoxypropyl) cytosine
ADP + (S)-1-(3-hydroxy-2-phosphonylmethoxypropyl) cytosine
show the reaction diagram
-
Cidofovir
-
-
-
ATP + 1-beta-D-arabinofuranosylcytosine
ADP + ?
show the reaction diagram
P30085
-
-
-
?
ATP + 2',2'-difluorodeoxycytidine
ADP + ?
show the reaction diagram
P30085
-
-
-
?
ATP + 2'-azido-CMP
ADP + 2'-azido-CDP
show the reaction diagram
-
4fold higher activity with 2'-azido-dCMP than with 2'-azido-CMP
-
-
?
ATP + 2'-azido-dCMP
ADP + 2'-azido-dCDP
show the reaction diagram
-
4fold higher activity with 2'-azido-dCMP than with 2'-azido-CMP
-
-
?
ATP + 2'-azido-dUMP
ADP + 2'-azido-dUDP
show the reaction diagram
-
similar activity with 2'-azido-UMP and 2'-azido-dUMP
-
-
?
ATP + 2'-azido-UMP
ADP + 2'-azido-UDP
show the reaction diagram
-
similar activity with 2'-azido-UMP and 2'-azido-dUMP
-
-
?
ATP + AMP
ADP + ADP
show the reaction diagram
-
-
-
-
r
ATP + AMP
ADP + ADP
show the reaction diagram
P30085
-
-
-
r
ATP + ara-CMP
ADP + ara-CDP
show the reaction diagram
P30085
-
-
-
?
ATP + ara-CMP
ADP + ara-CDP
show the reaction diagram
-
-
-
-
?
ATP + ara-CMP
ADP + ara-CDP
show the reaction diagram
-
-
-
-
?
ATP + beta-D-2',3'-dideoxy-CMP + H2O
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + beta-D-2'-azido-2'-dCMP
ADP + beta-D-2'-azido-2'-dCDP
show the reaction diagram
-
-
-
-
?
ATP + beta-D-2'-azido-2'-dUMP
ADP + beta-D-2'-azido-2'-dUDP
show the reaction diagram
-
-
-
-
?
ATP + beta-L-2',3'-dideoxy-2',3'-didehydro-5-fluoro-CMP
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
ADP + beta-L-2',3'-dideoxy-3'-thiacytidine diphosphate
show the reaction diagram
-
-
-
-
?
ATP + beta-L-2',3'-dideoxy-CMP + H2O
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + beta-L-2'-azido-2'-dCMP
ADP + beta-L-2'-azido-2'-dCDP
show the reaction diagram
-
-
-
-
?
ATP + beta-L-2'-azido-2'-dUMP
ADP + beta-L-2'-azido-2'-dUDP
show the reaction diagram
-
-
-
-
?
ATP + beta-L-dioxolane-cytidine
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
P30085
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
r
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-, O04905
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
Q5EBM0
low activity
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
the enzyme is required during rapid cell growth
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
the enzyme plays a crucial role in the formation of UDP, CDP and dCDP which are required for cellular nucleic acid synthesis
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
the enzyme catalyses an important step in the phosphorylation of UTP, CTP and dCTP. It is also involved in the necessary phosphorylation by cellular kinases of nucleoside analogs used in antiviral therapies
-
-
?
ATP + D-CMP
ADP + D-CDP
show the reaction diagram
-
-
-
-
?
ATP + D-dCMP
ADP + D-dCDP
show the reaction diagram
-
-
-
-
?
ATP + D-dUMP
ADP + D-dUDP
show the reaction diagram
-
-
-
-
?
ATP + D-UMP
ADP + D-UDP
show the reaction diagram
-
-
-
-
?
ATP + dAMP
ADP + dADP
show the reaction diagram
P30085
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
P30085
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
Q5EBM0
high activity
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
no evidence for reversal of the reaction
-
?, ir
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
the enzyme plays a crucial role in the formation of UDP, CDP and dCDP which are required for cellular nucleic acid synthesis
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
the enzyme catalyses an important step in the phosphorylation of UTP, CTP and cCTP. It is also involved in the necessary phosphorylation by cellular kinases of nucleoside analogs used in antiviral therapies
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
higher activity with the D-enantiomer compared to the L-enantiomer
-
-
?
ATP + dUMP
ADP + dUDP
show the reaction diagram
-
-
-
-
?
ATP + dUMP
ADP + dUDP
show the reaction diagram
-
-
-
-
?
ATP + dUMP
ADP + dUDP
show the reaction diagram
P30085
-
-
-
?
ATP + dUMP
ADP + dUDP
show the reaction diagram
Q5EBM0
best substrate
-
-
?
