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Literature summary for 4.1.1.23 extracted from

  • Reyes, A.C.; Amyes, T.L.; Richard, J.P.
    Enzyme architecture Erection of active orotidine 5'-monophosphate decarboxylase by substrate-induced conformational changes (2017), J. Am. Chem. Soc., 139, 16048-16051 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
D-erythritol 4-phosphate activates the decarboxylation of 5-fluoroorotate. This activation is due to the utilization of binding energy from interactions between OMPDC and activator Saccharomyces cerevisiae
D-glycerol 3-phosphate activates the decarboxylation of 5-fluoroorotate. Saccharomyces cerevisiae
phosphite dianion the activation with substrate 1-(beta-D-erythrofuranosyl)-orotate is due to the utilization of binding energy from interactions between OMPDC and activator to drive a complex conformational change from inactive open OMPDC (EO) to the active closed caged complex (EC), where EC is stabilized relative to EO by interactions between dianions and the side chains of Q215, Y217, and R235 Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information substrate specificity and kinetic analysis, overview Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Orotidine 5'-phosphate Saccharomyces cerevisiae
-
UMP + CO2
-
?
Orotidine 5'-phosphate Saccharomyces cerevisiae ATCC 204508 / S288c
-
UMP + CO2
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P03962
-
-
Saccharomyces cerevisiae ATCC 204508 / S288c P03962
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(beta-D-erythrofuranosyl)-5-fluoroorotate
-
Saccharomyces cerevisiae 1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2
-
?
1-(beta-D-erythrofuranosyl)-5-fluoroorotate
-
Saccharomyces cerevisiae ATCC 204508 / S288c 1-(beta-D-erythrofuranosyl)-5-fluorouracil + CO2
-
?
1-(beta-D-erythrofuranosyl)-orotate
-
Saccharomyces cerevisiae 1-(beta-D-erythrofuranosyl)uracil + CO2
-
?
1-(beta-D-erythrofuranosyl)-orotate
-
Saccharomyces cerevisiae ATCC 204508 / S288c 1-(beta-D-erythrofuranosyl)uracil + CO2
-
?
5-fluoroorotate
-
Saccharomyces cerevisiae 5-fluorouracil + CO2
-
?
additional information extraordinary specificity of OMPDC in binding the decarboxylation transition state with a higher affinity compared with the substrate orotidine 5'-phosphate. Substrate specificity and kinetic analysis, structure-function analysis, detailed overview Saccharomyces cerevisiae ?
-
?
additional information extraordinary specificity of OMPDC in binding the decarboxylation transition state with a higher affinity compared with the substrate orotidine 5'-phosphate. Substrate specificity and kinetic analysis, structure-function analysis, detailed overview Saccharomyces cerevisiae ATCC 204508 / S288c ?
-
?
orotate
-
Saccharomyces cerevisiae uracil + CO2
-
?
Orotidine 5'-phosphate
-
Saccharomyces cerevisiae UMP + CO2
-
?
Orotidine 5'-phosphate stepwise mechanism via a UMP carbanion intermediate, modeling of the transition state stabilization Saccharomyces cerevisiae UMP + CO2
-
?
Orotidine 5'-phosphate
-
Saccharomyces cerevisiae ATCC 204508 / S288c UMP + CO2
-
?
Orotidine 5'-phosphate stepwise mechanism via a UMP carbanion intermediate, modeling of the transition state stabilization Saccharomyces cerevisiae ATCC 204508 / S288c UMP + CO2
-
?

Synonyms

Synonyms Comment Organism
OMPDC
-
Saccharomyces cerevisiae
Orotidine 5'-monophosphate decarboxylase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information substrate specificity and kinetic analysis, structure-function analysis, detailed overview Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0000003
-
Orotate pH 7.0, 25°C, wild-type enzyme Saccharomyces cerevisiae
0.00002
-
1-(beta-D-erythrofuranosyl)-orotate pH 7.0, 25°C, wild-type enzyme Saccharomyces cerevisiae
0.0001
-
orotidine 5'-phosphate pH 7.0, 25°C, wild-type enzyme Saccharomyces cerevisiae
0.00014
-
5-Fluoroorotate pH 7.0, 25°C, wild-type enzyme Saccharomyces cerevisiae