Information on EC 2.4.2.9 - uracil phosphoribosyltransferase

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

EC NUMBER
COMMENTARY hide
2.4.2.9
-
RECOMMENDED NAME
GeneOntology No.
uracil phosphoribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyrimidine nucleobases salvage I
-
-
pyrimidine metabolism
-
-
Pyrimidine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
UMP:diphosphate phospho-alpha-D-ribosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-24-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene upp; strain DSM 405
SwissProt
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
K12
-
-
Manually annotated by BRENDA team
strain SO 1344 and SO 1346
-
-
Manually annotated by BRENDA team
strain Portland I, ATCC 30888
-
-
Manually annotated by BRENDA team
strain Portland I, ATCC 30888
-
-
Manually annotated by BRENDA team
Lactobacillus bifidus
strain ATCC 4963
-
-
Manually annotated by BRENDA team
strain ATCC 4797
-
-
Manually annotated by BRENDA team
strain BM604, gene upp
SwissProt
Manually annotated by BRENDA team
strain BM604, gene upp
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
oncolytic adenovirus AxE1CAUP
-
-
-
Manually annotated by BRENDA team
strain GL-7
-
-
Manually annotated by BRENDA team
strain GL-7
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the metabolism of uracil and related compounds in plants catalyzing the uracil salvage, which is of major importance for plant development, overview
physiological function
UPRTs, on-essential, energy-saving enzymes, are involved in the salvage of pyrimidines by catalyzing the formation of uridine monophosphate from uracil and phosphoribosylpyrophosphate. Uracil salvage is of major importance for plant development, especially early development
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
2-thio-5'-UMP + diphosphate
show the reaction diagram
-
substrate is anti-thyroid drug
-
?
4-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
4-thio-UMP + diphosphate
show the reaction diagram
-
-
-
-
?
4-thiouracil + 5-phospho-alpha-D-ribose 1-diphosphate
4-thiouridine monophosphate + diphosphate
show the reaction diagram
-
-
-
-
?
5'-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5'-fluoro-UMP + diphosphate
show the reaction diagram
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
show the reaction diagram
6-azauracil + 5-phospho-alpha-D-ribose 1-diphosphate
6-aza-UMP + diphosphate
show the reaction diagram
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
show the reaction diagram
uridine + ATP
UMP + ADP
show the reaction diagram
the bifunctional enzyme UK/UPRT also performs the uridine kinase reaction, EC 2.7.1.48
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluoro-UMP + diphosphate
show the reaction diagram
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
show the reaction diagram
uridine + ATP
UMP + ADP
show the reaction diagram
Q9FKS0
the bifunctional enzyme UK/UPRT also performs the uridine kinase reaction, EC 2.7.1.48
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
activates
Divalent cations
Ni2+
-
activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-dimethyl-uracil
-
-
4-thiouracil
-
substrate inhibition at high concentrations
5-acetoxyuracil
-
-
5-Bromouracil
-
-
5-fluoro-deoxyuracil
-
-
5-fluorouracil
5-n-propyl-2'-deoxyuridine
-
-
5-Nitrouracil
-
-
5-phosphoribose 1-diphosphate
-
inhibitory when higher concentrated as Mg2+
6-benzyl-2-thiouracil
-
-
6-formyluracil
-
-
dCMP
-
allosteric inhibition
dCTP
-
allosteric inhibition
diphosphate
DTNB
-
4 mM, 87% inhibition after 30 min
dUMP
-
allosteric inhibition
K+
-
slight inhibition at 0.1 M
Na+
-
slight inhibition at 0.1 M
phosphate
-
80% inhibition at 0.05 M
tetrahydrouridine
-
-
TTP
-
allosteric inhibition
UDP
-
allosteric inhibition
Uracil
-
substrate inhibition at high concentrations
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alendronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.5fold, increases the initial rate of synthesis of UMP 2.3fold
ATP
-
weak activation
clodronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2fold, increases the initial rate of synthesis of UMP 1.9fold
dGTP
-
highly activating, no effect on Km values
etidronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.8fold, increases the initial rate of synthesis of UMP 2.1fold
glutathione
Lactobacillus bifidus
-
omission of glutathione reduces the reaction rate about 25%
guanosine-3',5'-diphosphate
-
activates in the same range as GTP
pamidronate
-
