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DL-5-(p-Hydroxyphenyl)hydantoin + H2O
?
Blastobacter sp.
-
-
-
-
?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
D-4-hydroxyphenylglycine + NH3 + CO2
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
N-carbamoyl-D-amino acid + H2O
D-amino acid + NH3 + CO2
N-carbamoyl-D-Asp + H2O
D-Asp + NH3 + CO2
-
81% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Glu + H2O
D-Glu + NH3 + CO2
-
19% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-hydroxyphenylglycine + H2O
D-hydroxyphenylglycine + NH3 + CO2
N-carbamoyl-D-Ile + H2O
D-Ile + NH3 + CO2
-
72% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
N-carbamoyl-D-Met + H2O
D-Met + NH3 + CO2
48% of activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-norleucine + H2O
D-norleucine + NH3 + CO2
Blastobacter sp.
-
-
-
-
?
N-Carbamoyl-D-p-chloro-D-phenylglycine + H2O
D-p-Chloro-D-phenylglycine + NH3 + CO2
-
78% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
N-carbamoyl-D-p-methoxy-D-phenylglycine + H2O
D-p-methoxy-D-phenylglycine + NH3 + CO2
-
62% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Phe + H2O
D-Phe + NH3 + CO2
N-carbamoyl-D-phenylalanine + H2O
D-phenylalanine + NH3 + CO2
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
N-carbamoyl-D-Trp + H2O
D-Trp + NH3 + CO2
N-carbamoyl-D-tryptophan + H2O
D-tryptophan + NH3 + CO2
N-carbamoyl-D-Tyr + H2O
D-Tyr + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
N-Carbamoyl-DL-2-amino-n-butyric acid + H2O
?
N-Carbamoyl-DL-Met + H2O
?
N-Carbamoyl-DL-norleucine + H2O
?
N-Carbamoyl-DL-norvaline + H2O
?
N-Carbamoyl-DL-Thr + H2O
?
N-Carbamoyl-Gly + H2O
Gly + NH3 + CO2
-
12% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
additional information
?
-
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
D-4-hydroxyphenylglycine + NH3 + CO2
-
-
-
?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
D-4-hydroxyphenylglycine + NH3 + CO2
-
-
-
?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
D-4-hydroxyphenylglycine + NH3 + CO2
-
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
-
81% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
-
81% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
-
63% of the activity with N-carbamoyl-D-phenylglycine
-
-
?
N-carbamoyl-D-Ala + H2O
D-Ala + NH3 + CO2
-
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
-
-
?
N-carbamoyl-D-amino acid + H2O
D-amino acid + NH3 + CO2
-
-
-
?
N-carbamoyl-D-amino acid + H2O
D-amino acid + NH3 + CO2
-
-
-
?
N-carbamoyl-D-hydroxyphenylglycine + H2O
D-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-hydroxyphenylglycine + H2O
D-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
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
-
as active as with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Leu + H2O
D-Leu + NH3 + CO2
Blastobacter sp.
-
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
-
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
-
-
?
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
-
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
-
-
?
N-carbamoyl-D-p-hydroxyphenylglycine + H2O
D-p-hydroxyphenylglycine + NH3 + CO2
-
-
-
-
?
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
-
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
-
-
?
N-carbamoyl-D-Phe + H2O
D-Phe + NH3 + CO2
Blastobacter sp.
-
-
-
-
?
N-carbamoyl-D-Phe + H2O
D-Phe + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-Phe + H2O
D-Phe + NH3 + CO2
-
-
-
-
?
N-carbamoyl-D-phenylalanine + H2O
D-phenylalanine + NH3 + CO2
N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-phenylalanine + H2O
D-phenylalanine + NH3 + CO2
N-carbamoyl-DL-phenylalanine is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
-
-
-
-
?
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
N-carbamoyl-DL-phenylglycine is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
Blastobacter sp.
-
170% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-phenylglycine + H2O
D-phenylglycine + NH3 + CO2
-
24% of the activity with N-carbamoyl-D-Phe
-
-
?
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
-
-
?
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
-
55% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
-
55% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
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
-
-
?
N-carbamoyl-D-Ser + H2O
D-Ser + NH3 + CO2
-
7% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Trp + H2O
D-Trp + NH3 + CO2
-
42% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-carbamoyl-D-Trp + H2O
D-Trp + NH3 + CO2
Blastobacter sp.
-
18% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-Trp + H2O
D-Trp + NH3 + CO2
-
55% of the activity with N-carbamoyl-D-Phe
-
-
?
