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Literature summary for 3.5.1.87 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
Search for more literature for 3.5.1.87

Application

Application Comment Organism
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
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)

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

Protein Variants

Protein Variants Comment Organism
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

Metals/Ions Comment Organism Structure
Co2+ required Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q53389 gene Bslcar
-
Geobacillus stearothermophilus CECT43 Q53389 gene Bslcar
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
N-carbamoyl-DL-aminobutyric acid + H2O
-
 Geobacillus stearothermophilus L-aminobutyric acid + CO2 + NH3
-
 ?
N-carbamoyl-DL-homophenylalanine + H2O
-
 Geobacillus stearothermophilus L-homophenylalanine + CO2 + NH3
-
 ?
N-carbamoyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus L-methionine + CO2 + NH3
-
 ?
N-carbamoyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus CECT43 L-methionine + CO2 + NH3
-
 ?
N-carbamoyl-DL-norleucine + H2O
-
 Geobacillus stearothermophilus L-norleucine + CO2 + NH3
-
 ?
N-carbamoyl-DL-norvaline + H2O
-
 Geobacillus stearothermophilus L-norvaline + CO2 + NH3
-
 ?
N-formyl-DL-alanine + H2O
-
 Geobacillus stearothermophilus L-alanine + CO2
-
 ?
N-formyl-DL-alanine + H2O
-
 Geobacillus stearothermophilus CECT43 L-alanine + CO2
-
 ?
N-formyl-DL-aminobutyric acid + H2O
-
 Geobacillus stearothermophilus L-aminobutyric acid + CO2
-
 ?
N-formyl-DL-ethionine + H2O
-
 Geobacillus stearothermophilus L-ethionine + CO2
-
 ?
N-formyl-DL-homophenylalanine + H2O
-
 Geobacillus stearothermophilus L-homophenylalanine + CO2
-
 ?
N-formyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus L-methionine + CO2
-
 ?
N-formyl-DL-methionine + H2O
-
 Geobacillus stearothermophilus CECT43 L-methionine + CO2
-
 ?
N-formyl-DL-norleucine + H2O
-
 Geobacillus stearothermophilus L-norleucine + CO2
-
 ?
N-formyl-DL-norvaline + H2O
-
 Geobacillus stearothermophilus L-norvaline + CO2
-
 ?
N-formyl-DL-phenylalanine + H2O
-
 Geobacillus stearothermophilus L-phenylalanine + CO2
-
 ?
N-formyl-DL-phenylglycine + H2O
-
 Geobacillus stearothermophilus L-phenylglycine + CO2
-
 ?
N-formyl-DL-tryptophan + H2O
-
 Geobacillus stearothermophilus L-tryptophan + CO2
-
 ?
N-formyl-DL-tryptophan + H2O
-
 Geobacillus stearothermophilus CECT43 L-tryptophan + CO2
-
 ?

Synonyms

Synonyms Comment Organism
BsLcar
-
 Geobacillus stearothermophilus
L-N-carbamoylase
-
 Geobacillus stearothermophilus

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

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