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Literature summary extracted from

  • Huang, C.Y.
    Inhibition of a putative dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by flavonoids and substrates of cyclic amidohydrolases (2015), PLoS ONE, 10, e0127634 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.2.2 recombinant expression of wild-type and mutant His-tagged enzymes Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
3.5.2.2 D316A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
3.5.2.2 H183A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
3.5.2.2 H239A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
3.5.2.2 H59A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
3.5.2.2 H61A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
3.5.2.2 K150A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
3.5.2.2 N337A site-directed mutagenesis, the mutant enzyme is active, but its activity is about 20fold less than that of the wild-type dihydropyrimidinase Pseudomonas aeruginosa
3.5.2.2 S289A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa
3.5.2.2 Y155A site-directed mutagenesis, inactive mutant Pseudomonas aeruginosa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.2.2 3-Amino-1,2,4-triazole
-
 Pseudomonas aeruginosa
3.5.2.2 5-hydantoin acetic acid
-
 Pseudomonas aeruginosa
3.5.2.2 Acetohydroxamate
-
 Pseudomonas aeruginosa
3.5.2.2 allantoin slight inhibition Pseudomonas aeruginosa
3.5.2.2 dihydromyricetin competitive inhibitor, dihydromyricetin is docked in the active site pocket of dihydropyrimidinase, binding kinetics. Dihydromyricetin forms a stable complex with dihydropyrimidinase with the Kd value of 0.0226 mM Pseudomonas aeruginosa
3.5.2.2 dihydroorotate slight inhibition Pseudomonas aeruginosa
3.5.2.2 galangin
-
 Pseudomonas aeruginosa
3.5.2.2 kaempferol
-
 Pseudomonas aeruginosa
3.5.2.2 additional information myricetin and dihydromyricetin are computationally docked into the three-dimensional model of dihydropyrimidinase by using PatchDock. The dihydrouracil-complexed structure model of Pseudomonas aeruginosa dihydropyrimidinase is directly constructed by superimposing the crystal structure of the dihydrouracil-yeast dihydropyrimidinase complex (PDB ID 2FVK). Structure-inhibition relationship with dihydropyrimidinase, overview Pseudomonas aeruginosa
3.5.2.2 myricetin
-
 Pseudomonas aeruginosa
3.5.2.2 Myricitrin
-
 Pseudomonas aeruginosa
3.5.2.2 Orotic acid
-
 Pseudomonas aeruginosa
3.5.2.2 quercetin
-
 Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.2 additional information
-
 additional information Michaelis-Menten kinetics Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.2 Co2+ activates at 1 mM Pseudomonas aeruginosa
3.5.2.2 Mn2+ activates at 1 mM Pseudomonas aeruginosa
3.5.2.2 additional information no effects on enzyme activity by Cd2+, Ni2+, Mg2+, and Ca2+ at 1 mM Pseudomonas aeruginosa
3.5.2.2 Zn2+ activates at 1 mM Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa
-
 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa ATCC 15692
-
 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa 1C
-
 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa PRS 101
-
 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa DSM 22644
-
 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa CIP 104116
-
 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa LMG 12228
-
 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O Pseudomonas aeruginosa JCM 14847
-
 3-ureidopropanoate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.2 Pseudomonas aeruginosa Q9I676
-
-
3.5.2.2 Pseudomonas aeruginosa 1C Q9I676
-
-
3.5.2.2 Pseudomonas aeruginosa ATCC 15692 Q9I676
-
-
3.5.2.2 Pseudomonas aeruginosa CIP 104116 Q9I676
-
-
3.5.2.2 Pseudomonas aeruginosa DSM 22644 Q9I676
-
-
3.5.2.2 Pseudomonas aeruginosa JCM 14847 Q9I676
-
-
3.5.2.2 Pseudomonas aeruginosa LMG 12228 Q9I676
-
-
3.5.2.2 Pseudomonas aeruginosa PRS 101 Q9I676
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.2.2 recombinant wild-type and mutant His-tagged enzymes by nickel affinity chromatography and dialysis to over 97% purity Pseudomonas aeruginosa

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.2.2 0.74
-
 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Cd2+ Pseudomonas aeruginosa
3.5.2.2 0.82
-
 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in absence of metal ion Pseudomonas aeruginosa
3.5.2.2 0.82
-
 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Ca2+ Pseudomonas aeruginosa
3.5.2.2 0.82
-
 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Mg2+ Pseudomonas aeruginosa
3.5.2.2 0.91
-
 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Ni2+ Pseudomonas aeruginosa
3.5.2.2 1.72
-
 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Mn2+ Pseudomonas aeruginosa
3.5.2.2 2.9
-
 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Zn2+ Pseudomonas aeruginosa
3.5.2.2 5.8 5.9 substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Co2+ Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa ATCC 15692 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa 1C 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa PRS 101 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa DSM 22644 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa CIP 104116 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa LMG 12228 3-ureidopropanoate
-
 r
3.5.2.2 5,6-dihydrouracil + H2O
-
 Pseudomonas aeruginosa JCM 14847 3-ureidopropanoate
-
 r
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa N-carbamoyl-D-valine
-
 ?
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa ATCC 15692 N-carbamoyl-D-valine
-
 ?
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa 1C N-carbamoyl-D-valine
-
 ?
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa PRS 101 N-carbamoyl-D-valine
-
 ?
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa DSM 22644 N-carbamoyl-D-valine
-
 ?
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa CIP 104116 N-carbamoyl-D-valine
-
 ?
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa LMG 12228 N-carbamoyl-D-valine
-
 ?
3.5.2.2 5-propylhydantoin + H2O low activity Pseudomonas aeruginosa JCM 14847 N-carbamoyl-D-valine
-
 ?
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa ?
-
-
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa ATCC 15692 ?
-
-
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa 1C ?
-
-
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa PRS 101 ?
-
-
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa DSM 22644 ?
-
-
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa CIP 104116 ?
-
-
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa LMG 12228 ?
-
-
3.5.2.2 additional information the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates Pseudomonas aeruginosa JCM 14847 ?
-
-
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa ?
-
 ?
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa ATCC 15692 ?
-
 ?
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa 1C ?
-
 ?
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa PRS 101 ?
-
 ?
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa DSM 22644 ?
-
 ?
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa CIP 104116 ?
-
 ?
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa LMG 12228 ?
-
 ?
3.5.2.2 phthalimide + H2O
-
 Pseudomonas aeruginosa JCM 14847 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.2.2 More enzyme structure homology modeling Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
3.5.2.2 dht
-
 Pseudomonas aeruginosa
3.5.2.2 PA0441
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.2.2 25
-
 assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.2.2 8
-
 assay at Pseudomonas aeruginosa

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.5.2.2 0.04
-
 versus substrate 5-propylhydantoin, pH 8.0, 25°C Pseudomonas aeruginosa dihydromyricetin
3.5.2.2 0.048
-
 versus substrate dihydrouracil, pH 8.0, 25°C Pseudomonas aeruginosa dihydromyricetin

General Information

EC Number General Information Comment Organism
3.5.2.2 evolution dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis Pseudomonas aeruginosa
3.5.2.2 additional information enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview Pseudomonas aeruginosa