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Information on EC 2.7.4.22 - UMP kinase
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2.7.4.22 UMP kinaseIUBMB Comments
This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose . This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP .
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
umpk, ump kinase, uridine monophosphate kinase, uridylate kinase, ump-kinase, umpks, ssumpk, xc1936, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:UMP phosphotransferase
pyrH
Rv2883c
UMP kinase
UMPK
UMPKs
uridine monophosphate kinase
uridylate kinase
additional information
uridine monophosphate kinase
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uridine monophosphate kinase
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uridine monophosphate kinase
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uridine monophosphate kinase
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uridine monophosphate kinase
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uridine monophosphate kinase
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-
additional information
bacterial and archaeal UMPKs all belong to the amino acid kinase family
additional information
-
the enzyme belongs to the the amino-acid kinase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + UMP = ADP + UDP
-
-
-
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ATP + UMP = ADP + UDP
a sequential bi-bi reaction mechanism and, as a nucleophilic substitution reaction while both substrates are bound to the enzyme
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ATP:UMP phosphotransferase
This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1].
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CAS REGISTRY NUMBER
COMMENTARY
9036-23-1
-
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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
ATP + dUMP
ADP + dUDP
3.7% of the activity detected with UMP
-
-
?
ATP + UMP
ADP + UDP
Q81S73
an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview
-
-
?
ATP + UMP
ADP + UDP
Q81S73
an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview
-
-
?
ATP + UMP
ADP + UDP
at 30°C, pH 7.4, in the presence of 2 mM MgCl2
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-
?
ATP + UMP
ADP + UDP
the enzyme regulatory mechanisms involve GTP and UTP, overview
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-
?
ATP + UMP
ADP + UDP
movements induced by binding uridine nucleotides, GTP and UTP interaction mechanism, analysis, overview
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-
?
ATP + UMP
ADP + UDP
low activity with dUMP as substrate, no activity with CMP, dTMP, AMP, IMP, XMP, GMP, low activity with dATP, GTP, CTP and UTP as substrate
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r
ATP + UMP
ADP + UDP
high substrate specificity toward UMP and ATP
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-
?
ATP + UMP
ADP + UDP
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-
-
?
ATP + UMP
ADP + UDP
30°C, pH 7.4
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-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
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-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
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-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
37°C, pH 7.8, 7.5 mM MgCl2
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-
?
ATP + UMP
ADP + UDP
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UMP kinase catalyzes the transfer of the gamma-phosphate of ATP to UMP
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r
ATP + UMP
ADP + UDP
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UMP kinase catalyzes the transfer of the gamma-phosphate of ATP to UMP
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r
ATP + UMP
ADP + UDP
at 37°C, pH 7.5, in the presence of MnCl2 or MgCl2
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?
additional information
?
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no reaction with dUMP, CMP, dCMP or TMP as substrate
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?
additional information
?
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no reaction with dUMP, CMP, dCMP or TMP as substrate
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-
?
additional information
?
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Asp93 appears as one of the key amino acids in the transfer of information from the regulatory site to the active site
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?
additional information
?
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Asp93 appears as one of the key amino acids in the transfer of information from the regulatory site to the active site
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?
additional information
?
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no activity with CMP, dTMP, or the purine nucleotides (AMP, IMP, XMP, and GMP), ATP is by far the most effective phosphoryl donor, although a very weak activity (less than 1% of ATP activity) is seen with dATP, GTP, CTP, and UTP
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?
additional information
?
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no activity with CMP, dTMP, or the purine nucleotides (AMP, IMP, XMP, and GMP), ATP is by far the most effective phosphoryl donor, although a very weak activity (less than 1% of ATP activity) is seen with dATP, GTP, CTP, and UTP
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?
additional information
?
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UMP kinase exhibits an intrinsic fluorescence, due to its unique tryptophan, decreasing with the increase of UTP concentration
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?
additional information
?
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enzyme activity detection by the coupled pyruvate kinase/lactate dehydrogenase assay, UMP kinase assay development and optimization, overview
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?
additional information
?
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enzyme activity detection by the coupled pyruvate kinase/lactate dehydrogenase assay, UMP kinase assay development and optimization, overview
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?
additional information
?
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bacterial UMP kinases are crucial enzymes that are responsible for microbial UTP biosynthesis, and bacterial UMPKs are specific for the phosphorylation of UMP only showing no dual activity in contrast to eukaryotic enzymes
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?
additional information
?
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the enzyme possesses well defined loop regions involved in substrate-analogue binding, overview
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?
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NATURAL SUBSTRATE
NATURAL 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
ATP + UMP
ADP + UDP
Q81S73
an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview
-
-
?
ATP + UMP
ADP + UDP
Q81S73
an essential metabolic step with a structure-based mechanism for the allosteric behavior of bacterial enzyme, overview
-
-
?
