3.5.1.77: N-carbamoyl-D-amino-acid hydrolase
This is an abbreviated version!
For detailed information about N-carbamoyl-D-amino-acid hydrolase, go to the full flat file.
Word Map on EC 3.5.1.77
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3.5.1.77
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agrobacterium
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hydantoin
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radiobacter
-
d-hydantoinase
-
racemase
-
synthesis
-
decarbamoyl
-
shellfish
-
paralytic
-
d-specific
-
nitrilase
-
n-sulfocarbamoyl
-
biotechnology
- 3.5.1.77
-
agrobacterium
- hydantoin
- radiobacter
- d-hydantoinase
- racemase
- synthesis
-
decarbamoyl
-
shellfish
-
paralytic
-
d-specific
- nitrilase
-
n-sulfocarbamoyl
- biotechnology
Reaction
Synonyms
AcHyuC, Amidase, N-carbamoyl-D-amino acid, BJS_06659, carbamoylase, D-carbamoylase, D-N-alpha-Carbamoylase, D-N-carbamoylase, D-NCAase, Dcase, DCase-M3, DCHase, hyuD, N-carbamoyl D-amino acid amidohydrolase, N-Carbamoyl-D-amino acid amidase, N-carbamoyl-D-amino acid amidohydrolase, N-Carbamyl amino acid amidohydrolase, N-Carbamyl-D-amino acid amidohydrolase
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Substrates Products
Substrates Products on EC 3.5.1.77 - N-carbamoyl-D-amino-acid hydrolase
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REACTION DIAGRAM
N-carbamoyl-D-Asp + H2O
D-Asp + NH3 + CO2
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81% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Glu + H2O
D-Glu + NH3 + CO2
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19% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Ile + H2O
D-Ile + NH3 + CO2
-
72% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Met + H2O
D-Met + NH3 + CO2
48% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-Carbamoyl-D-p-chloro-D-phenylglycine + H2O
D-p-Chloro-D-phenylglycine + NH3 + CO2
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78% of the activity with N-carbamoyl-D-phenylglycine
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-
?
N-carbamoyl-D-p-methoxy-D-phenylglycine + H2O
D-p-methoxy-D-phenylglycine + NH3 + CO2
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62% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-Carbamoyl-Gly + H2O
Gly + NH3 + CO2
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12% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
D-4-hydroxyphenylglycine + NH3 + CO2
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-
-
?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
D-4-hydroxyphenylglycine + NH3 + CO2
Bradyrhizobium japonicum CPAC 15
-
-
-
?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
D-4-hydroxyphenylglycine + NH3 + CO2
-
-
-
?
D-Ala + NH3 + CO2
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81% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
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81% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
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63% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
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63% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
Blastobacter sp.
-
29% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
-
23% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
-
23% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
13% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
13% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
D-amino acid + NH3 + CO2
-
-
-
?
N-carbamoyl-D-amino acid + H2O
D-amino acid + NH3 + CO2
Arthrobacter crystallopoietes CGMCC1.1926
-
-
-
?
D-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-hydroxyphenylglycine + H2O
D-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
D-Leu + NH3 + CO2
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as active as with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
-
as active as with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
Blastobacter sp.
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23% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
-
28% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
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28% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
43% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
43% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
98% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
Blastobacter sp.
-
132% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
47% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
activity assay
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-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
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-
-
-
?
D-Phe + NH3 + CO2
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53% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Phe + H2O
D-Phe + NH3 + CO2
-
53% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Phe + H2O
D-Phe + NH3 + CO2
-
62% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Phe + H2O
D-Phe + NH3 + CO2
-
62% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
D-phenylalanine + NH3 + CO2
N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-phenylalanine + H2O
D-phenylalanine + NH3 + CO2
Arthrobacter crystallopoietes CGMCC1.1926
N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
-
110% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
N-carbamoyl-DL-phenylglycine is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
Arthrobacter crystallopoietes CGMCC1.1926
N-carbamoyl-DL-phenylglycine is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
Blastobacter sp.