1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.6fold, increases the initial rate of synthesis of UMP 2.1fold
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.67
2-Thiouracil
-
-
0.0071
4-thiouracil
-
at pH 7.5 and 25C
0.0064
5-fluorouracil
-
at pH 7.5 and 25C
0.0069 - 0.3
5-phospho-alpha-D-ribose 1-diphosphate
1
diphosphate
-
-
0.13
UMP
-
-
0.0004 - 0.159
Uracil
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 6.1
5-phospho-alpha-D-ribose 1-diphosphate
0.0015
UMP
Bacillus subtilis
-
reverse reaction
0.36 - 6.1
Uracil
additional information
additional information
Toxoplasma gondii
-
recombinant wild-type and mutant enzymes
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
5-fluorouracil
-
-
0.24
diphosphate
-
competitive versus 5-phosphoribose 1-diphosphate
0.017
tetrahydrouridine
-
-
0.015
UMP
-
competitive versus uracil
additional information
additional information
-
product inhibition pattern
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013
5-fluorouracil
Escherichia coli
-
pH 7.3, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0057
-
substrate 2-thiouracil
0.0067
-
substrate uracil
0.025
Lactobacillus bifidus
-
purified enzyme
0.068
-
partially purified enzyme
0.192
-
strain SO 1346
0.22
-
partially purified enzyme
0.76
-
crude extract, at pH 7.5 and 25C
1.56
-
after 2.1fold purification, at pH 7.5 and 25C
3.1
-
purified enzyme
6.602
-
purified enzyme, strain SO 1346
7.5
-
purified recombinant enzyme
11.4
-
pH 7.3, 37C
19.2
-
purified recombinant enzyme, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
-
plateau, substrate uracil
7.4
Lactobacillus bifidus
-
assay at
7.5 - 8.5
-
-
7.5 - 8
-
substrate 2-thiouracil
7.5 - 8
7.8
-
2-thiouracil
8.5
-
assay at
8.7
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
-
pH 3.8: no activity, pH 5.5: optimum, pH 8: about 20% of maximal activity
5.8 - 7
-
pH 5.8: about 55% of maximal activity, pH 7.0: about 45% of maximal activity
7.2 - 8
-
pH 7.2: about 50% of activity maximum, pH 8.0: about 70% of activity maximum
7.5 - 8.5
-
more than 90% activity between 7.5 and 8.5 with sharp drops in activity 0.5 pH units outside this range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
recombinant enzyme
95
-
optimal temperature exceeds 95C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.85
-
calculated from amino acid sequence; sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
; low level of expression
Manually annotated by BRENDA team
; lower expression level
Manually annotated by BRENDA team
-
; low level of expression
Manually annotated by BRENDA team
; higher expression level
Manually annotated by BRENDA team
-
high expression level; high level of expression
Manually annotated by BRENDA team
-
high expression level; high level of expression
Manually annotated by BRENDA team
-
; low level of expression
Manually annotated by BRENDA team
-
; low level of expression
Manually annotated by BRENDA team
; lower expression level
Manually annotated by BRENDA team
-
; low level of expression
Manually annotated by BRENDA team
-
high expression level; high level of expression
Manually annotated by BRENDA team
; higher expression level
Manually annotated by BRENDA team
-
high expression level; high level of expression
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain K96243)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000 - 27600
-
recombinant enzyme, gel filtration and DNA sequence determination
33800
-
calculated from amino acid sequence
46000
-
gel filtration
63000
-
sucrose density gradient centrifugation and gel filtration in absence of substrates
75000
-
gel filtration
76000
-
gel filtration
98000
-
sucrose density gradient centrifugation
100000
-
gel filtration
109700
-
gel filtration
111000
-
sucrose density gradient centrifugation and gel filtration in presence of substrates
120000
gel filtration
200000 - 250000
-
gel filtration
additional information
-
gel filtration and sedimentation analyses: a smaller oligomeric, less active form, dimeric or trimeric, predominates in absence of substrates, a larger aggregated, more active form, pentameric or hexameric, predominates in presence of substrates
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
monomer
-
1 * 27000, recombinant enzyme, SDS-PAGE
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapour diffusion using hanging or sitting drops, room temperature, protein solution 20 mg/ml, pH 7.0, 5 mM phosphate, 0.003 ml + 0.003 ml reservoir solution, pH 7.5, 6-10% polyethylene glycol 4000, 0.1 M HEPES, crystals appeared after 3 weeks, structure determination and analysis