ATP + UMP
ADP + UDP
the enzyme regulatory mechanisms involve GTP and UTP, overview
-
-
?
ATP + UMP
ADP + UDP
high substrate specificity toward UMP and ATP
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
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-
-
?
ATP + UMP
ADP + UDP
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?
ATP + UMP
ADP + UDP
-
-
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?
ATP + UMP
ADP + UDP
-
-
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?
additional information
?
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UMP kinase exhibits an intrinsic fluorescence, due to its unique tryptophan, decreasing with the increase of UTP concentration
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?
additional information
?
-
-
bacterial UMP kinases are crucial enzymes that are responsible for microbial UTP biosynthesis, and bacterial UMPKs are specific for the phosphorylation of UMP only showing no dual activity in contrast to eukaryotic enzymes
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
a stoichiometry between Mg2+ and ATP of 2:1 gives 1.6fold higher catalytic rates compared to a 1:1 stoichiometry
ATP
Q81S73
the cofactor, in addition to binding in the active sites, also interacts with separate binding pocket, with an allosteric binding site, located near the center of the hexameric structure
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Mg2+
MgCl2
in the presence of MgCl2 the saturation kinetics of recombinant purified UMP kinase are hyperbolic for UMP and sigmoidal for ATP
Mn2+
MnCl2
in the presence of MnCl2 the saturation kinetics of recombinant purified UMP kinase are hyperbolic for UMP and sigmoidal for ATP
additional information
Cd2+
causes severe precipitation problems in the phosphate buffer
Mg2+
the crystal structure contains two bound Mg ions, of which one helps stabilize the transition state
Mg2+
a stoichiometry between Mg2+ and ATP of 2:1 gave 1.6fold higher catalytic rates, compared to a 1:1 stoichiometry
Mg2+
a stoichiometry between Mg2+ and ATP of 2:1 gives 1.6fold higher catalytic rates compared to a 1:1 stoichiometry
additional information
Co2+ and Ni2+ substitute poorly for Mg2+ and give limited enzyme activity, while Ca2+ and Zn2+ are unable to activate UMP kinase within 0-5 mM. UMP kinase activity of the HP0777 protein is completely abolished in the absence of divalent cations
additional information
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Co2+ and Ni2+ substitute poorly for Mg2+ and give limited enzyme activity, while Ca2+ and Zn2+ are unable to activate UMP kinase within 0-5 mM. UMP kinase activity of the HP0777 protein is completely abolished in the absence of divalent cations
additional information
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only one metal ion in the active site. This ion is coordinated with phosphate groups of both ATP and UMP
additional information
only one metal ion in the active site. This ion is coordinated with phosphate groups of both ATP and UMP
additional information
UMP kinase is totally inactive in the absence of MgCl2 or MnCl2
additional information
-
UMP kinase is totally inactive in the absence of MgCl2 or MnCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-[([5-oxo-4-[(2R)-tetrahydrofuran-2-ylmethyl]-4,5-dihydro-1H-1,2,4-triazol-3-yl]sulfanyl)acetyl]piperidine-4-carboxylic acid
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2-(4-acetyl-3,5-dimethyl-1H-pyrazol-1-yl)-N-[1-(2-methoxybenzyl)-1H-pyrazol-5-yl]acetamide
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2-amino-8-(2-oxo-2-phenylethoxy)-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 75% inhibition, crystal enzyme complex structure, overview
2-amino-8-hydroxy-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 18% inhibition
2-amino-8-[2-(2-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 48% inhibition
2-amino-8-[2-(3-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 77% inhibition
2-amino-8-[2-(4-fluorophenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 73% inhibition
2-amino-8-[2-(4-hydroxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 77% inhibition
2-amino-8-[2-(4-methoxyphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 74% inhibition
2-amino-8-[2-(4-methylphenyl)-2-oxoethoxy]-1,4,5,9-tetrahydro-6H-purin-6-one
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10 micromol, 60 min, room temperature, 80% inhibition
4-[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)methyl]benzonitrile
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10 micromol, 60 min, room temperature, 53% inhibition, crystal enzyme complex structure, overview
4-[2-amino-4-(4-chlorophenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid
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4-[2-amino-4-(4-methoxyphenyl)-7-oxo-5,7-dihydro-6H-pyrrolo[3,4-d]pyrimidin-6-yl]butanoic acid
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4-[[(2-amino-6-oxo-4,5,6,9-tetrahydro-1H-purin-8-yl)oxy]acetyl]benzonitrile
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10 micromol, 60 min, room temperature, 68% inhibition
5-[(9H-[1,2,4]triazolo[4,3-a]benzimidazol-3-ylsulfanyl)methyl]furan-2-carboxylic acid
hydrogen bonding interactions of ZINC12561276 molecule with the active site residues of Mtb-UMPK homology model, overview
dUTP