4.1.1.23: orotidine-5'-phosphate decarboxylase
This is an abbreviated version!
For detailed information about orotidine-5'-phosphate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.23
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4.1.1.23
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pyrimidine
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phosphoribosyltransferase
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uracil
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auxotrophic
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dihydroorotase
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5-fluoroorotic
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2.4.2.10
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phosphoribosyl
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6-azauridine
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pyrazofurin
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transcarbamoylase
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carbanions
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oprtase
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aciduria
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5-fluorouridine
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dianion
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prototrophy
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barbituric
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succinate-grown
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phosphite
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phosphodianion
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pyre
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molecular biology
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pharmacology
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medicine
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biotechnology
- 4.1.1.23
- pyrimidine
-
phosphoribosyltransferase
- uracil
-
auxotrophic
- dihydroorotase
-
5-fluoroorotic
-
2.4.2.10
-
phosphoribosyl
- 6-azauridine
- pyrazofurin
-
transcarbamoylase
-
carbanions
- oprtase
-
aciduria
- 5-fluorouridine
- dianion
-
prototrophy
-
barbituric
-
succinate-grown
- phosphite
-
phosphodianion
-
pyre
- molecular biology
- pharmacology
- medicine
- biotechnology
Reaction
Synonyms
Decarboxylase, orotidine 5'-phosphate, More, ODCase, OMP decarboxylase, OMP-DC, OMPD, OMPDC, OMPDCase, OMPdecase, Orotate decarboxylase, Orotate monophosphate decarboxylase, Orotic decarboxylase, Orotidine 5'-monophosphate decarboxylase, Orotidine 5'-phosphate decarboxylase, orotidine 5-monophosphate decarboxylase, orotidine 5-phosphate decarboxylase, Orotidine monophosphate decarboxylase, Orotidine phosphate decarboxylase, Orotidine-5'-monophosphate decarboxylase, orotidine-5'-phosphate decarboxylase, orotidine-5-monophosphate decarboxylase, Orotidylate decarboxylase, Orotidylic acid decarboxylase, Orotidylic decarboxylase, Orotodylate decarboxylase, PbrURA3, PfODCase, PfOMPDC, pm-ura3, PyrF, ScOMPDC, UMP synthase, URA3, Uridine 5'-monophosphate synthase
ECTree
4.1.1.23 orotidine-5'-phosphate decarboxylaseAdvanced search results
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General Information on EC 4.1.1.23 - orotidine-5'-phosphate decarboxylase
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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
metabolism
additional information
metabolism
orotate phosphoribosyltransferase (OPRT) and orotidine 5'-monophosphate decarboxylase (OMPDC) from the human malaria parasite Plasmodium falciparum, the fifth and sixth enzyme of the de novo biosynthetic pathway, form a multienzyme complex. The complex physically exists as heterotetrameric (OPRT)2(OMPDC)2 complex containing two subunits each of OPRT and OMPDC, and has catalytic kinetic advantages over the monofunctional enzyme
additional information
protein-protein interaction in the (OPRT)2(OMPDC)2 enzyme complex by bifunctional chemical cross-linker, liquid chromatography-mass spectrometric analysis and homology modeling, structural models for the protein-protein interaction of the heterotetrameric (OPRT)2(OMPDC)2 multienzyme complex are proposed, allosteric control in protein-protein-interactions
additional information
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protein-protein interaction in the (OPRT)2(OMPDC)2 enzyme complex by bifunctional chemical cross-linker, liquid chromatography-mass spectrometric analysis and homology modeling, structural models for the protein-protein interaction of the heterotetrameric (OPRT)2(OMPDC)2 multienzyme complex are proposed, allosteric control in protein-protein-interactions
additional information
substrate specificity and kinetic analysis, structure-function analysis, detailed overview
additional information
the phosphodianion gripper loop [Pro202-Val220] is important for catalysis
additional information
the role of flexible loops in enzyme catalysis, important interactions of Gln215, Tyr217, and Arg235 side chains from the phosphodianion gripper loop with the ligand phosphodianion, structure-function analysis, overview. Mechanism by which ionic and hydrogen-bonding interactions of side chains from the gripper loop, and Arg235, with the phosphodianion of OMP, or with HPi, are utilized in stabilization of the transition state for OMPDC-catalyzed decarboxylation of OMP, deprotonation of UMP, and the corresponding reactions of the phosphodianion truncated substrates 1-(beta-D-erythrofuranosyl)orotic acid and FEU, respectively, at a site 10 A distant from the gripper loop
additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
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the phosphodianion gripper loop [Pro202-Val220] is important for catalysis
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additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
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the role of flexible loops in enzyme catalysis, important interactions of Gln215, Tyr217, and Arg235 side chains from the phosphodianion gripper loop with the ligand phosphodianion, structure-function analysis, overview. Mechanism by which ionic and hydrogen-bonding interactions of side chains from the gripper loop, and Arg235, with the phosphodianion of OMP, or with HPi, are utilized in stabilization of the transition state for OMPDC-catalyzed decarboxylation of OMP, deprotonation of UMP, and the corresponding reactions of the phosphodianion truncated substrates 1-(beta-D-erythrofuranosyl)orotic acid and FEU, respectively, at a site 10 A distant from the gripper loop
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additional information
Saccharomyces cerevisiae ATCC 204508 / S288c
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substrate specificity and kinetic analysis, structure-function analysis, detailed overview
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