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Literature summary extracted from

  • Soriano-Maldonado, P.; Las Heras-Vazquez, F.J.; Clemente-Jimenez, J.M.; Rodriguez-Vico, F.; Martinez-Rodriguez, S.
    Enzymatic dynamic kinetic resolution of racemic N-formyl- and N-carbamoyl-amino acids using immobilized L-N-carbamoylase and N-succinyl-amino acid racemase (2015), Appl. Microbiol. Biotechnol., 99, 283-291.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.87 additional information enzyme immobilization on solid matrix results in a great enhancement of the enzyme activity toward N-formyl-tryptophan, the reaction can be repeated for several cycles, method optimization, overview Geobacillus stearothermophilus
3.5.1.87 synthesis production of different optically pure L-alpha-amino acids starting from different racemic N-formyl- and N-carbamoyl-amino acids using a dynamic kinetic resolution approach with immobilized L-N-carbamoylase and N-succinyl-amino acid racemase as biocatalysts, the system is effective for the biosynthesis of natural and unnatural L-amino acids (enantiomeric excess over 99.5%), overview Geobacillus stearothermophilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.87 gene Bslcar, recombinant expression Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.87 additional information enzyme immobilization on solid matrix results in a great enhancement of the enzyme activity toward N-formyl-tryptophan, the reaction can be repeated for several cycles, method optimization, overview Geobacillus stearothermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.87 Co2+ required Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.87 Geobacillus stearothermophilus Q53389 gene Bslcar
-
3.5.1.87 Geobacillus stearothermophilus CECT43 Q53389 gene Bslcar
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.87 recombinant enzyme by cobalt affinity chromatography, ultrafiltration and dialysis Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.87 additional information catalytic promiscuity of L-N-carbamoylase from Geobacillus stearothermophilus CECT43, substrate specificity with different N-formyl- and N-carbamoyl-DL-amino acids, overview. No N-formyl-DL-tert-leucine Geobacillus stearothermophilus ?
-
 ?
3.5.1.87 additional information catalytic promiscuity of L-N-carbamoylase from Geobacillus stearothermophilus CECT43, substrate specificity with different N-formyl- and N-carbamoyl-DL-amino acids, overview. No N-formyl-DL-tert-leucine Geobacillus stearothermophilus CECT43 ?
-
 ?
3.5.1.87 N-carbamoyl-DL-aminobutyric acid + H2O
-
 Geobacillus stearothermophilus L-aminobutyric acid + CO2 + NH3
-
 ?
3.5.1.87 N-carbamoyl-DL-homophenylalanine + H2O
-
 Geobacillus stearothermophilus L-homophenylalanine + CO2 + NH3
-
 ?
3.5.1.87 N-carbamoyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus L-methionine + CO2 + NH3
-
 ?
3.5.1.87 N-carbamoyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus CECT43 L-methionine + CO2 + NH3
-
 ?
3.5.1.87 N-carbamoyl-DL-norleucine + H2O
-
 Geobacillus stearothermophilus L-norleucine + CO2 + NH3
-
 ?
3.5.1.87 N-carbamoyl-DL-norvaline + H2O
-
 Geobacillus stearothermophilus L-norvaline + CO2 + NH3
-
 ?
3.5.1.87 N-formyl-DL-alanine + H2O
-
 Geobacillus stearothermophilus L-alanine + CO2
-
 ?
3.5.1.87 N-formyl-DL-alanine + H2O
-
 Geobacillus stearothermophilus CECT43 L-alanine + CO2
-
 ?
3.5.1.87 N-formyl-DL-aminobutyric acid + H2O
-
 Geobacillus stearothermophilus L-aminobutyric acid + CO2
-
 ?
3.5.1.87 N-formyl-DL-ethionine + H2O
-
 Geobacillus stearothermophilus L-ethionine + CO2
-
 ?
3.5.1.87 N-formyl-DL-homophenylalanine + H2O
-
 Geobacillus stearothermophilus L-homophenylalanine + CO2
-
 ?
3.5.1.87 N-formyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus L-methionine + CO2
-
 ?
3.5.1.87 N-formyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus CECT43 L-methionine + CO2
-
 ?
3.5.1.87 N-formyl-DL-norleucine + H2O
-
 Geobacillus stearothermophilus L-norleucine + CO2
-
 ?
3.5.1.87 N-formyl-DL-norvaline + H2O
-
 Geobacillus stearothermophilus L-norvaline + CO2
-
 ?
3.5.1.87 N-formyl-DL-phenylalanine + H2O
-
 Geobacillus stearothermophilus L-phenylalanine + CO2
-
 ?
3.5.1.87 N-formyl-DL-phenylglycine + H2O
-
 Geobacillus stearothermophilus L-phenylglycine + CO2
-
 ?
3.5.1.87 N-formyl-DL-tryptophan + H2O
-
 Geobacillus stearothermophilus L-tryptophan + CO2
-
 ?
3.5.1.87 N-formyl-DL-tryptophan + H2O
-
 Geobacillus stearothermophilus CECT43 L-tryptophan + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.87 BsLcar
-
 Geobacillus stearothermophilus
3.5.1.87 L-N-carbamoylase
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.87 45
-
 assay at Geobacillus stearothermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.87 40 70 activity range Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.87 30 70 immobilized enzyme, in 100 mM borate-HCl, pH 8.0, 18 h, conversion rates decrease at temperatures over 55°C and are lost completely at over 70°C, for the immobilized enzyme system in production of optically pure L-amino acids, overview Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.87 8
-
 assay at Geobacillus stearothermophilus