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Literature summary for 4.1.1.23 extracted from

  • 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 (2014), Asian Pac. J. Trop. Med., 7, 184-192 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene OMPDC, recombinant expression of His-tagged enzyme in Escherichia coli Plasmodium falciparum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
76000
-
recombinant His-tagged enzyme, gel filtration Plasmodium falciparum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Orotidine 5'-phosphate Plasmodium falciparum
-
UMP + CO2
-
?

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum A0A1D3TG46
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate
-
Plasmodium falciparum UMP + CO2
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 33000, recombinant His-tagged enzyme, SDS-PAGE Plasmodium falciparum
More structure analysis, homology modeling Plasmodium falciparum

Synonyms

Synonyms Comment Organism
OMPDC
-
Plasmodium falciparum
Orotidine 5'-monophosphate decarboxylase
-
Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
38
-
assay at Plasmodium falciparum

General Information

General Information Comment Organism
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 Plasmodium falciparum
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 Plasmodium falciparum