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Information on EC 2.4.2.10 - orotate phosphoribosyltransferase
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EC Tree
2.4.2.10 orotate phosphoribosyltransferaseIUBMB Comments
The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase.
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Word Map
- 2.4.2.10
- pyrimidine
- 5-fluorouracil
- thymidylate
- dihydropyrimidine
- uridine
- thymidine
- uracil
- colorectal
- dihydroorotase
-
pyre
-
fluoropyrimidine
-
4.1.1.23
- orotidine-5'-monophosphate
-
5-fluoroorotic
-
transcarbamoylase
-
5-fu-based
- leucovorin
-
phosphoribosylpyrophosphate
-
5-fluorouracil-based
-
5-fu-related
-
prototrophy
-
tegafur
- odcase
- dihydrouracil
-
succinate-grown
-
5-phosphoribosyl
- fdump
-
5-fu-resistant
- podospora
-
phosphoribosyltransferases
- 5-fluoro-2'-deoxyuridine
-
fluoropyrimidine-based
- ompdc
-
5-phosphoribosyl-1-pyrophosphate
- anserina
- 1-pyrophosphate
- 5-fluorouridine
-
pyrophosphorolysis
- medicine
- diagnostics
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
oprt, orotate phosphoribosyltransferase, oprtase, orotate phosphoribosyl transferase, orotidine monophosphate pyrophosphorylase, omp synthase, orotidine-5'-phosphate pyrophosphorylase, orotic acid phosphoribosyltransferase, orotidylic acid pyrophosphorylase, type i phosphoribosyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
OPRT
OPRTase
orotate phosphoribosyl pyrophosphate transferase
-
-
-
-
orotate phosphoribosyl transferase
orotate phosphoribosyltransferase
orotate PRTase
-
-
-
-
orotic acid phosphoribosyltransferase
-
-
-
-
orotidine 5'-monophosphate pyrophosphorylase
orotidine 5'-phosphate pyrophosphorylase
-
-
-
-
orotidine monophosphate pyrophosphorylase
-
-
-
-
orotidine phosphoribosyltransferase
-
-
-
-
orotidine-5'-phosphate pyrophosphorylase
-
-
-
-
orotidylate phosphoribosyltransferase
-
-
-
-
orotidylate pyrophosphorylase
-
-
-
-
orotidylic acid phosphorylase
-
-
-
-
orotidylic acid pyrophosphorylase
-
-
-
-
orotidylic phosphorylase
-
-
-
-
orotidylic pyrophosphorylase
-
-
-
-
phosphoribosyltransferase, orotate
-
-
-
-
Pyr5
PyrE
rv0382c
ura5
additional information
OPRT
-
-
-
-
OPRT
-
-
OPRTase
-
-
-
-
orotate phosphoribosyltransferase
-
-
-
-
orotidine 5'-monophosphate pyrophosphorylase
-
-
-
-
additional information
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
additional information
-
constitutes together with orotidylate decarboxylase (EC 4.1.1.23) UMP-synthase, former complex U or multienzyme pyr-5,6
additional information
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
additional information
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
additional information
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
mechanism
-
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
mechanism
-
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
ping pong mechanism is not operable, NMR exchange experiments
-
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
mechanism is bi bi ping pong
-
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
random sequential kinetic mechanism
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
reaction scheme, half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to the enzyme supports an alternative variant of the Theorell-Chance mechanism with alternating site catalysis, in addition to a ping-pong bi-bi kinetic mechanism, overview
-
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
orotidine-5'-phosphate:diphosphate phospho-alpha-D-ribosyl-transferase
The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase.
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CAS REGISTRY NUMBER
COMMENTARY
9030-25-5
-
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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
5-fluoroorotate + 5-phospho-alpha-D-ribose 1-diphosphate
?
-
-
-
?
5-fluoroorotate + phosphoribose diphosphate
5-fluoroorotidine 5'-phosphate + diphosphate
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
orotate + 5-alpha-D-phosphorylribose 1-diphosphate
diphosphate + orotidine 5'-phosphate
-
-
-
-
?
orotate methylester + phosphoribose diphosphate
diphosphate + orotidine 4-methylester
-
-
-
-
?
uracil + phosphoribose diphosphate
diphosphate + uridine
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
essential enzyme for activation of 5-fluorouracil and its derivatives
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the activating OPRT and its antagonist the catabolizing dihydropyrimidine dehydrogenase play important roles in 5-fluorouracil metabolism, overview
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the enzyme is involved in degradation of 5-fluorouracil being the key enzyme related to the first-step activation process of 5-fluorouracil, and possibly predicts chemosensitivity to 5-fluorouracil, overview
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the enzyme is involved in the de novo biosynthesis of pyrimidine nucleotides, main enzyme involved in phosphoribosylation of 5-fluorouracil, an essential step that leads to tumor growth inhibition
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the enzyme is involved in the metabolism of 5-fluorouracil, a chemotherapeutic drug in treatment of solid cancers, major pathways of 5-fluorouracil metabolism, overview
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
reverse reaction: tri-, tetrapoly- or trimetaphosphate can replace diphosphate with 29%, 70% or 78% efficiency
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
involved in de novo synthesis of pyrimidine nucleotides
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
final steps in biosynthesis of UMP
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
i.e. orotidylate or OMP
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
final steps in biosynthesis of UMP
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
final steps in biosynthesis of UMP
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
Pyricularia oryzae ATCC MYA-4617
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
catalyzes stereospecific formation of beta-glycosidic bond between orotate and ribose 5'-phosphate portion of phospho-ribose diphosphate
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
predominant species of phosphoribose diphosphate: metal ion complex
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
high specificity for orotate
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
nucleotide-forming step in pyrimidine biosynthesis
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
involved in de novo synthesis of pyrimidine nucleotides
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotidine + diphosphate
orotate + alpha-D-ribose 1-diphosphate
-
-
-
-
?
orotidine + diphosphate
orotate + alpha-D-ribose 1-diphosphate
-
-
-
-
r
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
orotidine 5-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
orotidine 5-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
the compounds bind very tightly to the enzyme in a Mg2+-dependent manner, overview
the compounds bind very tightly to the enzyme in a Mg2+-dependent manner, overview
-
?
additional information
?
-
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
-
-
?
additional information
?
-
-
relationship between OPRT, antagonizing dihydropyrimidine dehydrogenase, and clinicopathologic features in cancer and treatment with 5-fluorouracil, relation of patients survival and enzyme activities after surgery, detailed overview
-
-
?
additional information
?
-
-
the enzyme expression is weakly correlated to 5-fluorouracil sensitivity and apoptotic cell rate, overview
-
-
?
additional information
?
-
-
the enzyme is associated with thymidylate synthase and dihydropyrimidine dehydrogenase in resectable colorectal cancer, overview, prognostic impact of the enzyme among 5-fluorouracil metabolic enzymes in resectable colorectal cancers treated by oral 5-fluorouracil-based adjuvant chemotherapy, overview
-
-
?
additional information
?
-
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
-
-
?
additional information
?
-
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
-
-
?
additional information
?
-
-
half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to the enzyme supports an alternative variant of the Theorell-Chance mechanism with alternating site catalysis, overview
-
-
?
additional information
?
-
-
enzyme from mammals is a bifunctional polypeptide, it also catalyzes the reaction listed as EC 4.1.1.23
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
orotidine 5-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
-
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
essential enzyme for activation of 5-fluorouracil and its derivatives
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the activating OPRT and its antagonist the catabolizing dihydropyrimidine dehydrogenase play important roles in 5-fluorouracil metabolism, overview
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the enzyme is involved in degradation of 5-fluorouracil being the key enzyme related to the first-step activation process of 5-fluorouracil, and possibly predicts chemosensitivity to 5-fluorouracil, overview
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the enzyme is involved in the de novo biosynthesis of pyrimidine nucleotides, main enzyme involved in phosphoribosylation of 5-fluorouracil, an essential step that leads to tumor growth inhibition
-
-
?
