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Literature summary extracted from
- Identification of D-carbamoylase for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity (2018), Biores. Technol., 249, 720-728 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.5.1.77 | synthesis | D-carbamoylase is used for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity | Arthrobacter crystallopoietes |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.5.1.77 | gene hyuD, sequence comparisons and phylogenetic tree, recombinant, mostly soluble His-tagged enzyme overexpression in Escherichia coli strain BL21(DE3) | Arthrobacter crystallopoietes |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.5.1.77 | additional information | a dynamic kinetic resolution (DKR) cascade is developed by combining Arthrobacter crystallopoietes D-carbamoylase AcHyuC with hydantoin racemase from Arthrobacter aurescens (AaHyuA) and D-hydantoinase from Agrobacterium tumefaciens (AtHyuH) for enantioselective resolution of L-indolylmethylhydantoin into D-Trp. Optimization of substrate/enzyme loadings in DKR cascade. Development and evaluation of the cascade system, overview. Inhibitory effect of detergents | Arthrobacter crystallopoietes |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.77 | Ca2+ | strong inhibition | Arthrobacter crystallopoietes |  |
| 3.5.1.77 | Cu2+ | strong inhibition | Arthrobacter crystallopoietes | |
| 3.5.1.77 | Ni2+ | slight inhibition | Arthrobacter crystallopoietes | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.77 | Ca2+ | slight activation | Arthrobacter crystallopoietes | |
| 3.5.1.77 | EDTA | slight activation | Arthrobacter crystallopoietes | |
| 3.5.1.77 | Mn2+ | slight activation | Arthrobacter crystallopoietes | |
| 3.5.1.77 | additional information | poor effect by Mg2+, Zn2+, and Fe2+ | Arthrobacter crystallopoietes |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.77 | N-carbamoyl-D-amino acid + H2O | Arthrobacter crystallopoietes | - |
D-amino acid + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-amino acid + H2O | Arthrobacter crystallopoietes CGMCC1.1926 | - |
D-amino acid + NH3 + CO2 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.77 | Arthrobacter crystallopoietes | Q84FR7 | - |
- |
| 3.5.1.77 | Arthrobacter crystallopoietes CGMCC1.1926 | Q84FR7 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.5.1.77 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Arthrobacter crystallopoietes |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.77 | 0.84 | - |
purified recombinant His-tagged enzyme, pH 8.0, 30°C, substrate N-carbamoyl-D-tryptophan | Arthrobacter crystallopoietes |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.77 | additional information | the enantioselective D-carbamoylase (AcHyuC) from Arthrobacter crystallopoietes is much more compatible with hydantoinase process than other reported D-N-carbamoylases. AcHyuC has a substrate preference for aromatic carbamoyl-compounds. No activity with N-carbamoyl-DL-2-chlorophenylglycine, N-carbamoyl-DL-methionine, N-carbamoyl-DL-leucine, and N-carbamoyl-DL-isoleucine | Arthrobacter crystallopoietes | ? | - |
- |
|
| 3.5.1.77 | additional information | the enantioselective D-carbamoylase (AcHyuC) from Arthrobacter crystallopoietes is much more compatible with hydantoinase process than other reported D-N-carbamoylases. AcHyuC has a substrate preference for aromatic carbamoyl-compounds. No activity with N-carbamoyl-DL-2-chlorophenylglycine, N-carbamoyl-DL-methionine, N-carbamoyl-DL-leucine, and N-carbamoyl-DL-isoleucine | Arthrobacter crystallopoietes CGMCC1.1926 | ? | - |
- |
|
| 3.5.1.77 | N-carbamoyl-D-amino acid + H2O | - |
Arthrobacter crystallopoietes | D-amino acid + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-amino acid + H2O | - |
Arthrobacter crystallopoietes CGMCC1.1926 | D-amino acid + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-phenylalanine + H2O | N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes | D-phenylalanine + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-phenylalanine + H2O | N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes CGMCC1.1926 | D-phenylalanine + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-phenylglycine + H2O | N-carbamoyl-DL-phenylglycine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes | D-phenylglycine + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-phenylglycine + H2O | N-carbamoyl-DL-phenylglycine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes CGMCC1.1926 | D-phenylglycine + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-tryptophan + H2O | N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes | D-tryptophan + NH3 + CO2 | - |
? | |
| 3.5.1.77 | N-carbamoyl-D-tryptophan + H2O | N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes CGMCC1.1926 | D-tryptophan + NH3 + CO2 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.77 | ? | x * 38280, sequence calculation, x * 39000, recombinant His-tagged enzyme, SDS-PAGE | Arthrobacter crystallopoietes |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.77 | AcHyuC | - |
Arthrobacter crystallopoietes |
| 3.5.1.77 | D-carbamoylase | - |
Arthrobacter crystallopoietes |
| 3.5.1.77 | D-N-carbamoylase | - |
Arthrobacter crystallopoietes |
| 3.5.1.77 | hyuD | - |
Arthrobacter crystallopoietes |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.77 | 30 | - |
assay at | Arthrobacter crystallopoietes |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.77 | 30 | - |
purified recombinant His-tagged enzyme, half-life is about 15 h | Arthrobacter crystallopoietes |
| 3.5.1.77 | 40 | - |
purified recombinant His-tagged enzyme, half-life is below 30 min, inactivation after about 7 h | Arthrobacter crystallopoietes |
| 3.5.1.77 | 50 | - |
purified recombinant His-tagged enzyme, inactivation within 1 h | Arthrobacter crystallopoietes |
| 3.5.1.77 | 100 | - |
purified recombinant His-tagged enzyme, 10 min, inactivation | Arthrobacter crystallopoietes |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.77 | 8 | - |
dynamic kinetic resolution (DKR) cascade, assay at | Arthrobacter crystallopoietes |
| 3.5.1.77 | 8.5 | - |
D-carbamoylase AcHyuC alone | Arthrobacter crystallopoietes |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.77 | additional information | the catalytic triad of AcHyuC is presumed to be formed by Glu46, Lys126, and Cys171 | Arthrobacter crystallopoietes |
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