EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.5.1.87 | an N-carbamoyl-L-2-amino acid + H2O |
- |
Brevibacillus reuszeri |
an L-2-amino acid + NH3 + CO2 |
- |
? |
| 3.5.1.87 | more |
strictly specific for the L-form of N-carbamoyl-amino acids as substrates and exhibits high activity in the hydrolysis of N-carbamoyl-L-cysteine as substrate |
Pseudomonas sp. ON4a |
? |
- |
? |
| 3.5.1.87 | more |
the enzyme in this study is strigently L-specific |
Geobacillus kaustophilus |
? |
- |
? |
| 3.5.1.87 | more |
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 | more |
the enzyme is a strict enantiospecific L-N-carbamoylase. Development of a bienzymatic system comprising an N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264 and the enantiospecific L-N-carbamoylase from Geobacillus stearothermophilus CECT43. The biocatalyst system is able to produce optically pure natural and non-natural L-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate is found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and the an N-succinylamino acid racemase proves to be the limiting stepof the system due to its lower specific activity, overview |
Geobacillus stearothermophilus |
? |
- |
? |
| 3.5.1.87 | more |
the enzyme shows stereospecificity and a broad substrate specificity. No or poor activitz with N-carbamoyl-alpha-alanine, N-carbamoyl-glycine, N-carbamoyl-beta-alanine, and N-carbamoyl-alpha-aminoisobutyrate |
Brevibacillus reuszeri |
? |
- |
? |
| 3.5.1.87 | more |
the enzyme shows stereospecificity and a broad substrate specificity. No or poor activitz with N-carbamoyl-alpha-alanine, N-carbamoyl-glycine, N-carbamoyl-beta-alanine, and N-carbamoyl-alpha-aminoisobutyrate |
Brevibacillus reuszeri HSN1 |
? |
- |
? |
| 3.5.1.87 | more |
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 | more |
the enzyme is a strict enantiospecific L-N-carbamoylase. Development of a bienzymatic system comprising an N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264 and the enantiospecific L-N-carbamoylase from Geobacillus stearothermophilus CECT43. The biocatalyst system is able to produce optically pure natural and non-natural L-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate is found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and the an N-succinylamino acid racemase proves to be the limiting stepof the system due to its lower specific activity, overview |
Geobacillus stearothermophilus CECT43 |
? |
- |
? |
| 3.5.1.87 | N-acetyl-L-alanine + H2O |
- |
Geobacillus stearothermophilus |
L-alanine + acetate |
- |
? |