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170% of the activity with N-carbamoyl-D-Phe
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-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
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24% of the activity with N-carbamoyl-D-Phe
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-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
58% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
58% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
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-
?
D-Ser + NH3 + CO2
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55% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
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-
?
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
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55% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
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-
?
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
Blastobacter sp.
-
10% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
-
7% of the activity with N-carbamoyl-D-Phe
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-
?
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
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7% of the activity with N-carbamoyl-D-Phe
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-
?
D-Trp + NH3 + CO2
-
42% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
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-
?
N-carbamoyl-D-Trp + H2O
D-Trp + NH3 + CO2
Blastobacter sp.
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18% of the activity with N-carbamoyl-D-Phe
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-
?
N-carbamoyl-D-Trp + H2O
D-Trp + NH3 + CO2
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55% of the activity with N-carbamoyl-D-Phe
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-
?
D-tryptophan + NH3 + CO2
N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction
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-
?
N-carbamoyl-D-tryptophan + H2O
D-tryptophan + NH3 + CO2
Arthrobacter crystallopoietes CGMCC1.1926
N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
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38% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
-
38% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
-
42% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
-
42% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
Blastobacter sp.
-
55% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
-
10% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
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10% of the activity with N-carbamoyl-D-Phe
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-
?
?
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110% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-Carbamoyl-DL-2-amino-n-butyric acid + H2O
?
Blastobacter sp.
-
48% of the activity with N-carbamoyl-D-Phe
-
-
?
N-Carbamoyl-DL-2-amino-n-butyric acid + H2O
?
-
14% of the activity with N-carbamoyl-D-Phe
-
-
?
N-Carbamoyl-DL-Met + H2O
?
-
160% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-Carbamoyl-DL-Met + H2O
?
Blastobacter sp.
-
84% of the activity with N-carbamoyl-D-Phe
-
-
?
?
-
105% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-Carbamoyl-DL-norleucine + H2O
?
-
92% of the activity with N-carbamoyl-D-Phe
-
-
?
N-Carbamoyl-DL-norleucine + H2O
?
-
90% of the activity with N-carbamoyl-D-Phe
-
-
?
?
-
76% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-Carbamoyl-DL-norvaline + H2O
?
Blastobacter sp.
-
26% of the activity with N-carbamoyl-D-Phe
-
-
?
N-Carbamoyl-DL-norvaline + H2O
?
-
6% of the activity with N-carbamoyl-D-Phe
-
-
?
?
-
27% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-Carbamoyl-DL-Thr + H2O
?
Blastobacter sp.
-
18% of the activity with N-carbamoyl-D-Phe
-
-
?
additional information
?
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D-stereospecific hydrolysis can be explained by unfavorable van der Waals contacts with an L-isomer
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-
?
additional information
?
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D-stereospecific hydrolysis can be explained by unfavorable van der Waals contacts with an L-isomer
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-
?
additional information
?
-
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no activity with N-acetyl-D-amino acids or N-carbamoyl-L-amino acids as substrate
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-
?
additional information
?
-
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no activity with N-acetyl-D-amino acids or N-carbamoyl-L-amino acids as substrate
-
-
?
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
-
-
-
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
-
-
-
additional information
?
-
Arthrobacter crystallopoietes CGMCC1.1926
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
-
-
-
additional information
?
-
Blastobacter sp.
-
the enzyme does not hydrolyze beta-ureidopropionate
-
-
?
additional information
?
-
modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview
-
-
-
additional information
?
-
-
modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview
-
-
-
additional information
?
-
Bradyrhizobium japonicum CPAC 15
modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview
-
-
-
additional information
?
-
modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview
-
-
-
additional information
?
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strict specificity towards N-carbamoyl-D-amino acids, no activity with N-carbamoyl-L-amino acids
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-
?
additional information
?
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strict specificity towards N-carbamoyl-D-amino acids, no activity with N-carbamoyl-L-amino acids
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-
?