-
computational docking of inhibitor 5-fluorouracil to the active site of the enzyme. 5-fluorouracil forms hydrogen bonds with residues Tyr192, Gly196, and Leu197 in the complex. 5-fluorouracil shows low average free energy binding with the enzyme which indicates stronger binding than the natural substrate uracil
-
sitting drop vapor diffusion method, using 0.1 M sodium acetate trihydrate pH 4.6, 1.5 M sodium formate with a 2:1 reservoir-to-protein solution ratio at 25C
enzyme in complex with UMP, enzyme in complex with CTP, structure with UMP bound in half of the active sites. Hanging-drop vapour-diffusion method
-
two structures of the activated state enzyme in complex with GTP, X-ray diffraction structure determination and analysis at 2.8 A resolution, the first structure which contains PRPP in all active sites, and 2.9 A resolution, for the second structure with PRPP in two sites and the hydrolysis products ribose-5-phosphate and diphosphate in the other sites, respectively, and a third structure of the enzyme in complex with UMP and the allosteric inhibitor CTP
-
hanging drop-vapour diffusion method, enzyme complexed with uracil and 5-phosphoribose 1-diphosphate, 20 mg/ml, mixing of equal volumes, 15 mM sodium citrate/phosphate, 0.2 M NaCl, pH 4.7, 10% polyethylene glycol 3400, X-ray diffraction structure analysis, dynamic light scattering
-
hanging drop-vapour diffusion technique, 2.0 M ammonium phosphate as precipitant, pH 8.0, room temperature, X-ray diffraction structure analysis, crystals are enzymatically active, wild-type and mutant enzymes
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
irreversible inactivation above
45
-
10 min, 90% remaining activity
50
-
begins to unfold irreversibly
56 - 57
-
10 min, 50% loss of activity, recombinant wild-type and mutant, scanning calorimetry
65
-
complete inactivation after 5 min
70
-
10 min, 70% remaining activity
75
-
10 min, 5% remaining activity
90
-
half-life: 4 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM DTT and 0.1 mM EDTA stabilize the purified enzyme
-
2-mercaptoethanol, not essential for stability in long-term storage
-
bovine serum albumin at 2 mg/ml stabilizes
-
dialysis against buffers of low ionic strength invariably results in complete inactivation, whereas after 3 h dialysis against 0.5 M KCl only 40% of the activity is lost
Lactobacillus bifidus
-
enzyme is extremly unstable, UMP stabilizes during storage
-
enzyme is highly unstable, dimethyl sulfoxide stabilizes during purification
-
ethylene glycol, significantly increases stability with virtually no loss of activity after storage at 4C for 13 days or after 1 year at -70C
-
GTP, 5 mM with 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 2 mM 2-mercaptoethanol, labilizes with only 15% activity remaining after 13 days, labilizing effect abolished in presence of 5-phospho-alpha-D-ribose 1-diphosphate
-
rapid precipitation of purified enzyme without thiol reducing agents
-
UMP stabilizes the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, partially purified enzyme, loss of 10% activity within 2 weeks
Lactobacillus bifidus
-
-20C, 20 mM Hepes-KOH, pH 7.4, 1 mM DTT, stable for 3 days
-
-70C, 20 mM Hepes-KOH, pH 7.4, 1-2 months without loss of activity
-
0C, enzyme concentration 0.001 mg/ml, 50% loss of activity in 1 h
-
4C for 13 days or 1 year at -70C, ethylene glycol, significantly increases stability with virtually no loss of activity
-
4C, 10 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 2 mM 2-mercaptoethanol, 44% loss of activity after 8 d
-
4C, concentrated enzyme is stable for several months, on dilution occurs rapid loss of activity
-
4C, purified enzyme, TMD50 buffer, stable for at least 1 week
-
4C, rapid loss of activity when stored in presence of Mg2+
-
4C, Tris-HCl, pH 8.0, 1 mM EDTA, 2 mM DTT, 1 mM UMP, loss of 40% activity in 1 week
-
4C, Tris-HCl, pH 8.0, 1 mM EDTA, 2 mM DTT, loss of 70% activity in 4 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-300 gel filtration
-
from strain SO 1346
-
MonoQ column chromatography and Superdex 200 gel filtration
Ni-NTA affinity column chromatography; recombinant His6-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography
-
Ni-NTA column chromatography
-
only partial, due to the labile nature of the enzyme further purification is unsuccessful
-
partial
recombinant from enzyme-deficient Escherichia coli
-
recombinant from Escherichia coli
-
recombinant from overexpressing strain
-