5-fluorouracil + 5-phospho-alpha-D-ribose 1-diphosphate
5-fluorouridine 5'-phosphate + diphosphate
-
the enzyme is involved in the metabolism of 5-fluorouracil, a chemotherapeutic drug in treatment of solid cancers, major pathways of 5-fluorouracil metabolism, overview
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
involved in de novo synthesis of pyrimidine nucleotides
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
final steps in biosynthesis of UMP
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
final steps in biosynthesis of UMP
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
final steps in biosynthesis of UMP
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
Pyricularia oryzae ATCC MYA-4617
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
-
r
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
nucleotide-forming step in pyrimidine biosynthesis
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
involved in de novo synthesis of pyrimidine nucleotides
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
orotidine 5'-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
additional information
?
-
-
relationship between OPRT, antagonizing dihydropyrimidine dehydrogenase, and clinicopathologic features in cancer and treatment with 5-fluorouracil, relation of patients survival and enzyme activities after surgery, detailed overview
-
-
?
additional information
?
-
-
the enzyme expression is weakly correlated to 5-fluorouracil sensitivity and apoptotic cell rate, overview
-
-
?
additional information
?
-
-
the enzyme is associated with thymidylate synthase and dihydropyrimidine dehydrogenase in resectable colorectal cancer, overview, prognostic impact of the enzyme among 5-fluorouracil metabolic enzymes in resectable colorectal cancers treated by oral 5-fluorouracil-based adjuvant chemotherapy, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
Mg2+
-
Mg2+ is necessary for the activity of the enzyme and can be substituted for by Mn2+ and Co2+
Mg2+
-
no orotate-Mg-complex formation, weak Mg-enzyme-complex
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3R,4S)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
(2R,3R,4S)-1-[2-(6-carboxy-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
(2S,3S,4R,5R)-2-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
(2S,3S,4R,5R)-2-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
(3R,4R)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
(7R,8R,9S,9aS)-8,9-dihydroxy-7-(hydroxymethyl)-8,9,9a,10-tetrahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidine-1,3,5(2H)-trione
2,6-dihydroxypyridine-4-carboxylic acid
-
competitive to orotate, uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate
3-(2-hydroxybenzylidene)-2,6-dioxo-1,2,3,6-tetrahydropyridine-4-carboxylic acid
-
competitive to orotate, uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate
3-benzylidene-2,6-dioxo-1,2,3,6-tetrahydropyridine-4-carboxylic acid
-
competitive to orotate, uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate
6-hydroxy-5-((2-hydroxyethylamino)methyl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
-
competitive to orotate, uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate
Orotic acid
-
when grown on glucose as carbon source, supplementation with orotic acid significantly decreases orotate phosphoribosyltransferase and orotidine 5'-monophoshate decarboxylase activities. In a strain deficient for dihydroorotase activity, orotic acid induces both phosphoribosyltransferase and orotidine 5'-monophoshate decarboxylase activites
[(2R,3R,4S,5S)-5-(4-carboxypyridin-3-yl)-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
[(2R,3R,4S,5S)-5-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
[(2R,3R,4S,5S)-5-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
[(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-4-hydroxypyrrolidin-1-ium-3-yl]methyl hydrogen phosphate
[(7R,8R,9S,9aS)-8,9-dihydroxy-1,3,5-trioxo-1,2,3,5,8,9,9a,10-octahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidin-7-yl]methyl hydrogen phosphate
(1R,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[(4-nitrophenyl)methyl]pyrrolidin-1-ium
-
-
(1R,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[(4-nitrophenyl)methyl]pyrrolidin-1-ium
-
-
(1S,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[2-(4-nitrophenyl)ethyl]pyrrolidin-1-ium
-
-
(1S,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[2-(4-nitrophenyl)ethyl]pyrrolidin-1-ium
-
-
(2R,3R,4S)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
-
(2R,3R,4S)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
-
(2R,3R,4S)-1-[2-(6-carboxy-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
-
(2R,3R,4S)-1-[2-(6-carboxy-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
-
(2R,3S)-3-hydroxy-2-(hydroxymethyl)-5-(4-nitrophenyl)pyrrolidin-1-ium
-
-
(2S,3S,4R,5R)-2-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
-
(2S,3S,4R,5R)-2-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
-
(2S,3S,4R,5R)-2-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
-
(2S,3S,4R,5R)-2-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
-
(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
-
(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
-
(3R,4R)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
-
(3R,4R)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
-
(7R,8R,9S,9aS)-8,9-dihydroxy-7-(hydroxymethyl)-8,9,9a,10-tetrahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidine-1,3,5(2H)-trione
-
-
(7R,8R,9S,9aS)-8,9-dihydroxy-7-(hydroxymethyl)-8,9,9a,10-tetrahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidine-1,3,5(2H)-trione
-
-
1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]pyrrolidin-1-ium
-
-
1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]pyrrolidin-1-ium
-
-
5-phospho-alpha-D-ribose 1-diphosphate
product inhibition, competitive to diphosphate, competitive to orotidine 5'-phosphate
5-phospho-alpha-D-ribose 1-diphosphate
-
phosphorolysis, product inhibition, kinetics
5-phospho-alpha-D-ribose 1-diphosphate
-
phosphorolysis, product inhibition, kinetics
diphosphate
product inhibition, noncompetitive to orotate, competitive to 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate
noncompetitive inhibition versus orotate, and noncompetitive versus 5-phospho-alpha-D-ribose 1-diphosphate with the bifunctional enzyme form, while competitive with the monofunctional and multienzyme form
diphosphate
-
product inhibition, kinetics
Orotate
product inhibition, noncompetitive to diphosphate, competitive to orotidine 5'-phosphate
Orotate
-
phosphorolysis, product inhibition, kinetics
orotidine 5'-phosphate
product inhibition, competitive to 5-phospho-alpha-D-ribose 1-diphosphate, competitive to orotate
orotidylate
-
product inhibition, kinetics
p-nitrophenyl beta-D-ribose 5'-phosphate
-
competitive inhibitor against orotidine 5'-phosphate
p-nitrophenyl beta-D-ribose 5'-phosphate
-
competitive inhibitor against orotidine 5'-phosphate
[(2R,3R,4S,5S)-5-(4-carboxypyridin-3-yl)-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
-
[(2R,3R,4S,5S)-5-(4-carboxypyridin-3-yl)-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
-
[(2R,3R,4S,5S)-5-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
-
[(2R,3R,4S,5S)-5-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
-
[(2R,3R,4S,5S)-5-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
-
[(2R,3R,4S,5S)-5-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
-
[(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-4-hydroxypyrrolidin-1-ium-3-yl]methyl hydrogen phosphate
-
-
[(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-4-hydroxypyrrolidin-1-ium-3-yl]methyl hydrogen phosphate
-
-
[(7R,8R,9S,9aS)-8,9-dihydroxy-1,3,5-trioxo-1,2,3,5,8,9,9a,10-octahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidin-7-yl]methyl hydrogen phosphate
-
-
[(7R,8R,9S,9aS)-8,9-dihydroxy-1,3,5-trioxo-1,2,3,5,8,9,9a,10-octahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidin-7-yl]methyl hydrogen phosphate
-
-
additional information
-
structural features of pyrimidine nucleobase inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0079
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, OPRT activity
0.009
5-phospho-alpha-D-ribose 1-diphosphate
ordered mechanism, pH 8.0, 25°C
0.0093
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OPRT activity
0.0113
5-phospho-alpha-D-ribose 1-diphosphate
37 °C, pH 8.0, native enzyme complex
0.0164
5-phospho-alpha-D-ribose 1-diphosphate
37 °C, pH 8.0, mixture of recombinant enzyme subunits
0.0286
5-phospho-alpha-D-ribose 1-diphosphate
37 °C, pH 8.0, recombinant monofunctional enzyme
0.0286
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OPRT activity
0.041
5-phospho-alpha-D-ribose 1-diphosphate
wild type enzyme
0.043
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme D131A
0.044
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.086
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme D131A/D132A
0.096
5-phospho-alpha-D-ribose 1-diphosphate
ping-pong mechanism, pH 8.0, 25°C
0.12
5-phospho-alpha-D-ribose 1-diphosphate
mutant enzyme D132A
0.0045
Orotate
37 °C, pH 8.0, mixture of recombinant enzyme subunits
