Application | Comment | Organism |
---|---|---|
synthesis | D-carbamoylase is used for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity | Arthrobacter crystallopoietes |
Cloned (Comment) | Organism |
---|---|
gene hyuD, sequence comparisons and phylogenetic tree, recombinant, mostly soluble His-tagged enzyme overexpression in Escherichia coli strain BL21(DE3) | Arthrobacter crystallopoietes |
Protein Variants | Comment | Organism |
---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | strong inhibition | Arthrobacter crystallopoietes | |
Cu2+ | strong inhibition | Arthrobacter crystallopoietes | |
Ni2+ | slight inhibition | Arthrobacter crystallopoietes |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | slight activation | Arthrobacter crystallopoietes | |
EDTA | slight activation | Arthrobacter crystallopoietes | |
Mn2+ | slight activation | Arthrobacter crystallopoietes | |
additional information | poor effect by Mg2+, Zn2+, and Fe2+ | Arthrobacter crystallopoietes |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-carbamoyl-D-amino acid + H2O | Arthrobacter crystallopoietes | - |
D-amino acid + NH3 + CO2 | - |
? | |
N-carbamoyl-D-amino acid + H2O | Arthrobacter crystallopoietes CGMCC1.1926 | - |
D-amino acid + NH3 + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arthrobacter crystallopoietes | Q84FR7 | - |
- |
Arthrobacter crystallopoietes CGMCC1.1926 | Q84FR7 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Arthrobacter crystallopoietes |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.84 | - |
purified recombinant His-tagged enzyme, pH 8.0, 30°C, substrate N-carbamoyl-D-tryptophan | Arthrobacter crystallopoietes |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | - |
- |
|
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 | ? | - |
- |
|
N-carbamoyl-D-amino acid + H2O | - |
Arthrobacter crystallopoietes | D-amino acid + NH3 + CO2 | - |
? | |
N-carbamoyl-D-amino acid + H2O | - |
Arthrobacter crystallopoietes CGMCC1.1926 | D-amino acid + NH3 + CO2 | - |
? | |
N-carbamoyl-D-phenylalanine + H2O | N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes | D-phenylalanine + NH3 + CO2 | - |
? | |
N-carbamoyl-D-phenylalanine + H2O | N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes CGMCC1.1926 | D-phenylalanine + NH3 + CO2 | - |
? | |
N-carbamoyl-D-phenylglycine + H2O | N-carbamoyl-DL-phenylglycine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes | D-phenylglycine + NH3 + CO2 | - |
? | |
N-carbamoyl-D-phenylglycine + H2O | N-carbamoyl-DL-phenylglycine is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes CGMCC1.1926 | D-phenylglycine + NH3 + CO2 | - |
? | |
N-carbamoyl-D-tryptophan + H2O | N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes | D-tryptophan + NH3 + CO2 | - |
? | |
N-carbamoyl-D-tryptophan + H2O | N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction | Arthrobacter crystallopoietes CGMCC1.1926 | D-tryptophan + NH3 + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 38280, sequence calculation, x * 39000, recombinant His-tagged enzyme, SDS-PAGE | Arthrobacter crystallopoietes |
Synonyms | Comment | Organism |
---|---|---|
AcHyuC | - |
Arthrobacter crystallopoietes |
D-carbamoylase | - |
Arthrobacter crystallopoietes |
D-N-carbamoylase | - |
Arthrobacter crystallopoietes |
hyuD | - |
Arthrobacter crystallopoietes |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Arthrobacter crystallopoietes |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
purified recombinant His-tagged enzyme, half-life is about 15 h | Arthrobacter crystallopoietes |
40 | - |
purified recombinant His-tagged enzyme, half-life is below 30 min, inactivation after about 7 h | Arthrobacter crystallopoietes |
50 | - |
purified recombinant His-tagged enzyme, inactivation within 1 h | Arthrobacter crystallopoietes |
100 | - |
purified recombinant His-tagged enzyme, 10 min, inactivation | Arthrobacter crystallopoietes |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
dynamic kinetic resolution (DKR) cascade, assay at | Arthrobacter crystallopoietes |
8.5 | - |
D-carbamoylase AcHyuC alone | Arthrobacter crystallopoietes |
General Information | Comment | Organism |
---|---|---|
additional information | the catalytic triad of AcHyuC is presumed to be formed by Glu46, Lys126, and Cys171 | Arthrobacter crystallopoietes |