recombinant wild-type and mutant P131D from overexpressing Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning from a fetal brain cDNA library, DNA and amino acid sequence determination, subcloning in Escherichia coli strain DH5alpha, expression of His6-tagged enzyme in Escherichia coli strain M15, phylogenetic analysis, expressionin AD293 cells, tissue and subcellular expression pattern; expressed in Escherichia coli strain M15 and in AD-293 cells
-
co-expression of gene CodA, encoding cytosine deaminase, and gene upp, encoding uracil phosphoribosyl transferase, renders HeLa cells sensitive to 5-fluorocytosine, converted to toxic 5-fluorouracil by cytosine deaminase, and enhanced a bystander effect mediated by a gap junction mechanism, 1% cytosine deaminase+-UPP+ cells are able to kill 40% of the cell population if the cells are communicating
-
coexpression of the uracil phosphoribosyltransferase gene with a chimeric human nerve growth factor receptor/yeast cytosine deaminase fusion gene, using a single retroviral vector, augments cytotoxicity of transduced human T cells, CEM cells, exposed to 5-fluorocytosine
-
cytosine deaminase-UPRT-red fluorescence protein fusion proteins are expressed in Rattus norvegicus R-3327-AT cells
-
DNA and amino acid sequence determination and analysis of the natural chimeric gene UK/UPRT1 encoding uridine kinase, UK, and uracil phosphoribosyltransferase, UPRT, expressionin Escherichia coli, transient expression as C-terminally GFP-tagged enzyme in Arabidopsis thaliana mesophyll protoplasts, 5-FU sensitivity of the Escherichia coli upp mutants is influenced by the expression of AtUK/UPRT1, as well as the 5-FU and 5-FD sensitivity of Escherichia coli upp-udk mutants, overview; expressed in Escherichia coli strain JM109
DNA and amino acid sequence determination and analysis, overexpression in enzyme-deficient Escherichia coli
DNA sequence determination and analysis, gene upp belongs to purMN operon, complementation of deficient Escherichia coli strain
-
DNA sequence determination, functional overexpression in Escherichia coli BL21(DE3)plyS
-
expressed in A2780 cells, A2780/Taxol cells, Skov3 cells, and Skov3/Taxol cells
-
expressed in AsPC-1, BxPC3, CaPan-1, MIA, PaCa-2, Panc-1, and HT-29 cell lines
-
expressed in BHK-21 cells and HAT-29 cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21Star (DE3) One Shot cells
-
expressed in Escherichia coli Tuner (DE3) cells
expressed in HaP-T1 cells
oncolytic adenovirus AxE1CAUP
-
expressed in HeLa cells
-
expressed in LNCaP cells
-
expression in Escherichia coli
-
expression in human adipose tissue-derived mesenchymal stem cells
-
expression of the fusion gene CDUPRT, combining cytosine deaminase combined with uracil phosphoribosyl transferase, in RM1 cancer cells in a gene therapeutic approach, overview
-
functional overexpression in Escherichia coli JM109
-
functional overexpression in Escherichia coli JM109; wild-type and mutant C128V
-
gene UPP, DNA and amino acid sequence determination and analysis, gene structure, sequence comparison, and phylogenetic analysis, Comparison to uracil kinase-like proteins possessing UPRT domains. The single nuclear gene encoding UPP targeted to plastids is responsible for almost all UPRT activity in Arabidopsis thaliana
gene upp, upp gene is part of the lp_2376-glyA-upp operon, upp expression depends on the upp-pyrP gene cluster, pyrP encodes a high affinity uracil transporter, which is expressed and regulated independently of upp, overview
overexpressing from plasmid in Escherichia coli strain NF1815
-
overexpression of wild-type and mutant P131D in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P131D
-
site-directed mutagenesis, 2-step mutagenic PCR, exchange of proline in 5-phosphoribose 1-diphosphate binding site, 50-60fold reduction of catalytic rate in both reaction directions, about 100fold increase in KM for uracil, strongly reduced Km for 5-phosphoribose 1-diphosphate
C128V
-
site-directed mutagenesis, required for structural sudy
K150A
-
site-directed mutagenesis, slightly reduced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy
K59A
-
site-directed mutagenesis, slightly enhanced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy
R68A
-
site-directed mutagenesis, slightly reduced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
biosynthetic labeling of RNA with uracil phosphoribosyltransferase allows cell-specific microarray analysis of mRNA synthesis and decay
medicine
pharmacology
-
potential target for the development of new antibiotics
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