0.007
Orotate
pH and temperature not specified in the publication, recombinant multienzyme complex, OPRT activity
0.0083
Orotate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OPRT activity
0.0182
Orotate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OPRT activity
0.091
Orotidine
-
pH not specified in the publication, temperature not specified in the publication
0.096
Orotidine
-
pH not specified in the publication, temperature not specified in the publication
0.00155
orotidine 5'-phosphate
-
in the presence of 1 mM diphosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.0016
orotidine 5'-phosphate
-
pH not specified in the publication, temperature not specified in the publication
0.00214
orotidine 5'-phosphate
-
in the presence of 20 mM phosphonoacetic acid, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.0026
orotidine 5'-phosphate
ping-pong mechanism, pH 8.0, 25°C
0.0029
orotidine 5'-phosphate
-
in the presence of 20 mM phosphonoacetic acid, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.0031 - 0.0036
orotidine 5'-phosphate
-
-
0.0037
orotidine 5'-phosphate
-
pH not specified in the publication, temperature not specified in the publication
0.00373
orotidine 5'-phosphate
-
in the presence of 1 mM diphosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
additional information
additional information
-
-
-
additional information
additional information
-
principles of assay
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
detailed kinetic analysis, isothermal titration calorimetry, the double Theorell-Chance mechanism yields a steady-state rate equation indistinguishable in form from the observed classical ping-pong bi-bi kinetics, steady-state kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.2
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OPRT activity
7.8
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, OPRT activity
3534
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OPRT activity
4.2
Orotate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OPRT activity
7.3
Orotate
pH and temperature not specified in the publication, recombinant multienzyme complex, OPRT activity
2972
Orotate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OPRT activity
0.014
orotidine 5'-phosphate
-
in the presence of 20 mM phosphonoacetic acid, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.017
orotidine 5'-phosphate
-
in the presence of 20 mM phosphonoacetic acid, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.1
orotidine 5'-phosphate
-
in the presence of 1 mM diphosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.28
orotidine 5'-phosphate
ping-pong mechanism, pH 8.0, 25°C
1.96
orotidine 5'-phosphate
-
in the presence of 1 mM diphosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6
5-phospho-alpha-D-ribose 1-diphosphate
ping-pong mechanism, pH 8.0, 25°C
6.6
5-phospho-alpha-D-ribose 1-diphosphate
ordered mechanism, pH 8.0, 25°C
111.88
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OPRT activity
987.3
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, OPRT activity
380000
5-phospho-alpha-D-ribose 1-diphosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OPRT activity
230.8
Orotate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, OPRT activity
1042.9
Orotate
pH and temperature not specified in the publication, recombinant multienzyme complex, OPRT activity
358072
Orotate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, OPRT activity
4.8
orotidine 5'-phosphate
-
in the presence of 20 mM phosphonoacetic acid, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
7.9
orotidine 5'-phosphate
-
in the presence of 20 mM phosphonoacetic acid, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
65
orotidine 5'-phosphate
-
in the presence of 1 mM diphosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
100
orotidine 5'-phosphate
ping-pong mechanism, pH 8.0, 25°C
530
orotidine 5'-phosphate
-
in the presence of 1 mM diphosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2 - 0.75
(1R,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[(4-nitrophenyl)methyl]pyrrolidin-1-ium
0.23 - 0.57
(1S,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[2-(4-nitrophenyl)ethyl]pyrrolidin-1-ium
0.08 - 0.27
(2R,3R,4S)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
0.29 - 0.69
(2R,3R,4S)-1-[2-(6-carboxy-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
0.35 - 0.53
(2S,3S,4R,5R)-2-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
0.3 - 0.36
(2S,3S,4R,5R)-2-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
0.083 - 0.22
(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
0.52 - 1.3
(3R,4R)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
0.11 - 0.27
(7R,8R,9S,9aS)-8,9-dihydroxy-7-(hydroxymethyl)-8,9,9a,10-tetrahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidine-1,3,5(2H)-trione
0.25 - 0.47
1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]pyrrolidin-1-ium
0.0074 - 0.014
3-(2-hydroxybenzylidene)-2,6-dioxo-1,2,3,6-tetrahydropyridine-4-carboxylic acid
0.0062 - 0.0135
6-hydroxy-5-((2-hydroxyethylamino)methyl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
4.3 - 15.5
[(2R,3R,4S,5S)-5-(4-carboxypyridin-3-yl)-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
0.2 - 0.37
[(2R,3R,4S,5S)-5-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
0.14 - 0.35
[(2R,3R,4S,5S)-5-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
0.24 - 0.5
[(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-4-hydroxypyrrolidin-1-ium-3-yl]methyl hydrogen phosphate
0.09 - 0.17
[(7R,8R,9S,9aS)-8,9-dihydroxy-1,3,5-trioxo-1,2,3,5,8,9,9a,10-octahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidin-7-yl]methyl hydrogen phosphate
0.2
(1R,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[(4-nitrophenyl)methyl]pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.75
(1R,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[(4-nitrophenyl)methyl]pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.23
(1S,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[2-(4-nitrophenyl)ethyl]pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.57
(1S,3R,4R)-3-hydroxy-4-(hydroxymethyl)-1-[2-(4-nitrophenyl)ethyl]pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.08
(2R,3R,4S)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.27
(2R,3R,4S)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.29
(2R,3R,4S)-1-[2-(6-carboxy-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.69
(2R,3R,4S)-1-[2-(6-carboxy-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3,4-dihydroxy-2-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.23
(2R,3S)-3-hydroxy-2-(hydroxymethyl)-5-(4-nitrophenyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.48
(2R,3S)-3-hydroxy-2-(hydroxymethyl)-5-(4-nitrophenyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.35
(2S,3S,4R,5R)-2-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.53
(2S,3S,4R,5R)-2-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.3
(2S,3S,4R,5R)-2-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.36
(2S,3S,4R,5R)-2-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxy-5-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.083
(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.22
(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.52
(3R,4R)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
1.3
(3R,4R)-1-[2-(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethyl]-3-hydroxy-4-(hydroxymethyl)pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.11
(7R,8R,9S,9aS)-8,9-dihydroxy-7-(hydroxymethyl)-8,9,9a,10-tetrahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidine-1,3,5(2H)-trione
-
at pH 8.0 and 25°C
0.27
(7R,8R,9S,9aS)-8,9-dihydroxy-7-(hydroxymethyl)-8,9,9a,10-tetrahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidine-1,3,5(2H)-trione
-
at pH 8.0 and 25°C
0.15
1,3-dihydroxy-N-[(4-nitrophenyl)methyl]propan-2-aminium
-
at pH 8.0 and 25°C
0.5
1,3-dihydroxy-N-[(4-nitrophenyl)methyl]propan-2-aminium
-
at pH 8.0 and 25°C
0.12
1,3-dihydroxy-N-[2-(4-nitrophenyl)ethyl]propan-2-aminium
-
at pH 8.0 and 25°C
0.51
1,3-dihydroxy-N-[2-(4-nitrophenyl)ethyl]propan-2-aminium
-
at pH 8.0 and 25°C
0.25
1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.47
1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]pyrrolidin-1-ium
-
at pH 8.0 and 25°C
0.00025
2,6-dihydroxypyridine-4-carboxylic acid
-
competitive to orotate, pH 8.0, 25°C
0.0082
2,6-dihydroxypyridine-4-carboxylic acid
-
uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate, pH 8.0, 25°C
0.0074
3-(2-hydroxybenzylidene)-2,6-dioxo-1,2,3,6-tetrahydropyridine-4-carboxylic acid
-
competitive to orotate, pH 8.0, 25°C
0.014
3-(2-hydroxybenzylidene)-2,6-dioxo-1,2,3,6-tetrahydropyridine-4-carboxylic acid
-
uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate, pH 8.0, 25°C
0.00019
3-benzylidene-2,6-dioxo-1,2,3,6-tetrahydropyridine-4-carboxylic acid
-
competitive to orotate, pH 8.0, 25°C
0.0065
3-benzylidene-2,6-dioxo-1,2,3,6-tetrahydropyridine-4-carboxylic acid
-
uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate, pH 8.0, 25°C
0.0423
5-phospho-alpha-D-ribose 1-diphosphate
pH 8.0, 37°C, cosubstrate diphosphate
0.1501
