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Information on EC 2.7.4.22 - UMP kinase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97ZE2
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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 taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + UMP = ADP + UDP
a sequential bi-bi reaction mechanism and, as a nucleophilic substitution reaction while both substrates are bound to the enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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].
CAS REGISTRY NUMBER
COMMENTARY
9036-23-1
-
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
high substrate specificity toward UMP and ATP
-
-
?
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
-
-
r
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
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
high substrate specificity toward UMP and ATP
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
causes severe precipitation problems in the phosphate buffer
additional information
additional information
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
UTP
feedback inhibition, competitive inhibitor against both substrates
UTP
binds the enzyme, competitive inhibitor for both substrates
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
GTP no influence, GTP does not bind, unlike most bacteria, is not activated by GTP, UTP acts as a competitive inhibitor against both substrates, high concentration of UMP abolishes the inhibition of UTP at low ATP concentrations, indicating that UTP binds to the acceptor site (UMP site)
-
additional information
GTP no influence, GTP does not bind, unlike most bacteria, is not activated by GTP, UTP acts as a competitive inhibitor against both substrates, high concentration of UMP abolishes the inhibition of UTP at low ATP concentrations, indicating that UTP binds to the acceptor site (UMP site)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.081
ATP
radioactive assay, 500 microM ATP and 100 microM UMP, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature
0.014
UMP
radioactive assay, 500 microM ATP and 100 microM UMP, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
UMP
radioactive assay, at 60°C, the more commonly used photometric assay using auxiliary enzymes is incompatible with high temperature
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
variation of pH only influences the turnover number, at 60°C, 50 mM succinate/phosphate buffer, phosphate buffer, glycine buffer, assays are performed with 100 microM UMP, 500 microM ATP, and 10 mM MgCl2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
variation of pH only influences the turnover number
additional information
variation of pH only influences the turnover number
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain P2, plasmid vector pUHE23-2, expression in Escherichia coli strain NF1830
UniProt
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ternary complex with UMP and the nonhydrolyzable ATP analogue alpha,beta-methylene-ATP (SsUMPK-UMP-AMPPCP), resolution 2.1 A, a complex with UMP (SsUMPK-UMP), resolution 2.2 A, a complex with UTP (SsUMPK-UTP), resolution 2.8 A, hanging drop vapor diffusion, protein solution (2UL) in 10 mM TRIS/Cl pH 7.6 with 4.6 mg/ml SSUMPK and 2 mM UMP and 5 mM MgCl2 mixed with 2 UL mother solution (0.65 M sodium acetate, 100 mM CdCl2, 0.1 M HEPES), pH 7.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heating at 70°C, ammonium sulfate precipitation, and column chromatography on Dyematrex Gel Red A and the anion exchange materials DE52 and Q6. Minor amounts (around 2%) of a smaller 15 kDa protein, presumably an SsUMPK degradation product, co-purified with SsUMP.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
plasmid vector pUHE23-2, expression in Escherichia coli strain NF1830
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jensen, K.S.; Johansson, E.; Jensen, K.F.
Structural and enzymatic investigation of the Sulfolobus solfataricus uridylate kinase shows competitive UTP inhibition and the lack of GTP stimulation
Biochemistry
46
2745-2757
2007
Saccharolobus solfataricus, Saccharolobus solfataricus (Q97ZE2)
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