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Literature summary extracted from

  • Cheng, J.H.; Huang, C.C.; Huang, Y.H.; Huang, C.Y.
    Structural basis for pH-dependent oligomerization of dihydropyrimidinase from Pseudomonas aeruginosa PAO1 (2018), Bioinorg. Chem. Appl., 2018, 9564391 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.2.2 recombinant expression of His-tagged enzyme Pseudomonas aeruginosa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.2.2 purified enzyme, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM MES, and 100 mM NaCl, pH 5.9, with reservoir solution containing 10% PEG 8000, 100 mM HEPES, 200 mM calcium acetate, pH 5.9, at room temperature, X-ray diffraction structure determination and analysis at 2.17 A resolution. An asymmetric unit of the crystal contains four crystallographically independent dihydropyrimidinase monomers. The crystals of the dimeric Pseudomonas aeruginosa dihydropyrimidinase belong to space group P3121 grown at the condition of 28% PEG 6000, 100 mM HEPES, 200 mM lithium acetate, pH 7.5 Pseudomonas aeruginosa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.2 Zn2+ a dimetalloenzyme 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 His-tagged enzyme by nickel affinity chromatography and dialysis to over 97% purity 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

Subunits

EC Number Subunits Comment Organism
3.5.2.2 dimer or tetramer pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers Pseudomonas aeruginosa
3.5.2.2 More Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
3.5.2.2 dht
-
 Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
3.5.2.2 evolution enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase Pseudomonas aeruginosa
3.5.2.2 metabolism dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway Pseudomonas aeruginosa
3.5.2.2 additional information the enzyme contains a carboxylated lysine within the active site Pseudomonas aeruginosa
3.5.2.2 physiological function dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids Pseudomonas aeruginosa