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Literature summary for 4.1.1.23 extracted from

  • Tokuoka, K.; Kusakari, Y.; Krungkrai, S.R.; Matsumura, H.; Krungkrai, J.; Horii, T.; Inoue, T.
    Structural basis for the decarboxylation of orotidine 5-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase (2008), J. Biochem., 143, 69-78.
    View publication on PubMed

Application

Application Comment Organism
medicine orotidine 5-monophosphate decarboxylase of Plasmodium falciparum could be a target for the development of antimalarial drugs Plasmodium falciparum

Cloned(Commentary)

Cloned (Comment) Organism
functional enzyme expression in Escherichia coli Plasmodium falciparum
into the vector pTrcHis-TOPO for expression in Escherichia coli TOP10 cells Plasmodium falciparum

Crystallization (Commentary)

Crystallization (Comment) Organism
apo, substrate or product-complex forms of OMPDC, X-ray diffraction structure determination and anaylsis at 2.65-2.7 A Plasmodium falciparum
the crystal structures of the apo form of OMPDC, and in complex with OMP and UMP are resolved at resolutions of 2.7, 2.65 and 2.65 A, respectively Plasmodium falciparum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
monomer, determined by SDS-PAGE Plasmodium falciparum
76000
-
active recombinant enzyme, gel filtration Plasmodium falciparum
76000
-
homodimer 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
functional recombinant enzyme 300fold from Escherichia coli by nickel affinity chromatography and gel filtration Plasmodium falciparum
using a Ni2+-nitrilotriacetic acid-agarose affinity and a Superdex-75 column Plasmodium falciparum

Reaction

Reaction Comment Organism Reaction ID
orotidine 5'-phosphate = UMP + CO2 decarboxylation mechanism, substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site Plasmodium falciparum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
10
-
-
Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Orotidine 5'-phosphate
-
Plasmodium falciparum UMP + CO2
-
?
Orotidine 5'-phosphate change in active-site structure upon binding of orotidine 5'-phosphate/UMP, the backbone amide of Arg294 interacts directly with the phosphate group of the ligands, rearrangement of hydrogen-bond network around Lys102, overview Plasmodium falciparum UMP + CO2
-
?

Subunits

Subunits Comment Organism
dimer 2 * 38000, active recombinant enzyme, SDS-PAGE Plasmodium falciparum
homodimer
-
Plasmodium falciparum
More structure-activity analysis, overview Plasmodium falciparum

Synonyms

Synonyms Comment Organism
OMP decarboxylase
-
Plasmodium falciparum
OMPDC
-
Plasmodium falciparum
orotidine 5-monophosphate decarboxylase
-
Plasmodium falciparum
PfOMPDC
-
Plasmodium falciparum