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Literature summary extracted from

  • Maurer, D.; Lohkamp, B.; Krumpel, M.; Widersten, M.; Dobritzsch, D.
    Crystal structure and pH-dependent allosteric regulation of human beta-ureidopropionase, an enzyme involved in anticancer drug metabolism (2018), Biochem. J., 475, 2395-2416 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.6 N-Carbamoyl-beta-alanine causes association to more active higher molecular mass species Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.6 expression in Escherichia coli Rosetta (DE3)pLysS cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.6 T299C is crystallized by the hanging-drop vapor diffusion method at 20°C. The T299C mutant enzyme crystallizes in space group C2221 with one polypeptide chain per asymmetric unit. The structure is determined to 2.08 A by molecular replacement Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.6 C233A inactive mutant enzyme Homo sapiens
3.5.1.6 E137K inactive mutant enzyme Homo sapiens
3.5.1.6 K132L inactive mutant enzyme, the mutant enzyme is exclusively dimeric Homo sapiens
3.5.1.6 L13S inactive mutant enzyme, the mutation is identified in beta-ureidopropionase-deficient patients Homo sapiens
3.5.1.6 additional information disruption of dimer-dimer interfaces by site-directed mutagenesis generated dimeric, inactive enzyme variants Homo sapiens
3.5.1.6 R130D inactive mutant enzyme Homo sapiens
3.5.1.6 R130D/S208R inactive mutant enzyme, the mutant enzyme is exclusively dimeric Homo sapiens
3.5.1.6 R130I inactive mutant enzyme, a significant monomer proportion is detected Homo sapiens
3.5.1.6 S208A inactive mutant enzyme, a significant monomer proportion is detected Homo sapiens
3.5.1.6 S208C inactive mutant enzyme, exclusively exists as dimer Homo sapiens
3.5.1.6 S208R inactive mutant enzyme, the mutant enzyme is exclusively dimeric Homo sapiens
3.5.1.6 T299C inactive mutant enzyme, exclusively exists as dimer Homo sapiens
3.5.1.6 T359M inactive mutant enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.6 4-ureidobutyrate
-
 Homo sapiens
3.5.1.6 5-aminolevulinic acid
-
 Homo sapiens
3.5.1.6 beta-Alanine causes dissociation to inactive dimers, competitive inhibition Homo sapiens
3.5.1.6 beta-aminoisobutyrate
-
 Homo sapiens
3.5.1.6 gamma-aminobutyrate
-
 Homo sapiens
3.5.1.6 iodoacetamide 30 min preincubation with 50 mM iodoacetamide renders the enzyme completely inactive, probably due to covalent modification of the active-site cysteine (C233) Homo sapiens
3.5.1.6 additional information preincubation of the enzyme with 1 mM EDTA has no influence on activity Homo sapiens
3.5.1.6 Zn2+ 5.5% residual activity is measured after preincubation with 50 mM ZnCl2 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.6 0.019
-
 3-ureidopropanoate pH 7.4, 37°C Homo sapiens
3.5.1.6 0.048
-
 3-ureidopropanoate pH 6.5, 37°C Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.6 3-ureidopropanoate + H2O Homo sapiens
-
 beta-alanine + CO2 + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.6 Homo sapiens Q9UBR1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.6
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.6 3-ureidopropanoate + H2O
-
 Homo sapiens beta-alanine + CO2 + NH3
-
 ?
3.5.1.6 3-ureidopropanoate + H2O 3-ureidopropanoate i.e. N-carbamoyl-beta-alanine Homo sapiens beta-alanine + CO2 + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.6 homodimer homodimer at pH 9, the enzyme increasingly associates to form octamers and larger oligomers with decreasing pH. Native PAGE analysis of wild-type enzyme indicates coexistence in at least five different oligomeric states, of which the smallest is most probably the dimer Homo sapiens
3.5.1.6 oligomer homodimer at pH 9, the enzyme increasingly associates to form octamers and larger oligomers with decreasing pH. Native PAGE analysis of wild-type enzyme indicates coexistence in at least five different oligomeric states, of which the smallest is most probably the dimer Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.5.1.6 betaUP
-
 Homo sapiens
3.5.1.6 UPB1
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.6 0.31
-
 3-ureidopropanoate pH 7.4, 37°C Homo sapiens
3.5.1.6 0.47
-
 3-ureidopropanoate pH 6.5, 37°C Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.1.6 0.0135
-
 beta-Alanine pH 6.5, 37°C Homo sapiens
3.5.1.6 0.047
-
 5-aminolevulinic acid pH 6.5, 37°C Homo sapiens

General Information

EC Number General Information Comment Organism
3.5.1.6 metabolism the enzyme catalyzes the third step of the reductive pyrimidine catabolic pathway responsible for breakdown of uracil-, thymine- and pyrimidine-based antimetabolites such as 5-fluorouracil Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.6 9.8
-
 3-ureidopropanoate pH 6.5, 37°C Homo sapiens
3.5.1.6 15.4
-
 3-ureidopropanoate pH 7.4, 37°C Homo sapiens