ATP + dUMP
ADP + dUDP
show the reaction diagram
-
no activity with CDP, dTMP, AMP, GMP
-
-
?
ATP + dUMP
ADP + dUDP
show the reaction diagram
-
higher activity with the D-enantiomer compared to the L-enantiomer
-
-
?
ATP + gemcitabine
ADP + gemcitabine monophosphate
show the reaction diagram
P30085
activity of DCK
i.e. 2',2'-difluorodeoxycytidine 5'-monophosphate
-
?
ATP + gemcitabine monophosphate
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + gemcitabine phosphate
ADP + gemcitabine diphosphate
show the reaction diagram
P30085
activity of CMPK
i.e. 2',2'-difluorodeoxycytidine 5'-diphosphate
-
?
ATP + L-(-)-2',3'-dideoxy-3'-thia-CMP
ADP + L-(-)-2',3'-dideoxy-3'-thia-CDP
show the reaction diagram
-
-
-
-
?
ATP + L-(-)-2',3'-dideoxy-3'-thia-CMP
ADP + L-(-)-2',3'-dideoxy-3'-thia-CDP
show the reaction diagram
-
-
-
-
-
ATP + L-(-)-2',3'-dideoxy-5-fluoro-3'-thia-CMP
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + L-3TCMP
ADP + L-3TCMP
show the reaction diagram
-
-
-
-
?
ATP + L-CMP
ADP + L-CDP
show the reaction diagram
-
-
-
-
-
ATP + L-CMP
ADP + L-CDP
show the reaction diagram
-
poor substrate
-
-
?
ATP + L-dCMP
ADP + L-dCDP
show the reaction diagram
-
-
-
-
-
ATP + L-dCMP
ADP + L-dCDP
show the reaction diagram
-
slower phosphorylation than the D-enantiomers
-
-
?
ATP + L-dUMP
ADP + L-dUDP
show the reaction diagram
-
-
-
-
-
ATP + L-dUMP
ADP + L-dUDP
show the reaction diagram
-
slower phosphorylation than the D-enantiomers
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
P30085
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
r
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-, O04905
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
-
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
Q5EBM0
low activity
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
the enzyme plays a crucial role in the formation of UDP, CDP and dCDP which are required for cellular nucleic acid synthesis
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
the enzyme catalyses an important step in the phosphorylation of UTP, CTP and cCTP. It is also involved in the necessary phosphorylation by cellular kinases of nucleoside analogs used in antiviral therapies
-
-
?
CTP + CMP
CDP + CDP
show the reaction diagram
-
-
-
-
?
CTP + CMP
CDP + CDP
show the reaction diagram
-
-
-
-
?
dATP + CMP
dADP + CDP
show the reaction diagram
-
-
-
-
?
dATP + CMP
dADP + CDP
show the reaction diagram
-
-
-
-
?
dATP + dCMP
dADP + dCDP
show the reaction diagram
-
-
-
-
?
dATP + UMP
dADP + ADP
show the reaction diagram
-
-
-
-
?
dATP + UMP
dADP + ADP
show the reaction diagram
-
-
-
-
r
dATP + UMP
dADP + ADP
show the reaction diagram
-
-
-
-
?
dATP + UMP
dADP + ADP
show the reaction diagram
-
dATP shows 10% of the activity with ATP
-
-
?
dCTP + CMP
dCDP + CDP
show the reaction diagram
-
-
-
-
?
dCTP + dCMP
dCDP + dCDP
show the reaction diagram
-
-
-
-
?
dCTP + UMP
dGDP + UDP
show the reaction diagram
-
-
-
-
?
dGTP + CMP
dGDP + CDP
show the reaction diagram
-
-
-
-
?
dGTP + CMP
dGDP + CDP
show the reaction diagram
-
-
-
-
?
dGTP + UMP
dGDP + UDP
show the reaction diagram
-
-
-
-
?
dTTP + CMP
dTDP + CDP
show the reaction diagram
-
-
-
-
?
dUTP + CMP
dUDP + CDP
show the reaction diagram
-
-
-
-
?
GTP + CMP
GDP + CDP
show the reaction diagram
-
-
-
-
?
GTP + CMP
GDP + CDP
show the reaction diagram
-
-
-
-
?
GTP + dCMP
GDP + dCDP
show the reaction diagram
-
-
-
-
?
GTP + UMP
GDP + UDP
show the reaction diagram
-
-
-
-
?
ITP + CMP
IDP + CDP
show the reaction diagram
-
-
-
-
?
TTP + CMP
TDP + CDP
show the reaction diagram
-
-
-
-
?