5-phospho-alpha-D-ribose 1-diphosphate
pH 8.0, 37°C, cosubstrate orotidine 5'-phosphate
0.0062
6-hydroxy-5-((2-hydroxyethylamino)methyl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
-
competitive to orotate, pH 8.0, 25°C
0.0135
6-hydroxy-5-((2-hydroxyethylamino)methyl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
-
uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate, pH 8.0, 25°C
0.001
diphosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, versus OPRT activity and substrate 5-phospho-alpha-D-ribose 1-diphosphate
0.007
diphosphate
pH and temperature not specified in the publication, recombinant multienzyme complex, versus OPRT activity and substrate orotate
0.026
diphosphate
mixed type inhibition, 5-phospho-alpha-D-ribose 1-diphosphate varied substrate, orotate unsaturated, pH 8.0, 25°C
0.029
diphosphate
mixed type inhibition, orotate varied substrate, 5-phospho-alpha-D-ribose 1-diphosphate unsaturated, pH 8.0, 25°C
0.08
diphosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, versus OPRT activity and substrate orotate
0.108
diphosphate
noncompetitive, 5-phospho-alpha-D-ribose 1-diphosphate varied substrate, orotate saturated, pH 8.0, 25°C
0.125
diphosphate
pH 8.0, 37°C, cosubstrate 5-phospho-alpha-D-ribose 1-diphosphate
0.125
diphosphate
pH and temperature not specified in the publication, recombinant monofunctional enzyme, versus OPRT activity and substrate 5-phospho-alpha-D-ribose 1-diphosphate
0.209
diphosphate
mixed type inhibition, orotate varied substrate, 5-phospho-alpha-D-ribose 1-diphosphate saturated, pH 8.0, 25°C
1.006
diphosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, versus OPRT activity and substrate 5-phospho-alpha-D-ribose 1-diphosphate
1.077
diphosphate
pH and temperature not specified in the publication, recombinant bifunctional enzyme, versus OPRT activity and substrate orotate
0.00044
orotidine 5'-phosphate
mixed type inhibition, 5-phospho-alpha-D-ribose 1-diphosphate varied substrate, orotate unsaturated, pH 8.0, 25°C
0.001
orotidine 5'-phosphate
mixed type inhibition, 5-phospho-alpha-D-ribose 1-diphosphate varied substrate, orotate saturated, pH 8.0, 25°C
0.0074
orotidine 5'-phosphate
mixed type inhibition, orotate varied substrate, 5-phospho-alpha-D-ribose 1-diphosphate unsaturated, pH 8.0, 25°C
0.0157
orotidine 5'-phosphate
pH 8.0, 37°C, cosubstrate 5-phospho-alpha-D-ribose 1-diphosphate
0.035
orotidine 5'-phosphate
noncompetitive, orotate varied substrate, 5-phospho-alpha-D-ribose 1-diphosphate saturated, pH 8.0, 25°C
0.000121
p-nitrophenyl beta-D-ribose
-
in the presence of orotidine 5'-phosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.000188
p-nitrophenyl beta-D-ribose
-
in the presence of orotidine 5'-phosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.00004
p-nitrophenyl beta-D-ribose 5'-phosphate
-
in the presence of orotidine 5'-phosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
0.000041
p-nitrophenyl beta-D-ribose 5'-phosphate
-
in the presence of orotidine 5'-phosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2
2.7
sulfate
-
orotidine 5'-phosphate as substrate, pH not specified in the publication, temperature not specified in the publication
3.1
sulfate
-
orotidine 5'-phosphate as substrate, pH not specified in the publication, temperature not specified in the publication
10.8
sulfate
-
orotidine 5'-phosphate as substrate, pH not specified in the publication, temperature not specified in the publication
17.6
sulfate
-
orotidine 5'-phosphate as substrate, pH not specified in the publication, temperature not specified in the publication
4.3
[(2R,3R,4S,5S)-5-(4-carboxypyridin-3-yl)-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
15.5
[(2R,3R,4S,5S)-5-(4-carboxypyridin-3-yl)-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.2
[(2R,3R,4S,5S)-5-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.37
[(2R,3R,4S,5S)-5-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.14
[(2R,3R,4S,5S)-5-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.35
[(2R,3R,4S,5S)-5-[(6-cyano-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]-3,4-dihydroxypyrrolidin-1-ium-2-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.24
[(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-4-hydroxypyrrolidin-1-ium-3-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.5
[(3R,4R)-1-[(6-carboxy-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)methyl]-4-hydroxypyrrolidin-1-ium-3-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.09
[(7R,8R,9S,9aS)-8,9-dihydroxy-1,3,5-trioxo-1,2,3,5,8,9,9a,10-octahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidin-7-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
0.17
[(7R,8R,9S,9aS)-8,9-dihydroxy-1,3,5-trioxo-1,2,3,5,8,9,9a,10-octahydro-7H-pyrrolo[1',2':4,5]pyrazino[1,2-c]pyrimidin-7-yl]methyl hydrogen phosphate
-
at pH 8.0 and 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17
2
crude enzyme, at pH 8.0, temperature not specified in the publication
225
-
recombinant enzyme after 17fold purification, in the presence of Mn2+
24
-
recombinant enzyme from crude cell extract, in the presence of Mg2+
423
-
recombinant enzyme after 17fold purification, in the presence of Mg2+
71
-
recombinant enzyme after 17fold purification, in the presence of Co2+
additional information
17
after 8.5fold purification, at pH 8.0, temperature not specified in the publication
additional information
-
ELISA assay method development and evaluation for enzyme detection and quantification in cancer tissue, overview
additional information
-
enzyme expression rate in tumor tissue with or without treatment with 5-fluorouracil
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
-
preferred buffer: Tris-HCl, when substrates are non-saturating, phosphate buffer, when substrate are saturating, not: maleate, imidazole, N-tris[hydroxymethyl] methyl-2-aminoethane-sulfonic acid (i.e. TES) or 3-[N-morpholino]-2-hydroxypropanesulfonic acid (i.e. MOPS) buffer
additional information
-
2 isozymes: pI: 5.65 (minor form), pI: 5.85 (major form)
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 9.2
-
about half-maximal activity at pH 7.2 and about 70% of maximal activity at pH 9.2
8.5 - 10.5
-
about half-maximal activity at pH 8.5 and about 70% of maximal activity at pH 10.5, wild-type
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 17536. When grown on glucose as carbon source, supplementation with orotic acid significantly decreases orotate phosphoribosyltransferase and orotidine 5'-monophoshate decarboxylase activities. In a strain deficient for dihydroorotase activity, orotic acid induces both phosphoribosyltransferase and orotidine 5'-monophoshate decarboxylase activites
-
-
brenda
K-12, overproducing strains C-600(pNE24) (wild-type) and its purine-sensitive mutant PS100(pNE31), both harbouring hybrid multi-copy plasmids
-
-
brenda
-
4187, 489721, 489731, 658935, 672923, 673097, 673120, 674045, 674056, 676267, 676270, 676296, 677169, 684221, 684875, 685814, 685927, 686922, 687155, 689294, 704190, 706021, 706023, 706025, 721644, 722451, 735748, 736435, 759577, 759774, 760110
-
-
brenda
multienzyme complex together with orotidine 5-monophosphate decarboxylase
-
-
brenda
-
-
-
brenda
structural gene pyrE cloned and overexpressed via multi-copy plasmid in Escherichia coli strain MB13
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in normal non-neoplastic colorectal epithelium, granular staining is observed only in the crypt
brenda
-
in gallbladder carcinoma, mucosal neoplastic epithelium shows dense cytoplasmic expression but expression is absent in the deeply invasive lesions
brenda
-
mucosal neoplastic epithelium, granular expression
brenda
-
OPRT is involved in early events of invasion of hepatocellular carcinoma cells
brenda
-
normal tissue, hormone-sensitive prostate cancer (HSPC) or hormonerefractory prostate cancer (HRPC) tissue
brenda
-
gastric cancer cell line with low baseline expression levels of OPRT
brenda
additional information
-
colorectal cancer, 150 patients with cancer at different stages, stage-related enzyme expression level, overview
brenda
-
221 specimen, expression profile of the enzyme and its antagonist dihydropyrimidine dehydrogenase both active in 5-fluorouracil metabolism, the enzyme expression levels correlate, overview
brenda
-
OPRT levels are high in well differentiated and localized gastric carcinomas and are significantly higher in gastric carcinoma tissue than in normal gastric mucosa
brenda
-
gastric cancer cell line with low baseline expression levels of OPRT
brenda
-
OPRT is involved in early events of pancreatic carcinogenesis
brenda
additional information
-
expression analysis in carcinoma cell lines, no expression in pancreatic ducts and PanIN-1A cells, overview
brenda
additional information
-
the enzyme expression is increased in tumor tissue compared to non-tumor tissue
brenda
additional information
-
in mucosal carcinoma lesions frequency of OPRT expression is 32.1%, in infiltrative lesions frequency of OPRT expression is 69.8%. In lymphovascularly invasive lesions frequency of OPRT expression is 88.2% and in metastatic lymph nodes frequency of OPRT expression is 88.8%
brenda
additional information
