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Literature summary for 4.1.1.23 extracted from

  • Amyes, T.L.; Ming, S.A.; Goldman, L.M.; Wood, B.M.; Desai, B.J.; Gerlt, J.A.; Richard, J.P.
    Orotidine 5-monophosphate decarboxylase: transition state stabilization from remote protein-phosphodianion interactions (2012), Biochemistry, 51, 4630-4632.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
Q215A 2.5% of wild-type activity Saccharomyces cerevisiae
Q215A/R235A less than 0.1% of wild-type activity Saccharomyces cerevisiae
Q215A/Y217F less than 0.1% of wild-type activity Saccharomyces cerevisiae
Q215A/Y217F/R235A effect of the triple mutation on the catalytic activity toward OMP can be ascribed almost entirely to the loss of stabilizing interactions of the three excised side chains with the transition state for decarboxylation Saccharomyces cerevisiae
R235A less than 0.1% of wild-type activity Saccharomyces cerevisiae
Y217F 1.6% of wild-type activity Saccharomyces cerevisiae
Y217F/R235A less than 0.1% of wild-type activity Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-(beta-D-erythrofuranosyl)orotic acid truncated substrate Saccharomyces cerevisiae 1-(beta-D-erythrofuranosyl)uracil + CO2
-
?
additional information in reaction model phosphodianion binding interactions are utilized to stabilize a rare closed enzyme form that exhibits a high catalytic activity for decarboxylation. The thermodynamic barrier to formation of the productive catalytic complex from the inactive enzyme arises largely from the desolvation of the active site accompanying the conformational change and sequestration of the substrate from bulk solvent. The energetically unfavorable conformational change and desolvation of the active site are paid for by the binding energy available from the formation of strong phosphodianion-protein interactions in the desolvated environment present at the EC·S complex. The phosphodianion binding energy is recovered as transition state stabilization via the enhanced electrostatic and hydrogen bonding interactions at the transition state in the desolvated active site Saccharomyces cerevisiae ?
-
?
Orotidine 5'-phosphate
-
Saccharomyces cerevisiae UMP + CO2
-
?

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00004
-
orotidine 5'-phosphate mutant Q215A/Y217F/R235A, pH 7.1, 25°C Saccharomyces cerevisiae
0.0041
-
orotidine 5'-phosphate mutant Y217F/R235A, pH 7.1, 25°C Saccharomyces cerevisiae
0.013
-
orotidine 5'-phosphate mutant Q215A/R235A, pH 7.1, 25°C Saccharomyces cerevisiae
0.61
-
orotidine 5'-phosphate mutant R235A, pH 7.1, 25°C Saccharomyces cerevisiae
2.3
-
orotidine 5'-phosphate mutant Q215A/Y217F, pH 7.1, 25°C Saccharomyces cerevisiae
3
-
1-(beta-D-erythrofuranosyl)orotic acid mutant Q215A/Y217F/R235A, pH 7.1, 25°C Saccharomyces cerevisiae
4.2
-
1-(beta-D-erythrofuranosyl)orotic acid mutant Q215A/R235A, pH 7.1, 25°C Saccharomyces cerevisiae
4.6
-
1-(beta-D-erythrofuranosyl)orotic acid mutant Q215A/Y217F, pH 7.1, 25°C Saccharomyces cerevisiae
10
-
1-(beta-D-erythrofuranosyl)orotic acid mutant Y217F/R235A, pH 7.1, 25°C Saccharomyces cerevisiae
11
-
1-(beta-D-erythrofuranosyl)orotic acid mutant Q215A, pH 7.1, 25°C Saccharomyces cerevisiae
12
-
1-(beta-D-erythrofuranosyl)orotic acid mutant Y217F, pH 7.1, 25°C Saccharomyces cerevisiae
26
-
1-(beta-D-erythrofuranosyl)orotic acid wild-type, pH 7.1, 25°C Saccharomyces cerevisiae
26
-
1-(beta-D-erythrofuranosyl)orotic acid mutant R235A, pH 7.1, 25°C Saccharomyces cerevisiae
180
-
orotidine 5'-phosphate mutant Y217F, pH 7.1, 25°C Saccharomyces cerevisiae
260
-
orotidine 5'-phosphate mutant Q215A, pH 7.1, 25°C Saccharomyces cerevisiae
11000
-
orotidine 5'-phosphate wild-type, pH 7.1, 25°C Saccharomyces cerevisiae