TTP + dCMP
TDP + dCMP
show the reaction diagram
-
-
-
-
?
TTP + UMP
TDP + UDP
show the reaction diagram
-
-
-
-
?
UTP + CMP
UDP + CDP
show the reaction diagram
-
-
-
-
?
XTP + CMP
XDP + CDP
show the reaction diagram
-
-
-
-
?
ITP + UMP
IDP + UDP
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
formation of a ternary complex, addition of substrates is random
-
-
-
additional information
?
-
-
the UMP-CMP kinase has a relaxed enantiospecificity for the nucleoside monophosphate acceptor site, but it is restricted to D-nucleotides at the donor site
-
-
-
additional information
?
-
-
the enzyme is involved in the phosphorylation of nucleic acid precursors, and is critical in the ribo- and deoxyribonucleoside salvage pathway, as well as the anabolic phosphorylation of nucleoside analogues used in viral and anticancer therapies, e.g. cidofovir, which is activated by the enzyme, overview
-
-
-
additional information
?
-
Q5EBM0
UMP-CMPK2 may have other functions in addition to the supply of substrates for mtDNA synthesis, it is highly expressed in leukemia cells, in bone marrow, and is tightly correlated with macrophage activation and inflammatory response
-
-
-
additional information
?
-
-
substrate/product binding site determination and kinetics using MABA-CDP in a competition assay, overview
-
-
-
additional information
?
-
-
the enzyme shows enantioselectivity, acceptor-binding site structure of human UMP-CMP kinase in the closed form or in ligand-bound forms, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
the enzyme is required during rapid cell growth
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
the enzyme plays a crucial role in the formation of UDP, CDP and dCDP which are required for cellular nucleic acid synthesis
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
the enzyme catalyses an important step in the phosphorylation of UTP, CTP and dCTP. It is also involved in the necessary phosphorylation by cellular kinases of nucleoside analogs used in antiviral therapies
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
-
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
the enzyme plays a crucial role in the formation of UDP, CDP and dCDP which are required for cellular nucleic acid synthesis
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
the enzyme catalyses an important step in the phosphorylation of UTP, CTP and cCTP. It is also involved in the necessary phosphorylation by cellular kinases of nucleoside analogs used in antiviral therapies
-
-
?
ATP + dCMP
ADP + dCDP
show the reaction diagram
-
higher activity with the D-enantiomer compared to the L-enantiomer
-
-
?
ATP + dUMP
ADP + dUDP
show the reaction diagram
-
higher activity with the D-enantiomer compared to the L-enantiomer
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
the enzyme plays a crucial role in the formation of UDP, CDP and dCDP which are required for cellular nucleic acid synthesis
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
the enzyme catalyses an important step in the phosphorylation of UTP, CTP and cCTP. It is also involved in the necessary phosphorylation by cellular kinases of nucleoside analogs used in antiviral therapies
-
-
?
additional information
?
-
-
the enzyme is involved in the phosphorylation of nucleic acid precursors, and is critical in the ribo- and deoxyribonucleoside salvage pathway, as well as the anabolic phosphorylation of nucleoside analogues used in viral and anticancer therapies, e.g. cidofovir, which is activated by the enzyme, overview
-
-
-
additional information
?
-
Q5EBM0
UMP-CMPK2 may have other functions in addition to the supply of substrates for mtDNA synthesis, it is highly expressed in leukemia cells, in bone marrow, and is tightly correlated with macrophage activation and inflammatory response
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
required for the phosphorylation of CMP, IUMP and dCMP by either ATP or dCTP. With CMP as phosphate acceptor and ATP as phosphate donor, Mn2+, Ni2+ and Ca2+ are able to substitute for Mg2+ but are less effective. The relative rates are Mg2+ (100%), Mn2+ (42%), Ni2+ (16%), and Ca2+ (13%)
