Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fernald, N.J.; Ramaley, R.F.
    Purification and properties of dicarboxylate omega-amidase from Bacillus subtilis 168 and Thermus aquaticus YT-1 (1972), Arch. Biochem. Biophys., 153, 95-104.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.3 additional information no activation by ATP or Coenzyme A Thermus aquaticus
3.5.1.3 additional information no activation by ATP or Coenzyme A Bacillus subtilis

General Stability

EC Number General Stability Organism
3.5.1.3 does not require mercaptoethanol or succinate for stability Thermus aquaticus
3.5.1.3 does not require mercaptoethanol or succinate for stability Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.3 additional information amide and acyl transfer activity: no inhibition by high concentrations of hydroxylamine; no inhibition by EDTA Bacillus subtilis
3.5.1.3 additional information amide and acyl transfer activity: no inhibition by high concentrations of hydroxylamine; no inhibition by EDTA Thermus aquaticus
3.5.1.3 NH4+ biosynthesis of omega-amidase is repressed by free ammonium ions Bacillus subtilis
3.5.1.3 NH4+ synthesis of omega-amidase is repressed by about 50% Thermus aquaticus
3.5.1.3 phosphate phosphate buffer: slightly inhibitory Bacillus subtilis
3.5.1.3 phosphate phosphate buffer: slightly inhibitory Thermus aquaticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.3 1.3
-
 succinamate
-
 Bacillus subtilis
3.5.1.3 1.34
-
 succinamate
-
 Thermus aquaticus
3.5.1.3 30
-
 succinate
-
 Thermus aquaticus
3.5.1.3 50
-
 hydroxylamine with substrate succinamate Bacillus subtilis
3.5.1.3 63
-
 succinate
-
 Bacillus subtilis
3.5.1.3 100
-
 hydroxylamine with substrate succinamate Thermus aquaticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.3 additional information no activation by Mg2+ Thermus aquaticus
3.5.1.3 additional information no activation by Mg2+ Bacillus subtilis
3.5.1.3 additional information no requirement for any metal ions for hydroxamate formation Thermus aquaticus
3.5.1.3 additional information no requirement for any metal ions for hydroxamate formation Bacillus subtilis
3.5.1.3 additional information no Mg2+ requirement for omega-amidase activity Thermus aquaticus
3.5.1.3 additional information no Mg2+ requirement for omega-amidase activity Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.3 36000 38500 gel filtration Thermus aquaticus
3.5.1.3 120000
-
 gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.3 2-oxoglutaramate + H2O Thermus aquaticus alpha-ketoglutaramate 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O Bacillus subtilis alpha-ketoglutaramate 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O Thermus aquaticus physiological function of omega-amidase might be hydrolysis or transfer of amide group of alpha-ketoglutarate 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O Bacillus subtilis physiological function of omega-amidase might be hydrolysis or transfer of amide group of alpha-ketoglutarate 2-oxoglutarate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.3 Bacillus subtilis
-
 168, wild-type
-
3.5.1.3 Bacillus subtilis 168
-
 168, wild-type
-
3.5.1.3 Thermus aquaticus
-
 YT-1
-
3.5.1.3 Thermus aquaticus
-
 gram-negative extreme thermophilic bacterium
-
3.5.1.3 Thermus aquaticus YT-1
-
 YT-1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.3
-
 Thermus aquaticus
3.5.1.3
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.1.3 10.9
-
-
 Bacillus subtilis
3.5.1.3 66
-
-
 Thermus aquaticus

Storage Stability

EC Number Storage Stability Organism
3.5.1.3 -20°C, protein concentration above 0.1 mg/ml, 0.05 M potassium phosphate, pH 7.2, 0.05 M KCl, 3 months, quite stable Bacillus subtilis
3.5.1.3 -20°C, protein concentration above 0.1 mg/ml, 3 months, quite stable Thermus aquaticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.3 2-oxoglutaramate + H2O alpha-ketoglutaramate Thermus aquaticus 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O alpha-ketoglutaramate Bacillus subtilis 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O physiological function of omega-amidase might be hydrolysis or transfer of amide group of alpha-ketoglutarate Thermus aquaticus 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O physiological function of omega-amidase might be hydrolysis or transfer of amide group of alpha-ketoglutarate Bacillus subtilis 2-oxoglutarate + NH3
-
 ?