-
MKN-45/F2R cell, 5-fluorouracil resistant gastric cancer cell line
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in metastatic lymph nodes and lymphovascularly invasive lesions
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
fusion of the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a C-terminal orotate phosphoribosyltransferase (OPRT) and an N-terminal orotidine 5'-monophosphate decarboxylase (OMPDC), as OMPDC-OPRT, are described in many organisms. During evolution a gene fusion (i.e., the new gene coding for hybrid protein) is the immediate form between a stand-alone gene of a monofunctional enzyme and a gene fission of multienzyme complex (i.e., single gene from multiple smaller coding segments) responsible for protein-protein interaction, in response to different allosteric controls
malfunction
-
decreased activity of OPRT plays an important role in the acquired resistance of gastric cancer cells towards 5-fluorouracil. OPRT-knockout MKN-45 parent cells using small interfering RNA demonstrate 15.8fold increased resistance to 5-fluorouracil compared to the control cell
physiological function
physiological function
the enzyme is required for mycelial growth, appressorial turgor pressure and penetration into plant tissues, invasive hyphal growth, and pathogenicity
physiological function
Pyricularia oryzae ATCC MYA-4617
-
the enzyme is required for mycelial growth, appressorial turgor pressure and penetration into plant tissues, invasive hyphal growth, and pathogenicity
-
Show AA Sequence and Transmembrane Helices (44599 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
158000
recombinant bifunctional OMPDC-OPRT enzyme, gel filtration
18761
2 * 20000, SDS-PAGE, gel filtration; 2 * 18761, mass spectrometry, gel filtration
20000
32000
33000
33400
2 * 33400, recombinant enzyme, SDS-PAGE, 2 * 33000, calculated
38000
51500
52000
67000
140000
gel filtration and SDS-PAGE of native enzyme crosslinked with dimethyl suberimidate
20000
2 * 20000, SDS-PAGE, gel filtration; 2 * 18761, mass spectrometry, gel filtration
32000
-
2 * 32000, enzyme subunit, + 2 * 38000, orotidine 5-monophosphate decarboxylase subunit, SDS-PAGE
32000
2 * 32000, enzyme subunit, + 2 * 38000, orotidine 5-monophosphate decarboxylase subunit, SDS-PAGE, native enzyme
33000
2 * 33400, recombinant enzyme, SDS-PAGE, 2 * 33000, calculated
33000
2 * 33000, SDS-PAGE. Orotate phosphoribosyltransferase and orotidine 5-monophosphate decarboxylase exist physically as a heterotetrameric enzyme complex containing two subunits of each enzyme
38000
-
2 * 32000, enzyme subunit, + 2 * 38000, orotidine 5-monophosphate decarboxylase subunit, SDS-PAGE
38000
2 * 32000, enzyme subunit, + 2 * 38000, orotidine 5-monophosphate decarboxylase subunit, SDS-PAGE, native enzyme
51500
-
1 * 51500, SDS-PAGE, enzyme activity and orotidine 5-monophosphate decarboxylating activity on a single polypeptide
51500
-
x * 51500, SDS-PAGE, sedimentation studies reveal monomer or dimer, enzyme activity and orotidine 5-monophosphate decarboxylating activity on a single polypeptide
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
-
1 * 51500, SDS-PAGE, enzyme activity and orotidine 5'-monophosphate decarboxylating activity on a single polypeptide
tetramer
additional information
?
-
x * 51500, SDS-PAGE, sedimentation studies reveal monomer or dimer, enzyme activity and orotidine 5'-monophosphate decarboxylating activity on a single polypeptide
dimer
2 * 33400, recombinant enzyme, SDS-PAGE, 2 * 33000, calculated
dimer
2 * 33000, OPRT subunits, + 2 * 38000, OMPDC subunits, SDS-PAGE
dimer
-
homodimer, with catalytically important residues from one subunit available for the other, crystalline structure
homodimer
2 * 20000, SDS-PAGE, gel filtration; 2 * 18761, mass spectrometry, gel filtration
homodimer
-
2 * 20000, SDS-PAGE, gel filtration; 2 * 18761, mass spectrometry, gel filtration
-
homodimer
2 * 33000, SDS-PAGE. Orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase exist physically as a heterotetrameric enzyme complex containing two subunits of each enzyme
tetramer
-
2 * 32000, enzyme subunit, + 2 * 38000, orotidine 5-monophosphate decarboxylase subunit, SDS-PAGE
tetramer
2 * 32000, enzyme subunit, + 2 * 38000, orotidine 5-monophosphate decarboxylase subunit, SDS-PAGE, native enzyme
additional information
three-dimensional structure of the bifunctional OMPDC-OPRT (residues 1-323 and 324-604, respectively) is predicted using the crystal structure of Leishmania donovani UMPS (PDB ID 3QW4) as template with OMPDC (residues 1-323) and OPRT (residues 387-604) in which residues 324-386 are not present in the homology model
additional information
-
three-dimensional structure of the bifunctional OMPDC-OPRT (residues 1-323 and 324-604, respectively) is predicted using the crystal structure of Leishmania donovani UMPS (PDB ID 3QW4) as template with OMPDC (residues 1-323) and OPRT (residues 387-604) in which residues 324-386 are not present in the homology model
additional information
-
active site of enzyme requires D125 of one subunit and K103 of second subunit
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method. Enzyme in complex with phosphate: 0.1 M HEPES pH 7.5, 10% (w/v) PEG8000, 8% (v/v) ethylene glycol. Enzyme in complex with 5-phospho-alpha-D-ribose 1-diphosphate: 0.1 M HEPES pH 7.5, 10% (w/v) PEG6000, 5% (v/v) 2-methyl-2,4-pentanediol. Enzyme in complex with ferric dicitrate: 0.01 M iron(III) chloride hexahydrate, 0.1 M sodium citrate tribasic dehydrate pH 6.1, 10% (v/v) and Jeffamine M-600
hanging drop vapor diffusion method, using 100 mM ammonium sulfate, 30% (w/v) PEG 3350, at 4°C
sitting drop vapour diffusion method, the apoenzyme is crystallized in 100 mM Tris-HCl, pH 7.4, 0.2 M magnesium acetate, and 26% (w/v) PEG 6000, crystals of OPRTase in complex with substrates (5.0 mM 5-phospho-alpha-D-ribose 1-diphosphate and 5.0 mM orotate) or product (5.0 mM orotidine 5'-phosphate) are grown in 100 mM sodium acetate, pH 4.6, 0.14 M ammonium acetate, and 38% (w/v) PEG 4000, crystals of the OMP complex are grown from solutions containing 100 mM Tris HCl, pH 7.4, 0.08 M magnesium acetate, and 28% (w/v) PEG 6000
complexed with orotidine monophosphate, homodimer, with catalytically important residues from one subunit available for the other
-
hanging-grop vapour-diffusion method, 2.3 M ammonium sulfate, pH 8.6
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G213A
-
OPRT, the gene polymorphism predicts toxicity in patients treated with bolus 5-fluorouracil regimen, the Ala allele in the enzyme G213A polymorphism and the two tandem repeats in the TYMS promoter polymorphism are associated with grade 3 to 4 neutropenia and diarrhea, distribution in 69 patients samples, genotyping, relationship between OPRT mRNA expression and the OPRT G213A polymorphism, overview
G133D
D125N
-
active site of enzyme requires D125 of one subunit and K103 of second subunit
K103A
-
active site of enzyme requires D125 of one subunit and K103 of second subunit
additional information
additional information
-
mutational separation of catalytic activity of enzyme and EC4.1.1.23 activity results in active but unstable proteins
additional information
construction of a chimeric fusion enzyme from the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a C-terminal orotate phosphoribosyltransferase (OPRT) and an N-terminal orotidine 5'-monophosphate decarboxylase (OMPDC) as OMPDC-OPRT in Plasmodium falciparum, the chimeric mutant acts as a bifunctional enzyme. The activitiy, although unstable, is stabilized by the substrate and product during purification and long-term storage. The kcat is selectively enhanced up to three orders of magnitude, while the Km is not much affected and remains at low micromolar levels when compared to the monofunctional enzymes. The fusion of the two enzymes creates a super-enzyme with perfect catalytic power and more flexibility
additional information
-
construction of a chimeric fusion enzyme from the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a C-terminal orotate phosphoribosyltransferase (OPRT) and an N-terminal orotidine 5'-monophosphate decarboxylase (OMPDC) as OMPDC-OPRT in Plasmodium falciparum, the chimeric mutant acts as a bifunctional enzyme. The activitiy, although unstable, is stabilized by the substrate and product during purification and long-term storage. The kcat is selectively enhanced up to three orders of magnitude, while the Km is not much affected and remains at low micromolar levels when compared to the monofunctional enzymes. The fusion of the two enzymes creates a super-enzyme with perfect catalytic power and more flexibility
additional information
-
point mutations for negative complementation of enzyme activity
additional information
-
deletion of 1-5 C-terminal amino acids, activities reduced to 22%-75% of wild type activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
OPRTase activity decreases with the increase in incubation temperature and more than 50% of the activity is lost upon incubation at 50°C for 30 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0.05 mM UMP and 1% polyethyleneglycol stabilize during final stage of purification
-