Co2+
-
divalent cation required, Mn2+ can substitute for Mg2+
Mg2+
-
required for the phosphorylation of CMP, IUMP and dCMP by either ATP or dCTP. With CMP as phosphate acceptor and ATP as phosphate donor, Mn2+, Ni2+ and Ca2+ are able to substitute for Mg2+ but are less effective. The relative rates are Mg2+ (100%), Mn2+ (42%), Ni2+ (16%), and Ca2+ (13%)
Mg2+
-
optimal concentration is 2-3 mM
Mg2+
-
required for phosphorylation of CMP, UMP and dCMP by either ATP or dCTP
Mg2+
-
divalent cation required, Mg2+ is most effective
Mg2+
-
strong requirement, maximal activity at 3 mM
Mn2+
-
required for the phosphorylation of CMP, IUMP and dCMP by either ATP or dCTP. With CMP as phosphate acceptor and ATP as phosphate donor, Mn2+, Ni2+ and Ca2+ are able to substitute for Mg2+ but are less effective. The relative rates are Mg2+ (100%), Mn2+ (42%), Ni2+ (16%), and Ca2+ (13%)
Mn2+
-
with CMP as phosphate donor, Mn2+, Ni2+ and Ca2+ are able to substitute for Mg2+, 100%, Mn2+, 42%, Ni2+, 15% and Ca2+, 13%
Mn2+
-
divalent cation required, Mn2+ can substitute for Mg2+
Na2SO4
-
250 mM, stimulates
NaCl
-
250 mM, stimulates
Ni2+
-
required for the phosphorylation of CMP, IUMP and dCMP by either ATP or dCTP. With CMP as phosphate acceptor and ATP as phosphate donor, Mn2+, Ni2+ and Ca2+ are able to substitute for Mg2+ but are less effective. The relative rates are Mg2+ (100%), Mn2+ (42%), Ni2+ (16%), and Ca2+ (13%)
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5-Br-uracil vinylphosphonate
-
-
5-Cl-uracil vinylphosphonate
-
-
5-F-Phe-uracil vinylphosphonate
-
-
5-Phe-S-uracil vinylphosphonate
-
-
5-Phe-uracil vinylphosphonate
-
-
CDP
-
competitive withCMP
CMP
-
above 0.13 mM, substrate inhibition
CMP
-
competitive inhibition of UMP phosphorylation
CMP
-
substrate inhibition above 0.2 mM
CTP
-
inhibits reaction with ATP and UMP, CMP or dCMP
CuSO4
-
0.25 mM, 96% inhibition of enzyme form UMPK1 and 92% inhibition of enzyme form UMPK2
dCMP
-
competitive inhibition of UMP phosphorylation
dCTP
-
inhibits reaction with ATP and UMP, CMP or dCMP
DTNB
-
0.009 mM, 50% inhibition
F-
-
complete inhibition at 25 mM
HgCl2
-
0.25 mM, complete inhibition of enzyme form UMPK1 and UMPK2
HgCl2
-
0.1 mM, 88% inhibition
iodoacetamide
-
-
iodoacetate
-
0.05 mM, 50% inhibition
L-CMP
-
excess of L-CMP
lead nitrate
-
0.25 mM, 52% inhibition of enzyme form UMPK1 and 40% inhibition of enzyme form UMPK2
NEM
-
0.035 mM, 50% inhibition
NEM
-
1.0 mM; 41% inhibition
p-hydroxymercuribenzoate
-
0.02 mM, 50% inhibition
p-Hydroxymercuriphenyl sulfonate
-
0.02 mM, 50% inhibition
P1,P5-di(adenosine-5')pentaphosphate
-, O04905
-
PCMB
-
0.1 mM, 69% loss of activity
TTP
-
inhibits reaction with ATP and UMP, CMP or dCMP
UDP
-
product inhibition
UMP
-
substrate inhibition above 0.2 mM
uracil vinylphosphonate
-
-
UTP
-
inhibits reaction with ATP and UMP, CMP or dCMP
ZnCl2
-
0.25 mM, 55% inhibition of enzyme form UMPK1 and 30% inhibition of enzyme form UMPK2
MgATP2-
-
competitive with UMP
additional information
-
no substrate inhibition with 3 mM dCMP and 1 mM UMP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
at 5 mM: reduction in molecular weight from approximately 53000 Da to 17000 Da. This low molecular weight form is partially active in the presence of 2-mercaptoethanol. In absence of 2-mercaptoethanol the low molecular weight form is inactive. At 50 mM: full reactivation of the CMP(ATP) kinase activity followed by dCMP(ATP) and CMP(dCTP)
2-mercaptoethanol
-
activates
dithiothreitol
-
activates
dithiothreitol
-
1 mM, activates; activates
glutathione
-
activates
L-Cys
-
activates
NADPH
-
NADPH-dependent activation system is composed of at least two protein factors: one is heat-stable and the other is indistinguishable from NADPH-dependent disulfide reductase
reduced DL-alpha-lipoic acid
-
activates
-
thioredoxin
-
activates
thioredoxin
-