3.5.1.3 asparagine + H2O
-
 Bacillus subtilis aspartate + NH3
-
 ?
3.5.1.3 fumarate + H2O
-
 Thermus aquaticus ?
-
 ?
3.5.1.3 fumarate + hydroxylamine acyl transfer reaction Thermus aquaticus fumaryl hydroxamate + H2O
-
 ?
3.5.1.3 L-asparagine + hydroxylamine amide transfer reaction Bacillus subtilis L-asparaginyl hydroxamate + H2O
-
 ?
3.5.1.3 malate + H2O
-
 Thermus aquaticus ?
-
 ?
3.5.1.3 malate + H2O
-
 Bacillus subtilis ?
-
 ?
3.5.1.3 malate + hydroxylamine acyl transfer reaction Thermus aquaticus malyl hydroxamate + H2O
-
 ?
3.5.1.3 malate + hydroxylamine acyl transfer reaction Bacillus subtilis malyl hydroxamate + H2O
-
 ?
3.5.1.3 additional information substrate specificity Thermus aquaticus ?
-
 ?
3.5.1.3 additional information substrate specificity Bacillus subtilis ?
-
 ?
3.5.1.3 additional information no reaction with monocarboxylic acids Thermus aquaticus ?
-
 ?
3.5.1.3 additional information no reaction with monocarboxylic acids Bacillus subtilis ?
-
 ?
3.5.1.3 additional information catalyzes several enzymatic reactions: amide transfer, acyl transfer, and amide hydrolysis, are consistent with acyl enzyme type of intermediate Thermus aquaticus ?
-
 ?
3.5.1.3 additional information catalyzes several enzymatic reactions: amide transfer, acyl transfer, and amide hydrolysis, are consistent with acyl enzyme type of intermediate Bacillus subtilis ?
-
 ?
3.5.1.3 additional information glutamine, acetamide, acetate, propionate, aspartate and glutamate not or very poor substrates Thermus aquaticus ?
-
 ?
3.5.1.3 additional information glutamine, acetamide, acetate, propionate, aspartate and glutamate not or very poor substrates Bacillus subtilis ?
-
 ?
3.5.1.3 additional information catalyzes hydrolysis of dicarboxylic acid amides and the formation of hydroxamates from amides, amide transfer, of the corresponding acids, acyl transfer Thermus aquaticus ?
-
 ?
3.5.1.3 additional information catalyzes hydrolysis of dicarboxylic acid amides and the formation of hydroxamates from amides, amide transfer, of the corresponding acids, acyl transfer Bacillus subtilis ?
-
 ?
3.5.1.3 additional information substrate specificity Bacillus subtilis 168 ?
-
 ?
3.5.1.3 additional information no reaction with monocarboxylic acids Bacillus subtilis 168 ?
-
 ?
3.5.1.3 additional information catalyzes several enzymatic reactions: amide transfer, acyl transfer, and amide hydrolysis, are consistent with acyl enzyme type of intermediate Bacillus subtilis 168 ?
-
 ?
3.5.1.3 additional information glutamine, acetamide, acetate, propionate, aspartate and glutamate not or very poor substrates Bacillus subtilis 168 ?
-
 ?
3.5.1.3 additional information catalyzes hydrolysis of dicarboxylic acid amides and the formation of hydroxamates from amides, amide transfer, of the corresponding acids, acyl transfer Bacillus subtilis 168 ?
-
 ?
3.5.1.3 additional information substrate specificity Thermus aquaticus YT-1 ?
-
 ?
3.5.1.3 additional information no reaction with monocarboxylic acids Thermus aquaticus YT-1 ?
-
 ?