5 mM Mg2+, 1 mM phosphoribose diphosphate and 2 mM DTT stabilize dilute enzyme solutions
-
native enzyme complex, stable for at least 6 months at -20°C or -80°C in 50 mM Hepes, pH 7.4, 300 mM NaCl, 5 mM dithiothreitol, 20% glycerol. At 4°C, loss of 50% of activity within 4 weeks.
recombinant enzyme dimer, stable for at least 3 months at -20°C or -80°C in 50 mM Hepes, pH 7.4, 5 mM dithiothreitol, 20% glycerol. In absence of dithiothreitol and glycerol, loss of 50% of activity during overnight storage at 4°C.
recombinant enzyme, stable for at least 3 months at 4°C or -20°C in presence of 1 mM dithiothreitol and 10% glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-25°C, in 50% v/v glycerol, 0.1 mM DTT, about 35% loss of activity within 40 days
-
4°C, 50 mM Tris-HCl, 2 mM EDTA, 2 mM mercaptoethanol, pH 6.4, several months, no apparent loss of activity
-
4°C, purified recombinant bifunctional enzyme, stability property of both domains in the bifunctional enzyme in the absence or presence of 0.5 mM PRPP and 0.5 mM UMP: half-life of the OPRT activity is about 3-4 days and 3 weeks, respectively. The OMPDC activity is much more stable with half-life of about 3-4 weeks. 90% of the bifunctional protein, stored for 4 weeks, remains as a bifunctional protein band in SDS-PAGE and image analyses
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose Fast Flow column chromatography, and Superdex-75 gel filtration
-
anion exchange chromatography, gel filtration, hydrophobic interaction chromatography
HisTrap column chromatography, HiTrap Q-Sepharose column chromatography, and S200 XK gel filtration
immobilized metal ion affinity chromatography (Co2+), His-tag cleavage (TEV protease), immobilized metal ion affinity chromatography (Co2+)
-
immobilized metal ion affinity chromatography (Ni2+), gel filtration
Ni-NTA column chromatography and Sephacryl 200 gel filtration
Ni2+ affinity column
partial, affinity chromatography on Blue-Dextran- or Cibacron Blue F3GA-Sepharose
-
recombinant enzyme
recombinant His-tagged chimeric fusion enzyme from Escherichia coli by nickel affinity and anion exchange chromatography to near homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
functional recombinant expression of the His-tagged chimeric fusion enzyme in Escherichia coli
His-tagged protein expressed in Escherichia coli BL21(DE3)
His-tagged protein expressed in Escherichia coli BL21(DE3), gel filtration
-
into the pDONR221 vector, expressed from pDEST14-OPRT in Escherichia coli BL21-AI competent cells
-
OPRT, stable overexpression in the gastric cancer cell lines TMK-1 and MKN-45, enhancing the effect of 5-fluorouracil on the cells, transfected cells show a similar growth curve as the wild-type parent cells, while the drug sensitivity is increased compared to the untransfected cells, overview
-
structural gene pyrE, subcloned from a genomic library in pBR328(pAV002), transduced into pyr-auxotroph Salmonella typhimurium strain SA2434 with phage P22, finally cloned to and expressed in overproducing strain Escherichia coli MB13
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is extremely high in malignant pleural mesothelioma tumor tissue
-
lexpression of OPRT in mucosal carcinoma components, in infiltrative components, in lymphovascularly invasive lesions and in metastatic lymph nodes. No significant correlation between OPRT expression and cancer stage, T-grade or N-grade, but OPRT expression correlates positively with the presence of lymphovascular invasion. OPRT is diffusely expressed to a greater extent, especially in the tumor cells adjacent to the infiltrative margin
-
mRNA expression of OPRT is markedly decreased to 12.4% and activity to 46.9% in the 5-fluorouracil resistant MKN-45/F2R cell line compared to the MKN-45 parent cell line. OPRT gene expression is markedly decreased to 14.4% when down-regulated by siRNA
-
strong expression of OPRT in prostate cancer cells, significant correlation between OPRT mRNA expression levels and the tumor pathological grade. The OPRT/dihydropyrimidine dehydrogenase expression ratio in the HRPC group is significantly higher than that in the low grade HSPC group
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
diagnostics
-
OPRT activity in tumor tissue is a predictor of prognosis in resectable CRC patients treated by oral 5-fluorouracil-based adjuvant chemotherapy, and is useful to pick-up high risk patients independent from known prognosis factors
medicine
-
enzyme activity is 7.5fold enhanced in bladder carcinoma compared to normal. Bladder carcinoma subtypes show distinct levels of enzyme activity and there is positive association between the activity levels of enzyme and thymidylate synthase/thymidine kinase. Enzyme activity in bladder carcinoma cells also correlates positively with their sensitivity to 5-fluorouracil
medicine
-
immunochemical detection of tumoral enzyme expression by antibody, method for predicting the clinical response to 5-fluorouracil-based chemotherapy
medicine
-
OPRT activity is significantly lower in tumors with lymph node metastasis than in tumors lacking lymph node metastasis, thus OPRT activity level in tumor tissue may be an important prognostic factor for survival in Dukes B and C colorectal carcinoma cells with radical resection and adjuvant chemotherapy with orally administered tegafur/uracil
medicine
-
OPRT expression is negatively associated with colorectal cancer progression
medicine
-
the expression of OPRT may be useful to predict the response to adjuvant chemotherapy with 5-fluorouracil in human pancreatic cancer
medicine
-
the OPRT mRNA level is positively correlated with the 5-fluorouracil efficacy in antitumor therapy
medicine
-
the enzyme is used as a predictor of benefit from S-1 adjuvant chemotherapy for cholangiocarcinoma patients. Cholangiocarcinoma patients with high enzyme expression can benefit from postoperative adjuvant S-1 therapy, which increases the disease-free survival
medicine
-
the expression of the enzyme shows no association with the overall survival or diseasex1efree survival, even in the patients who receive Sx1e1 adjuvant chemotherapy
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303
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Orotate phosphoribosyltransferase (yeast)
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Saccharomyces cerevisiae
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Divalent metal ion activation of the yeast orotate phosphoribosyltransferase catalyzed reaction
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18
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Purification of orotate phosphoribosyltransferase and orotidylate decarboxylase by affinity chromatography on Sepharose dye derivatives
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88
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Saccharomyces cerevisiae
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98
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1985
Escherichia coli
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Orotidylate-metabolizing enzymes of the human malarial parasite, Plasmodium falciparum, differ from host cell enzymes
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29
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1990
Salmonella enterica subsp. enterica serovar Typhimurium
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230
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1993
Salmonella enterica subsp. enterica serovar Typhimurium
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Orotate Phosphoribosyltransferase and orotidine-5'-monophosphate decarboxylase of black gram (phaseolus mungo) seedlings
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87
225-241
1978
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-
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34
10764-10770
1995
Salmonella enterica subsp. enterica serovar Typhimurium
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58
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1999
Toxoplasma gondii
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Transition state structure of Salmonella typhimurium orotate phosphoribosyltransferase
Biochemistry
35
14-21
1996
Salmonella enterica subsp. enterica serovar Typhimurium
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125
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Thermus thermophilus
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118
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A nonradioactive high-performance liquid chromatographic microassay for uridine 5'-monophosphate synthase, orotate phosphoribosyltransferase, and orotidine 5'-monophosphate decarboxylase
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299
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Homo sapiens, Mus musculus
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Sequence and phylogenetic analysis of the Rhizobium leguminosarum biovar trifolii pyrE gene, overproduction, purification and characterization of orotate phosphoribosyltransferase
Gene
195
329-336
1997
Rhizobium leguminosarum
brenda
Witte, J.F.; Tsou, R.; McClard, R.W.