activity is strictly dependent upon sulfhydryl reducing agents. Reduced thioredoxin is by far the most effective
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.45
-
2',2'-difluorodeoxycytidine
-
pH 8.0, 37C
0.36
-
2'-azido-D-dCMP
-
pH 7.4, 37C
0.9
-
2'-azido-D-dUMP
-
pH 7.4, 37C
1.2
-
2'-azido-L-dCMP
-
pH 7.4, 37C
1.3
-
2'-azido-L-dUMP
-
pH 7.4, 37C
0.26
-
ara-CMP
-
pH 7.4, 37C, His-tagged UMP/CMP kinase
0.34
-
ara-CMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
0.917
-
ara-CMP
-
37C
1.4
-
araCMP
-
pH 8.0, 37C
0.029
-
ATP
-, O04905
pH 6.5, when UMP is the other substrate
0.067
-
ATP
-
pH 7.1, 37C
0.134
-
ATP
-
reaction with dCMP, enzyme from Novikoff ascites hepatoma
0.204
-
ATP
-
37C, 196-aa enzyme form, in presence of 8 mM MgATP2-
0.25
-
ATP
-
37C, enzyme form UMPK2
0.292
-
ATP
-, O04905
pH 6.5, reaction with CMP
0.32
-
ATP
-
reaction with CMP, liver enzyme
0.35
-
ATP
-
pH 7.1, 37C
0.36
-
ATP
-
37C, enzyme form UMPK1
0.58
-
ATP
-
reaction with UMP, liver enzyme
0.68
-
ATP
-
reaction with dCMP, liver enzyme
0.272
-
beta-D-2',3'-dideoxy-CMP
-
37C
1.037
-
beta-D-2',3'-dideoxy-CMP
-
37C
0.36
-
beta-D-2'-azido-2'-dCMP
-
-
0.9
-
beta-D-2'-azido-2'-dUMP
-
-
0.228
-
beta-L-(-)-2',3'-dideoxy-2',3'-didehydro-5-fluoro-CMP
-
37C
-
0.15
-
beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
-
pH 7.4, 37C, His-tagged UMP/CMP kinase
0.3
-
beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
2
-
beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
-
pH 7.4, 37C
0.697
-
beta-L-2',3'-dideoxy-CMP
-
37C
1.2
-
beta-L-2'-azido-2'-dCMP
-
-
1.3
-
beta-L-2'-azido-2'-dUMP
-
-
2
-
cCMP
-
pH 7.4, 37C
1
-
Cidofovir
-
-
0.0053
-
CMP
-
reaction with ATP, enzyme from Novikoff ascites hepatoma
0.015
-
CMP
-
37C, 196-aa and 228-aa enzyme form, in presence of 8 mM MgATP2-
0.022
-
CMP
-
pH 7.4, 37C
0.023
-
CMP
-
pH 8.0, 37C
0.026
-
CMP
-
37C enzyme form UMPK 1
0.028
-
CMP
-
37C, enzyme form UMPK2
0.03
-
CMP
-
reaction with ATP, liver enzyme
0.07
-
CMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
0.07
-
CMP
-
-
0.071
-
CMP
-
pH 7.5, 25C
0.13
-
CMP
-
pH 7.1, 37C
0.2
-
CMP
-
pH 7.4, 37C
0.211
-
CMP
-
37C, 196-aa enzyme form, in presence of 8 mM MgATP2-
0.266
-
CMP
-, O04905
pH 6.5
0.5
-
CMP
-
pH 8.0, 37C
0.98
-
CMP
-
reaction with dCTP, liver enzyme
3.09
-
CMP
Q5EBM0
pH 8.0, 37C, wild-type enzyme
0.02
-
D-CMP
-
-
0.02
-
D-CMP
-
pH 7.4, 37C
1
-
D-dCMP
-
-
1
-
D-dCMP
-
pH 7.4, 37C
1.3
-
D-dUMP
-
-
1.3
-
D-dUMP
-
pH 7.4, 37C
0.05
-
D-UMP
-
-
0.05
-
D-UMP
-
pH 7.4, 37C
0.074
-
dATP
-
reaction with CMP, liver enzyme
0.42
-
dATP
-
reaction with UMP, liver enzyme
0.61
-
dATP
-
reaction with dCMP, liver enzyme
0.017
-
dCMP
-
pH 8.0, 37C
0.023
-
dCMP
-
37C, 196-aa enzyme form, in presence of 8 mM MgATP2-
0.027
-
dCMP
-
reaction with dATP, liver enzyme
0.027
-
dCMP
-
-
0.354
-
dCMP
-
37C, 196-aa enzyme form, in presence of 8 mM MgATP2-
0.513
-
dCMP
-
37C, 196-aa enzyme form, in presence of 8 mM MgATP2-
0.54
-
dCMP
-
pH 7.5, 25C
0.715
-
dCMP
-
reaction with ATP, enzyme from Novikoff ascites hepatoma
0.9
-
dCMP
-
pH 7.4, 37C, His-tagged UMP/CMP kinase
1.1
-
dCMP
-
reaction with dATP, liver enzyme
1.1
-
dCMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
1.1
-
dCMP
-
-
1.31
-
dCMP
Q5EBM0
pH 8.0, 37C, wild-type enzyme
2.77
-
dCMP
-
reaction with ATP, liver enzyme
0.82
-
dCTP
-
reaction with CMP, liver enzyme
0.1
-
dUMP
Q5EBM0
pH 8.0, 37C, wild-type enzyme
0.43
-
dUMP
-
pH 8.0, 37C
1.3
-
dUMP
-
-
5.9
-
dUMP
-
pH 8.0, 37C
8.5
-
dUMP
-
pH 7.5, 25C
0.0146
-
gemcitabine
P30085
wild-type DCK
0.581
-
gemcitabine monophosphate
-
37C
0.246
-
gemcitabine phosphate
P30085
wild-type CMPK
0.494
-
L-(-)-2',3'-dideoxy-3'-thia-CMP
-
37C
0.25
-
L-(-)-2',3'-dideoxy-5-fluoro-3'-thia-CMP
-
37C, His-tagged UMP/CMP kinase
0.15
-
L-3TCMP
-
-
0.75
-
L-CMP
-
-
0.75
-
L-CMP
-
pH 7.4, 37C
0.73
-
L-dCMP
-
L-enantiomers have lower reaction rates
0.73
-
L-dCMP
-
pH 7.4, 37C
0.7
-
L-dUMP
-
L-enantiomers have lower reaction rates
0.02
-
UMP
-
pH 7.4, 37C, His-tagged UMP/CMP kinase
0.04
-
UMP
-
reaction with ATP, liver enzyme
0.043