3.5.1.3 additional information catalyzes several enzymatic reactions: amide transfer, acyl transfer, and amide hydrolysis, are consistent with acyl enzyme type of intermediate Thermus aquaticus YT-1 ?
-
 ?
3.5.1.3 additional information glutamine, acetamide, acetate, propionate, aspartate and glutamate not or very poor substrates Thermus aquaticus YT-1 ?
-
 ?
3.5.1.3 additional information catalyzes hydrolysis of dicarboxylic acid amides and the formation of hydroxamates from amides, amide transfer, of the corresponding acids, acyl transfer Thermus aquaticus YT-1 ?
-
 ?
3.5.1.3 succinamate + H2O amidase activity, hydrolysis proceeds at a slower rate than formation of succinyl hydroxamate in the presence of hydroxylamine Thermus aquaticus succinic acid + NH3
-
 ?
3.5.1.3 succinamate + H2O amidase activity, hydrolysis proceeds at a slower rate than formation of succinyl hydroxamate in the presence of hydroxylamine Bacillus subtilis succinic acid + NH3
-
 ?
3.5.1.3 succinamate + hydroxylamine amide transfer reaction Thermus aquaticus succinyl hydroxamate + NH3
-
 r
3.5.1.3 succinamate + hydroxylamine amide transfer reaction Bacillus subtilis succinyl hydroxamate + NH3
-
 r
3.5.1.3 succinamide + H2O
-
 Thermus aquaticus succinate + NH3
-
 ?
3.5.1.3 succinamide + H2O
-
 Bacillus subtilis succinate + NH3
-
 ?
3.5.1.3 succinamide + hydroxylamine amide transfer reaction Thermus aquaticus succinyl hydroxamate + ?
-
 r
3.5.1.3 succinamide + hydroxylamine amide transfer reaction Bacillus subtilis succinyl hydroxamate + ?
-
 r
3.5.1.3 succinate + hydroxylamine very high substrate concentration required for acyl transfer reaction Thermus aquaticus succinyl hydroxamate + H2O
-
 r
3.5.1.3 succinate + hydroxylamine very high substrate concentration required for acyl transfer reaction Bacillus subtilis succinyl hydroxamate + H2O
-
 r
3.5.1.3 succinate + hydroxylamine acyl transfer reaction Thermus aquaticus succinyl hydroxamate + H2O
-
 r
3.5.1.3 succinate + hydroxylamine acyl transfer reaction Bacillus subtilis succinyl hydroxamate + H2O
-
 r
3.5.1.3 succinimide + hydroxylamine amide transfer reaction Thermus aquaticus ?
-
 ?
3.5.1.3 succinimide + hydroxylamine amide transfer reaction Bacillus subtilis ?
-
 ?
3.5.1.3 succinyl hydroxamate + H2O
-
 Thermus aquaticus succinate + hydroxylamine
-
 r
3.5.1.3 succinyl hydroxamate + H2O
-
 Bacillus subtilis succinate + hydroxylamine
-
 r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.3 37
-
 assay at Bacillus subtilis
3.5.1.3 45 56 broad temperature optimum Bacillus subtilis
3.5.1.3 70
-
 assay at Thermus aquaticus
3.5.1.3 80
-
-
 Thermus aquaticus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.3 25 63 about 50% of maximum activity Bacillus subtilis
3.5.1.3 63 87 about 50% of maximum activity Thermus aquaticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.3 additional information
-
-
 Thermus aquaticus
3.5.1.3 additional information
-
-
 Bacillus subtilis
3.5.1.3 6.5
-
 acyl transferase activity, sharp optimum Thermus aquaticus
3.5.1.3 6.5
-
 acyl transferase activity, sharp optimum Bacillus subtilis
3.5.1.3 7 9 amide transferase activity, broad optimum Thermus aquaticus
3.5.1.3 7 9 amide transferase activity, broad optimum Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
3.5.1.3 additional information no requirement for any cofactors for hydroxamate formation Thermus aquaticus
3.5.1.3 additional information no requirement for any cofactors for hydroxamate formation Bacillus subtilis