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Literature summary for 3.5.1.77 extracted from

  • Liu, Y.; Xu, G.; Han, R.; Dong, J.; Ni, Y.
    Identification of D-carbamoylase for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity (2018), Biores. Technol., 249, 720-728 .
    View publication on PubMed

Application

Application Comment Organism
synthesis D-carbamoylase is used for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity Arthrobacter crystallopoietes

Cloned(Commentary)

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

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

Inhibitors Comment Organism Structure
Ca2+ strong inhibition Arthrobacter crystallopoietes
Cu2+ strong inhibition Arthrobacter crystallopoietes
Ni2+ slight inhibition Arthrobacter crystallopoietes

Metals/Ions

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Arthrobacter crystallopoietes Q84FR7
-
-
Arthrobacter crystallopoietes CGMCC1.1926 Q84FR7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Arthrobacter crystallopoietes

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

Subunits Comment Organism
? x * 38280, sequence calculation, x * 39000, recombinant His-tagged enzyme, SDS-PAGE Arthrobacter crystallopoietes

Synonyms

Synonyms Comment Organism
AcHyuC
-
Arthrobacter crystallopoietes
D-carbamoylase
-
Arthrobacter crystallopoietes
D-N-carbamoylase
-
Arthrobacter crystallopoietes
hyuD
-
Arthrobacter crystallopoietes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Arthrobacter crystallopoietes

Temperature Stability [°C]

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

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

General Information Comment Organism
additional information the catalytic triad of AcHyuC is presumed to be formed by Glu46, Lys126, and Cys171 Arthrobacter crystallopoietes