-
UMP
-
reaction with ATP, enzyme from Novikoff ascites hepatoma
0.044
-
UMP
-
pH 7.4, 37C
0.045
-
UMP
-
pH 7.4, 37C, His-tagged UMP/CMP kinase
0.052
-
UMP
-
pH 7.5, 25C
0.053
-
UMP
-
reaction with dATP, liver enzyme
0.053
-
UMP
-
37C, enzyme form UMPK1
0.064
-
UMP
-
37C, enzyme form UMPK2
0.067
-
UMP
-
37C, 196-aa enzyme form, in presence of 8 mM MgATP2-
0.069
-
UMP
-
37C, 228-aa enzyme form, in presence of 8 mM MgATP2-
0.095
-
UMP
-
pH 8.0, 37C
0.13
-
UMP
-
-
0.14
-
UMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
0.153
-
UMP
-, O04905
pH 6.5
0.2
-
UMP
-
pH 7.4, 37C
1.4
-
UMP
-
pH 7.1, 37C
1.6
-
UMP
-
pH 8.0, 37C
6.3
-
UMP
Q5EBM0
pH 8.0, 37C, wild-type enzyme
0.7
-
L-dUMP
-
pH 7.4, 37C
additional information
-
additional information
P30085
Km values of mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
45
-
ara-CMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
150
-
ara-CMP
-
pH 7.4, 37C, His-tagged UMP-CMP kinase
10
-
beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
-
pH 7.4, 37C
14
-
beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
-
pH 7.4, 37C, GST fusion UMP/CMP kinase
36
-
beta-L-2',3'-dideoxy-3'-thiacytidine monophosphate
-
pH 7.4, 37C, His-tagged UMP-CMP kinase
8.57
-
CMP
-, O04905
pH 6.5
72
-
CMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
130
-
CMP
-
pH 7.4, 37C, His-tagged UMP-CMP kinase
410
-
CMP
-
pH 7.4, 37C
22
-
dCMP
-
pH 7.4, 37C
30
-
dCMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
73
-
dCMP
-
pH 7.4, 37C, His-tagged UMP-CMP kinase
0.65
-
UMP
-
pH 7.0, 25C, AUA chimeric enzyme
7.64
-
UMP
-, O04905
pH 6.5
13.7
-
UMP
-
pH 7.0, 25C, UAU chimeric enzyme
92
-
UMP
-
pH 7.4, 37C, GST fusion UMP-CMP kinase
130
-
UMP
-
pH 7.4, 37C, His-tagged UMP-CMP kinase
174
-
UMP
-
pH 7.0, 25C, UMP-CMP kinase
217
-
UMP
-
pH 7.4, 37C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.017
-
5-Br-uracil vinylphosphonate
-
-
0.016
-
5-Cl-uracil vinylphosphonate
-
-
0.028
-
5-Phe-S-uracil vinylphosphonate
-
-
0.12
-
CMP
-
pH 7.4, 37C, GST fusion UMP/CMP kinase
0.5
-
CMP
-
pH 7.4, 37C, His-tagged UMP/CMP kinase
0.0012
-
P1,P5-di(adenosine-5') pentaphosphate
-, O04905
versus ATP
0.00653
-
P1,P5-di(adenosine-5') pentaphosphate
-, O04905
versus UMP
0.5
-
UMP
-
pH 7.4, 37C, GST fusion UMP/CMP kinase
1.5
-
UMP
-
pH 7.4, 37C, His-tagged UMP/CMP kinase
0.7
-
uracil vinylphosphonate
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.035
-
5-Br-uracil vinylphosphonate
-
-
0.03
-
5-Cl-uracil vinylphosphonate
-
-
0.23
-
5-F-Phe-uracil vinylphosphonate
-
-
0.05
-
5-Phe-S-uracil vinylphosphonate
-
-
0.12
-
5-Phe-S-uracil vinylphosphonate
-
amplitude 50%
1.2
-
uracil vinylphosphonate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.2
-
-
reaction with CMP and ATP
4.98
-
-
reaction with dCMP and ATP
8.76
-
-
reaction with UMP and dCMP
337
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-, O04905
-
7.4
-
-
assay at
7.5
-
-
reaction with UMP and ATP
8
-
Q5EBM0
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9
-
pH 4.0: about 40% of maximal activity, pH 9.0: about 65% of maximal activity, reaction with UMP and ATP
6.2
8.6
-
50% of maximal activity at pH 6.2 and at pH 8.6
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
Q5EBM0
assay at
37
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.7
4.8
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
lung carcinoma
Manually annotated by BRENDA team
-
melanoma cell
Manually annotated by BRENDA team
-
chronic myelogenous leukemia cell
Manually annotated by BRENDA team
Q5EBM0
chronic myelogenous leukemia cell line
Manually annotated by BRENDA team
Q5EBM0
high expression
Manually annotated by BRENDA team
-
lymphoblastic leukemia cell
Manually annotated by BRENDA team
-
promyelocytic leukemia
Manually annotated by BRENDA team
-
growth for 14 days without phosphate, increase in enzyme transkript level, coordinate regulation of aspartate transcarbamoylase, ATCase, EC 2.1.3.2, carbamoyl phosphate synthetase, CPSase, EC 6.3.5.5, UMP synthase, EC 2.4.1.10, EC 4.1.1.23, uracil phosphoribosyltransferase, UPRTase, EC 2.4.2.9, UMP kinase, EC 2.7.4.14