Cloning, overproduction, and purification of native and mutant recombinant yeast orotate phosphoribosyltransferase and the demonstration from magnetization inversion transfer that a proposed oxocarbocation intermediate does not have a kinetic lifetime
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361
106-112
1999
Saccharomyces cerevisiae
brenda
Henriksen, A.; Aghajari, N.; Jensen, K.F.; Gajhede, M.
A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase
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35
3803-3809
1996
Escherichia coli
brenda
Scapin, G.; Grubmeyer, C.; Sacchettini, J.C.
Crystal structure of orotate phosphoribosyltransferase
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33
1287-1294
1994
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Krungkrai, S.R.; Prapunwattana, P.; Horii, T.; Krungkrai, J.
Orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase exist as multienzyme complex in human malaria parasite Plasmodium falciparum
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318
1012-1018
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Plasmodium falciparum
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Krungkrai, S.R.; DelFraino, B.J.; Smiley, J.A.; Prapunwattana, P.; Mitamura, T.; Horii, T.; Krungkrai, J.
A novel enzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase in human malaria parasite Plasmodium falciparum: physical association, kinetics, and inhibition characterization
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44
1643-1652
2005
Plasmodium falciparum (Q8T6J6), Plasmodium falciparum
brenda
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Cloning and sequencing of the ura3 and ura5 genes, and isolation and characterization of uracil auxotrophs of the fungus Mortierella alpina 1S-4
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68
277-285
2004
Mortierella alpina, Mortierella alpina 1S-4
brenda
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Prognostic significance of orotate phosphoribosyltransferase activity in bladder carcinoma
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100
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Homo sapiens
brenda
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16
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Homo sapiens
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Human malaria parasite orotate phosphoribosyltransferase: functional expression, characterization of kinetic reaction mechanism and inhibition profile
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134
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Plasmodium falciparum (Q8N0R1), Plasmodium falciparum
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Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori
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15
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Helicobacter pylori
brenda
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Half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to orotate phosphoribosyltransferase from Saccharomyces cerevisiae supports a novel variant of the Theorell-Chance mechanism with alternating site catalysis
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45
5330-5342
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Saccharomyces cerevisiae
brenda
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53
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Homo sapiens
brenda
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12
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Homo sapiens
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118
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Homo sapiens
brenda
Kawai, K.; Watabe, S.; Matsuda, M.; Sakamoto, K.; Kamano, T.
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35
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2005
Homo sapiens
brenda
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16
1165-1172
2006
Homo sapiens
brenda
Taomoto, J.; Yoshida, K.; Wada, Y.; Tanabe, K.; Konishi, K.; Tahara, H.; Fukushima, M.
Overexpression of the orotate phosphoribosyl-transferase gene enhances the effect of 5-fluorouracil on gastric cancer cell lines
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70
458-464
2006
Homo sapiens
brenda
Sanada, Y.; Yoshida, K.; Ohara, M.; Tsutani, Y.
Expression of orotate phosphoribosyltransferase (OPRT) in hepatobiliary and pancreatic carcinoma
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13
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Homo sapiens
brenda
Tokunaga, Y.; Sasaki, H.; Saito, T.
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141
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Homo sapiens
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48
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brenda
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41
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2008
Homo sapiens
brenda
Sakamoto, E.; Nagase, H.; Kobunai, T.; Oie, S.; Oka, T.; Fukushima, M.; Oka, T.
Orotate phosphoribosyltransferase expression level in tumors is a potential determinant of the efficacy of 5-fluorouracil
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363
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2007
Homo sapiens
brenda
Gonzalez-Segura, L.; Witte, J.F.; McClard, R.W.; Hurley, T.D.
Ternary complex formation and induced asymmetry in orotate phosphoribosyltransferase
Biochemistry
46
14075-14086
2007
Saccharomyces cerevisiae (P13298), Saccharomyces cerevisiae
brenda
Ishikawa, M.; Miyauchi, T.; Kashiwagi, Y.
Clinical implications of thymidylate synthetase, dihydropyrimidine dehydrogenase and orotate phosphoribosyl transferase activity levels in colorectal carcinoma following radical resection and administration of adjuvant 5-FU chemotherapy
BMC Cancer
8
188
2008
Homo sapiens
brenda
Kai, K.; Kitajima, Y.; Hiraki, M.; Satoh, S.; Tanaka, M.; Nakafusa, Y.; Tokunaga, O.; Miyazaki, K.
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258
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2007
Homo sapiens
brenda
Sakurai, Y.; Kamoshida, S.; Furuta, S.; Sunagawa, R.; Inaba, K.; Isogaki, J.; Komori, Y.; Uyama, I.; Tsutsumi, Y.
Levels and expressions of orotate phosphoribosyltransferase in gastric carcinoma and normal gastric mucosa tissues
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10
234-240
2007
Homo sapiens
brenda
Miyake, K.; Imura, S.; Yoshizumi, T.; Ikemoto, T.; Morine, Y.; Shimada, M.
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12
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2007
Homo sapiens
brenda
Wang, X.; Ma, C.; Wang, X.; Xu, P.
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189
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2007
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brenda
Nio, Y.; Toga, T.; Maruyama, R.; Fukushima, M.
Expression of orotate phosphoribosyl transferase in human pancreatic cancer: implication for the efficacy of uracil and tegafur-based adjuvant chemotherapy
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18
59-64
2007
Homo sapiens
brenda
Zhang, Y.; Luo, M.; Schramm, V.L.
Transition states of Plasmodium falciparum and human orotate phosphoribosyltransferases
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131
4685-4694
2009
Homo sapiens, Plasmodium falciparum
brenda
Sanada, Y.; Yoshida, K.; Hihara, J.; Okada, M.
Expression of orotate phosphoribosyltransferase in colorectal carcinoma: an immunohistochemical analysis in several components of neoplastic lesions
Oncol. Rep.
20
1005-1011
2008
Homo sapiens
brenda
Tsutani, Y.; Yoshida, K.; Sanada, Y.; Wada, Y.; Konishi, K.; Fukushima, M.; Okada, M.
Decreased orotate phosphoribosyltransferase activity produces 5-fluorouracil resistance in a human gastric cancer cell line
Oncol. Rep.
