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Literature summary extracted from

  • Traut, T.W.
    beta-Alanine synthase, an enzyme involved in catabolism of uracil and thymine (2000), Methods Enzymol., 324, 399-410.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.5.1.6 the hexamer is a stable enzyme species, detergents, e.g. 3% v/v CHAPSO or CHAPS, and reducing thiols stabilize purified enzyme in solution, 1 mM dithiothreitol stabilizes Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.6 2-methyl-beta-alanine product inhibition, the presence of product leads to dissociation of hexamers to inactive trimers Rattus norvegicus
3.5.1.6 beta-Alanine product inhibition, the presence of product leads to dissociation of hexamers to inactive trimers Rattus norvegicus
3.5.1.6 gamma-aminobutyrate
-
 Rattus norvegicus
3.5.1.6 additional information removal of the enzyme-bound zinc by chelators leads to loss of activity Rattus norvegicus
3.5.1.6 propionate
-
 Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.6 0.006
-
 2-methyl-N-carbamoyl-beta-alanine
-
 Rattus norvegicus
3.5.1.6 0.008
-
 N-Carbamoyl-beta-alanine
-
 Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.6 Zn2+ contains two tightly bound Zn2+, removal leads to loss of activity Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.6 42000
-
 12 * 42000, active dodecamer in the presence of substrate, SDS-PAGE Rattus norvegicus
3.5.1.6 42000
-
 3 * 42000, inactive trimer in the presence of the product, SDS-PAGE Rattus norvegicus
3.5.1.6 42000
-
 6 * 42000, the native enzyme is a hexamer, which readily associates to an active dodecamer in the presence of substrate and dissociates to an inactive trimer in the presence of the product, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.6 2-methyl-N-carbamoyl-beta-alanine + H2O Rattus norvegicus completes the catabolism of the pyrimidine bases uracil and thymine 2-methyl-beta-alanine + CO2 + NH3
-
 ?
3.5.1.6 N-carbamoyl-beta-alanine + H2O Rattus norvegicus completes the catabolism of the pyrimidine bases uracil and thymine beta-alanine + CO2 + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.6 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.6 1096fold Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.6 liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.6 0.88
-
 N-carbamoyl-beta-alanine as substrate Rattus norvegicus

Storage Stability

EC Number Storage Stability Organism
3.5.1.6 4°C, buffer without stabilizing detergents and reducing thiols, 26 days, almost complete loss of activity Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.6 2-methyl-N-carbamoyl-beta-alanine + H2O
-
 Rattus norvegicus 2-methyl-beta-alanine + CO2 + NH3
-
 ?
3.5.1.6 2-methyl-N-carbamoyl-beta-alanine + H2O completes the catabolism of the pyrimidine bases uracil and thymine Rattus norvegicus 2-methyl-beta-alanine + CO2 + NH3
-
 ?
3.5.1.6 additional information enzyme shows cooperativity for the substrate and allosteric regulation Rattus norvegicus ?
-
 ?
3.5.1.6 N-carbamoyl-beta-alanine + H2O
-
 Rattus norvegicus beta-alanine + CO2 + NH3
-
 ?
3.5.1.6 N-carbamoyl-beta-alanine + H2O completes the catabolism of the pyrimidine bases uracil and thymine Rattus norvegicus beta-alanine + CO2 + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.6 dodecamer 12 * 42000, active dodecamer in the presence of substrate, SDS-PAGE Rattus norvegicus
3.5.1.6 hexamer 6 * 42000, the native enzyme is a hexamer, which readily associates to an active dodecamer in the presence of substrate and dissociates to an inactive trimer in the presence of the product, SDS-PAGE Rattus norvegicus
3.5.1.6 trimer 3 * 42000, inactive trimer in the presence of the product, SDS-PAGE Rattus norvegicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.6 additional information
-
 heating destabilizes Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.6 0.6
-
 N-Carbamoyl-beta-alanine
-
 Rattus norvegicus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.1.6 0.09
-
 propionate
-
 Rattus norvegicus
3.5.1.6 1.1
-
 beta-Alanine
-
 Rattus norvegicus
3.5.1.6 1.6
-
 gamma-aminobutyrate
-
 Rattus norvegicus
3.5.1.6 3.9
-
 2-methyl-beta-alanine
-
 Rattus norvegicus