Manually annotated by BRENDA team
-
colorectal adenocarcinoma cell
Manually annotated by BRENDA team
Q5EBM0
lymphoblastic leukemia cell line
Manually annotated by BRENDA team
additional information
-
two mRNA species are expressed in all immune tissues examined, an all cases the 3.4 kb form is the more prominent RNA species
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
N-terminal signal targets the enzyme to mitochondria
Manually annotated by BRENDA team
Q5EBM0
UMP-CMPK2 contains an N-terminal mitochondrial targeting sequence
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22500
-
-
sucrose density gradient centrifugation
26000
-
-
gel filtration
26000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, O04905
x * 22448, mass spectroscopy, calculation from nucleotide sequence
?
-
x * 22222, calculation from nucleotide sequence
?
P20425
x * 22000
additional information
P30085
DCK and CMPK structural models from crystal structures, overview
additional information
P20425
UmpK tertiary structure and protein folding kinetics and mechanism, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
of the selenomethionine labelled protein in complex with UMP, CMP, ADP, AMP-PCP, cidofovor and P1-(5-adenosyl) P5-(5-uridyl) pentaphosphate
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
more stable than at higher pH
7
-
-
at pH 7.0, the enzyme is most stable when kept at 4C
additional information
-
-
more stable in histidine buffer than in phosphate buffer
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
24 h, in absence of dithiothreitol the purified enzyme shows considerable loss of activity
4
-
-
at pH 7 the enzyme is most stable when kept at 4C
20
-
-
in absence of glycerol, the half-life of a preparation with a specific activity of 80 is about 10 min, inactivation is partially reversed by addition of 2-mercaptoethanol
25
-
-
30 min, stable
40
-
-
30 min, enzyme form UMPK2 loses 70% of maximal activity, enzyme form UMPK1 loses 30% of its activity
45
-
-
30 min, enzyme form UMPK2 loses more than 80% of maximal activity, enzyme form UMPK1 loses more than 60% of its activity
50
-
-
30 min, enzyme forms UMPK2 and UMPK1 lose 90% of its activity
50
-
-
midpoint denaturation temperature of the AUA chimeric enzyme
51
-
-
midpoint denaturation temperature of UMP/CMP kinase
52
-
-
midpoint denaturation temperature of the UAU chimeric enzyme
58
-
-, O04905
10 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
more stable in histidine than in phosphate buffer
-
the purified enzyme is notably unstable
-
dialysis against 20 mM phosphate, 1 mM MgCl2, 20% ethylene glycol, pH 8.0, 90% loss of activity
-
freeze-thawing inactivates
-
the enzyme is unstable when fully activated, anions promoting hydrophobic interactions stabilize the active conformation
-
bovine serum albumin, 0.1 mg/ml, is completely effective in preventing the loss of activity in the dilute preparation
-
three-fold dilution of a preparation of 0.2 mg of protein per ml results in less of 50% of the activity in 1 h
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-10C, 30% loss of activity within 2 months
-
-20C, concentrated enzyme solution in 30% glycerol, less than 5% loss of activity per month
-
-20C, in 25 mM Tris-acetate buffer, pH 7.5, 50 mM 2-mercaptoethanol, 50% glycerol, stable for at least 2 months
-
-80C, up to 12 months
-
4C, considerable loss of activity within 24 h, DTT stabilizes, more stable in 20 mM phosphate buffer, pH 8 than in Tris-HCl buffer
-
4C, 0.2 mg/ml, 2 weeks, 20% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
of the recombinant protein
-
of the recombinant proteins
-
partial, two allelic gene products UMPK1 and UMPK2
-
recombinant His6-tagged mutant UMP-CMPK2DELTA21 from Spodoptera frugiperda Sf9 cells by affinity chromatography
Q5EBM0
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNA is subcloned into pGEX-4T-3 and expressed as a glutathione S-transferase fusion protein in Escherichia coli