20
1545-1551
2008
Homo sapiens
brenda
Tanaka, T.; Kawashima, H.; Matsumura, K.; Yamashita-Hosono, T.; Yoshimura, R.; Kuratsukuri, K.; Harimoto, K.; Nakatani, T.
Overexpression of orotate phosphoribosyl transferase in hormone-refractory prostate cancer
Oncol. Rep.
21
33-37
2009
Homo sapiens
brenda
Liu, C.; Xu, R.; Gao, Z.; Xu, J.; Hou, H.; Li, L.; She, Z.; Li, L.; Su, X.; Liu, P.; Dong, Y.
Structure of orotate phosphoribosyltransferase from the caries pathogen Streptococcus mutans
Acta Crystallogr. Sect. F
66
498-502
2010
Streptococcus mutans (Q8DTV2), Streptococcus mutans
brenda
Takashima, Y.; Mizohata, E.; Tokuoka, K.; Krungkrai, S.; Kusakari, Y.; Konishi, S.; Satoh, A.; Matsumura, H.; Krungkrai, J.; Horii, T.; Inoue, T.
Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum
Acta Crystallogr. Sect. F
68
244-246
2012
Plasmodium falciparum
brenda
Zhang, Y.; Schramm, V.
Ground-state destabilization in orotate phosphoribosyltransferases by binding isotope effects
Biochemistry
50
4813-4818
2011
Homo sapiens, Plasmodium falciparum
brenda
Hansen, M.; Harris, R.; Barr, E.; Cheng, H.; Girvin, M.; Grubmeyer, C.
Backbone 1H, 13C, 15N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate
Biomol. NMR Assign.
8
103-108
2014
Saccharomyces cerevisiae
brenda
Breda, A.; MacHado, P.; Rosado, L.; Souto, A.; Santos, D.; Basso, L.
Pyrimidin-2(1H)-ones based inhibitors of Mycobacterium tuberculosis orotate phosphoribosyltransferase
Eur. J. Med. Chem.
54
113-122
2012
Mycobacterium tuberculosis
brenda
Zhang, Y.; Deng, H.; Schramm, V.
Leaving group activation and pyrophosphate ionic state at the catalytic site of plasmodium falciparum orotate phosphoribosyltransferase
J. Am. Chem. Soc.
132
17023-17031
2010
Plasmodium falciparum
brenda
Zhang, Y.; Schramm, V.
Pyrophosphate interactions at the transition states of plasmodium falciparum and human orotate phosphoribosyltransferases
J. Am. Chem. Soc.
132
8787-8794
2010
Homo sapiens, Plasmodium falciparum
brenda
Breda, A.; Rosado, L.; Lorenzini, D.; Basso, L.; Santos, D.
Molecular, kinetic and thermodynamic characterization of Mycobacterium tuberculosis orotate phosphoribosyltransferase
Mol. Biosyst.
8
572-586
2012
Mycobacterium tuberculosis (P9WHK9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHK9)
brenda
Kumar, S.; Krishnamoorthy, K.; Mudeppa, D.G.; Rathod, P.K.
Structure of Plasmodium falciparum orotate phosphoribosyltransferase with autologous inhibitory protein-protein interactions
Acta Crystallogr. Sect. F
71
600-608
2015
Plasmodium falciparum (Q8N0R1), Plasmodium falciparum
brenda
Qi, Z.; Liu, M.; Dong, Y.; Yang, J.; Zhang, H.; Zheng, X.; Zhang, Z.
Orotate phosphoribosyl transferase MoPyr5 is involved in uridine 5-phosphate synthesis and pathogenesis of Magnaporthe oryzae
Appl. Microbiol. Biotechnol.
100
3655-3666
2016
Pyricularia oryzae (G4MT58), Pyricularia oryzae, Pyricularia oryzae ATCC MYA-4617 (G4MT58)
brenda
Imprasittichail, W.; Roytrakul, S.; Krungkrai, S.R.; Krungkrail, J.
A unique insertion of low complexity amino acid sequence underlies protein-protein interaction in human malaria parasite orotate phosphoribosyltransferase and orotidine 5-monophosphate decarboxylase
Asian Pac. J. Trop. Med.
7
184-192
2014
Plasmodium falciparum (Q8N0R1), Plasmodium falciparum
brenda
Hozumi, Y.; Tanaka, T.; Nakano, T.; Matsui, H.; Nasu, T.; Koike, S.; Kakehata, S.; Ito, T.; Goto, K.
Orotate phosphoribosyltransferase localizes to the Golgi complex and its expression levels affect the sensitivity to anti-cancer drug 5-fluorouracil
Biomed. Res.
36
403-409
2015
Homo sapiens
brenda
Subrahmanyeswara Rao, N.; Deshpande, P.
An organism-independent unified model for activity of orotate phosphoribosyltransferases for orotidine monophosphate synthesis
Chem. Eng. Sci.
128
109-118
2015
Saccharomyces cerevisiae, Mycobacterium tuberculosis, Plasmodium falciparum, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Surekha, K.; Prabhu, D.; Richard, M.; Nachiappan, M.; Biswal, J.; Jeyakanthan, J.
Investigation of vital pathogenic target orotate phosphoribosyltransferases (OPRTase) from Thermus thermophilus HB8: Phylogenetic and molecular modeling approach
Gene
583
102-111
2016
Thermus thermophilus (Q5SHI8), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SHI8)
brenda
Zhang, Y.; Evans, G.B.; Clinch, K.; Crump, D.R.; Harris, L.D.; Froehlich, R.F.; Tyler, P.C.; Hazleton, K.Z.; Cassera, M.B.; Schramm, V.L.
Transition state analogues of Plasmodium falciparum and human orotate phosphoribosyltransferases
J. Biol. Chem.
288
34746-34754
2013
Homo sapiens, Plasmodium falciparum
brenda
Paojinda, P.; Imprasittichai, W.; Krungkrai, S.R.; Palacpac, N.M.Q.; Horii, T.; Krungkrai, J.
Bifunctional activity of fused Plasmodium falciparum orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase
Parasitol. Int.
67
79-84
2018
Plasmodium falciparum (Q8N0R1), Plasmodium falciparum
brenda
Akahoshi, K.; Ban, D.; Kuboki, R.; Oba, A.; Ono, H.; Mitsunori, Y.; Kudo, A.; Tanaka, S.; Tanabe, M.
Orotate phosphoribosyltransferase as a predictor of benefit from S-1 adjuvant chemotherapy for cholangiocarcinoma patients
J. Gastroenterol. Hepatol.
34
1108-1115
2019
Homo sapiens
brenda
Okuda, K.; Tatematsu, T.; Yano, M.; Nakamae, K.; Yamada, T.; Kasugai, T.; Nishida, T.; Sano, M.; Moriyama, S.; Haneda, H.; Kawano, O.; Sakane, T.; Oda, R.; Watanabe, T.; Nakanishi, R.
The relationship between the expression of thymidylate synthase, dihydropyrimidine dehydrogenase, orotate phosphoribosyltransferase, excision repair cross-complementation group 1 and class III beta-tubulin, and the therapeutic effect of S-1 or carboplatin plus paclitaxel in nonx1esmallx1ecell lung cancer
Mol. Clin. Oncol.
9
21-29
2018
Homo sapiens
brenda
Hamamoto, Y.; Takeoka, S.; Mouri, A.; Fukusumi, M.; Wakuda, K.; Ibe, T.; Honma, C.; Arimoto, Y.; Yamada, K.; Wagatsuma, M.; Tashiro, A.; Kamoshida, S.; Kamimura, M.
Orotate phosphoribosyltransferase is overexpressed in malignant pleural mesothelioma Dramatically responds one case in high OPRT expression
Rare Dis.
4
e1165909
2016
Homo sapiens
brenda
Donini, S.; Ferraris, D.M.; Miggiano, R.; Massarotti, A.; Rizzi, M.
Structural investigations on orotate phosphoribosyltransferase from Mycobacterium tuberculosis, a key enzyme of the de novo pyrimidine biosynthesis
Sci. Rep.
7
1180
2017
Mycobacterium tuberculosis (P9WHK9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WHK9)
brenda
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