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Information on EC 2.7.4.14 - UMP/CMP kinase and Organism(s) Rattus norvegicus
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2.7.4.14 UMP/CMP kinaseIUBMB Comments
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, (d)CMP kinase and EC 2.7.4.22, UMP kinase.
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Word Map
- 2.7.4.14
- dcmp
- deoxycytidine
- gemcitabine
- cidofovir
-
nmp-binding
- umpks
- medicine
- diagnostics
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
cmpk2, cmpk, cmp kinase, ump-cmp kinase, cmpk1, ump/cmp kinase, cytidylate kinase, pyrimidine nucleoside monophosphate kinase, cytidine monophosphate kinase, cytidine/uridine monophosphate kinase 2, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:UMP-CMP phosphotransferase
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-
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CMP kinase
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-
-
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CMPK
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-
-
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CTP:CMP phosphotransferase
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-
-
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cytidine monophosphate kinase
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-
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cytidylate kinase
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-
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kinase, cytidylate (phosphorylating)
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-
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MssA protein
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-
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P25
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pyrimidine nucleoside monophosphate kinase
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UCK
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UMP-CMP kinase
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UMP/CMP kinase
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UMPK
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + UMP = ADP + UDP
reaction mechanism is sequential and nonequilibrium in nature, substrates bind to the enzyme in a random order, substrate binding is cooperative
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -, -
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, (d)CMP kinase and EC 2.7.4.22, UMP kinase.
CAS REGISTRY NUMBER
COMMENTARY
37278-21-0
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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
METALS and IONS
ORGANISM
UNIPROT
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%)
Mg2+
Mn2+
Ni2+
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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+
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required for phosphorylation of CMP, UMP and dCMP by either ATP or dCTP
Mg2+
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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+
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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+
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with CMP as phosphate donor, Mn2+, Ni2+ and Ca2+ are able to substitute for Mg2+, 100%, Mn2+, 42%, Ni2+, 15% and Ca2+, 13%
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no substrate inhibition with 3 mM dCMP and 1 mM UMP
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additional information
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no substrate inhibition with 3 mM dCMP and 1 mM UMP
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
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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
2-mercaptoethanol
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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)
thioredoxin
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activity is strictly dependent upon sulfhydryl reducing agents. Reduced thioredoxin is by far the most effective
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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). KCY_RAT
196
0
22169
Swiss-Prot
other Location (Reliability: 5)
A0A0G2JTN5_RAT
239
0
27065
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I6AP91_RAT
227
0
25833
TrEMBL
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
24 h, in absence of dithiothreitol the purified enzyme shows considerable loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 20 mM phosphate, 1 mM MgCl2, 20% ethylene glycol, pH 8.0, 90% loss of activity
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the enzyme is unstable when fully activated, anions promoting hydrophobic interactions stabilize the active conformation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 25 mM Tris-acetate buffer, pH 7.5, 50 mM 2-mercaptoethanol, 50% glycerol, stable for at least 2 months
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4°C, considerable loss of activity within 24 h, DTT stabilizes, more stable in 20 mM phosphate buffer, pH 8 than in Tris-HCl buffer
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Orengo, A.; Maness, P.
Pyrimidine nucleoside monophosphate kinase from rat liver and rat Novikoff ascites hepatoma (EC 2.7.4.14)
Methods Enzymol.
51
321-331
1978
Rattus norvegicus
Maness, P.; Orengo, A.
Activation of rat liver pyrimidine nucleoside monophosphate kinase
Biochim. Biophys. Acta
429
182-190
1976
Rattus norvegicus
Maness, P.; Orengo, A.
A pyrimidine nucleoside monophosphate kinase from rat liver
Biochemistry
14
1484-1489
1975
Rattus norvegicus
Kobayashi, S.; Kanayama, K.
NADPH activation of deoxycytidylate kinase in rat liver extract: involvement of an endogenous disulfide reductase system
Biochem. Biophys. Res. Commun.
74
1249-1255
1977
Rattus norvegicus
Seagrave, J.; Reyes, P.
Pyrimidine nucleoside monophosphate kinase from rat bone marrow cells: chromatographic, electrophoretic, and sedimentation behavior of active and inactive enzyme forms
Arch. Biochem. Biophys.
247
76-83
1986
Rattus norvegicus
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