-, O04905
expression in Escherichia coli
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expressed in HCT-8 cell
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expression in Escherichia coli. The 228-aa and the 196-11 form are expressed as His-tagged fusion protein. The 196-aa UMP/CMP kinase is the actual form of the enzyme
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expression of His-tagged UMP-CMP kinase and UMP-CMP kinase fusion protein with glutathione S-transferase
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overexpression in Escherichia coli
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overexpression in Escherichia coli, wild type and selenomethionine labelled protein
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transient expression of wild-type and mutant DCK/CMPK enzymes in COS-1 cells
P30085
UMP-CMPK2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of His6-tagged mutant UMP-CMPK2DELTA21, lacking the mitochondrial targeting sequence, in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system, expression of GFP-tagged wild-type and E448G mutant enzymes in HeLa cells
Q5EBM0
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
G21A
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mutant enzyme is degraded during the purification phase
G22A
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mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 59% of that of the wild-type enzyme
G24A
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mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 48% of that of the wild-type enzyme
G26A
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mutant enzyme with decreased turnover-number/KmATP value
G27R
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mutant enzyme is degraded during the purification phase. Turnover-number is 45% of that of the wild-type enzyme
K27E
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mutant enzyme with 2600fold decreased turnover-number/KmATP value. Turnover-number is 21% of that of the wild-type enzyme
K27M
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mutant enzyme with 1000fold decreased turnover-number/KmATP value. Turnover-number is 22% of that of the wild-type enzyme
E448G
Q5EBM0
site-directed mutagenesis
additional information
P30085
determination and analysis of 28 polymorphisms in DCK/CMPK enzymes, genotyping with humans of different ethnic origins, overview. Variant allozyme enzyme activities range from 32 to 105% of the wild-type enzyme for DCK and from 78 to 112% of wild-type enzyme for CMPK, with no significant differences in apparent Km values for either enzyme except for a DCK Val24/Ser122 double variant allozyme, overview
additional information
Q5EBM0
construction of a UMP-CMPK2DELTA21 mutant lacking the mitochondrial targeting sequence
additional information
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two types of chimeric enzymes have been constructed by genetic engineering of chicken cytosolic adenylate kinase and porcine brain UMP/CMP kinase. One designated as UAU carries an AMP-binding domain of AK in the remaining body of UMP/CMP kinase, and the other, designated as AUA, carries a UMP/CMP-binding domain in the remaining body of adenylate kinase. UAU is 4fold more active with AMP, 40fold less active with UMP, and 4fold less active with CMP than the parental UMP/CMP kinase, although AUA has considerably lowered reactivity for both AMP and UMP. AUA has a Tm-value 11C lower than adenylate kinase, whereas UAU has a Tm-value similar to that of UMP/CMP kinase. Expression in Escherichia coli JM109
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after treatment with urea, UmpK protein unfolding and refolding kinetics, and folding mechanism, overview
P20425
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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screening of acyclic phosphonate analogs to find antimetabolites for antivirus and anticancer therapies