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Information on EC 4.1.1.23 - orotidine-5'-phosphate decarboxylase and Organism(s) Bacillus subtilis and UniProt Accession P25971

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.23 orotidine-5'-phosphate decarboxylase
IUBMB Comments
The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase .
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This record set is specific for:
Bacillus subtilis
UNIPROT: P25971
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
odcase, ump synthase, orotidine 5'-monophosphate decarboxylase, orotidine-5'-phosphate decarboxylase, omp decarboxylase, orotidine-5'-monophosphate decarboxylase, ompdc, orotidylate decarboxylase, orotidine monophosphate decarboxylase, orotidine 5'-phosphate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Decarboxylase, orotidine 5'-phosphate
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ODCase
OMP decarboxylase
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-
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OMP-DC
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-
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OMPDCase
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-
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OMPdecase
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-
-
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Orotate decarboxylase
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Orotate monophosphate decarboxylase
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Orotic decarboxylase
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Orotidine 5'-monophosphate decarboxylase
Orotidine 5'-phosphate decarboxylase
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Orotidine monophosphate decarboxylase
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Orotidine phosphate decarboxylase
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Orotidine-5'-monophosphate decarboxylase
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Orotidylate decarboxylase
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Orotidylic acid decarboxylase
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Orotidylic decarboxylase
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Orotodylate decarboxylase
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-
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UMP synthase
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-
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Uridine 5'-monophosphate synthase
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
reaction mechanism
orotidine 5'-phosphate = UMP + CO2
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
orotidine-5'-phosphate carboxy-lyase (UMP-forming)
The enzyme from higher eukaryotes is identical with EC 2.4.2.10 orotate phosphoribosyltransferase .
CAS REGISTRY NUMBER
COMMENTARY hide
9024-62-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
additional information
?
-
theoretical studies of the effect of thio substitution on orotidine monophosphate decarboxylase substrates
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
catalyzes the final step in the de novo biosynthesis of uridine monophosphate
-
?
Orotidine 5'-phosphate
UMP + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
metal-independent reaction
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-aminouridine 5'-monophosphate
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6-azauridine 5'-monophosphate
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6-cyanouridine 5'-monophosphate
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6-iodouridine 5'-monophosphate
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6-thiocarboxamidouridine 5'-monophosphate
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barbituric acid ribonucleoside 5'-monophosphate
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pyrazofurin 5'-monophosphate
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xanthosine 5'-monophosphate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
active form, subunit structure
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray crystal structure with bound uridine 5’-monophosphate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unliganded enzyme without bound UMP or OMP forms heavy precipitates during purification
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miller, B.G.; Wolfenden, R.
Catalytic proficiency: the unusual case of OMP decarboxylase
Annu. Rev. Biochem.
71
847-885
2002
Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Wise, E.; Yew, W.S.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
41
3861-3869
2002
Bacillus subtilis
Manually annotated by BRENDA team
Appleby, T.C.; Kinsland, C.; Begley, T.P.; Ealick, S.E.
The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase
Proc. Natl. Acad. Sci. USA
97
2005-2010
2000
Bacillus subtilis (P25971), Bacillus subtilis
Manually annotated by BRENDA team
Phillips, L.M.; Lee, J.K.
Theoretical studies of the effect of thio substitution on orotidine monophosphate decarboxylase substrates
J. Org. Chem.
70
1211-1221
2005
Bacillus subtilis (P25971)
Manually annotated by BRENDA team
Meza-Avina, M.E.; Wei, L.; Buhendwa, M.G.; Poduch, E.; Bello, A.M.; Pai, E.F.; Kotra, L.P.
Inhibition of orotidine 5-monophosphate decarboxylase and its therapeutic potential
Mini Rev. Med. Chem.
8
239-247
2008
Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Plasmodium falciparum, Plasmodium vivax, Methanococcus thermoautotrophicum
Manually annotated by BRENDA team