N-carbamoyl-D-tryptophan + H2O
D-tryptophan + NH3 + CO2
N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-tryptophan + H2O
D-tryptophan + NH3 + CO2
N-carbamoyl-DL-tryptophan is used as substrate, enantiospecific reaction
-
-
?
N-carbamoyl-D-Val + H2O
D-Val + NH3 + CO2
-
-
-
-
?
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
-
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
-
10% of the activity with N-carbamoyl-D-Phe
-
-
?
N-Carbamoyl-DL-2-amino-n-butyric acid + H2O
?
-
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
?
-
-
-
-
?
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
-
-
?
N-Carbamoyl-DL-Met + H2O
?
-
92% of the activity with N-carbamoyl-D-Phe
-
-
?
N-Carbamoyl-DL-norleucine + H2O
?
-
105% of the activity with N-carbamoyl-D-p-hydroxyphenylglycine
-
-
?
N-Carbamoyl-DL-norleucine + H2O
?
Blastobacter sp.
-
-
-
-
?
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
-
-
?
N-Carbamoyl-DL-norvaline + H2O
?
-
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
-
-
?
N-Carbamoyl-DL-Thr + H2O
?
-
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
-
-
?
N-Carbamoyl-DL-Thr + H2O
?
-
3% of the activity with N-carbamoyl-D-Phe
-
-
?
additional information
?
-
-
strictly D-specific
-
-
?
additional information
?
-
-
D-stereospecific hydrolysis can be explained by unfavorable van der Waals contacts with an L-isomer
-
-
?
additional information
?
-
-
D-stereospecific hydrolysis can be explained by unfavorable van der Waals contacts with an L-isomer
-
-
?
additional information
?
-
-
no activity with N-acetyl-D-amino acids or N-carbamoyl-L-amino acids as substrate
-
-
?
additional information
?
-
-
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
?
-
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
?
-
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
?
-
strict specificity towards N-carbamoyl-D-amino acids, no activity with N-carbamoyl-L-amino acids
-
-
?
additional information
?
-
strict specificity towards N-carbamoyl-D-amino acids, no activity with N-carbamoyl-L-amino acids
-
-
?
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H57L
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
H57Y
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
P203A
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203H
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203I
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203L
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
P203N
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
P203S
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
P203T
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
V236A
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
V236S
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
V236T
-
mutant Val236Ala shows a 10°C increase in thermostability compared to the wild type enzyme. The following mutant enzymes show increased thermostability: His57Leu, Pro203Asn, Pro203Glu, Pro203Ala, Pro203Ile, Pro203His, Pro203Thr, Val236Thr, Val236Ser
H57Y
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
-
P203L
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
-
P203S
-
mutant enzymes His57Tyr, Pro203Leu or Pro203Ser show an improved thermostability by about 5°C compared with those of the wild type enzyme
-
A222C
-
crystal structure is nearly identical to wild-type enzyme, half-life at 50°C is 1.1fold higher than that of wild-type enzyme
A302C
-
crystal structure is nearly identical to wild-type enzyme, 123.9% of wild-type activity, temperature-optimum is 10°C higher than that of wild-type enzyme, half-life at 50°C is 2.5fold higher than that of wild-type enzyme, 4.2fold increase in kcat/Km at 65°C, 1.5fold increase at 55°C and 1.15fold increase at 37°C
G75S
-
96% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 42.5% compared to 5% for the wild-type enzyme
G75S/V237A
-
mutant, thermal stability 55.6%, wild-type 3.0%, oxidative stability 42.8%, wild-type 5.0%
H129A
-
inactive mutant enzyme
H129N
-
inactive mutant enzyme
H129R
-
inactive mutant enzyme
H144A
-
5% of the activity of wild-type enzyme
H215A
-
17% of the activity of wild-type enzyme
H58Y
-
80% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 20.6% compared to 5% for the wild-type enzyme
I286V/F287A
-
mutant, thermal stability 4.5%, wild-type 3.0%, oxidative stability 4.8%, wild-type 5.0%
M167L/M169L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 37% for mutant enzyme, compared to 21% for wild-type enzyme
M184L/T262A
-
46% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 54.8% compared to 5% for the wild-type enzyme. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 58.6% of the wild-type ratio
M220L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 62% for mutant enzyme, compared to 21% for wild-type enzyme
M239L
-
mutant enzyme is stable after treatment with 0.5 mM H2O2 for 15 min compared to 79% loss of wild-type activity
M239L/M244L
-
mutant enzyme is stable after treatment with 0.5 mM H2O2 for 15 min compared to 79% loss of wild-type activity
M244L
-
mutant enzyme is stable after treatment with 0.5 mM H2O2 for 15 min compared to 79% loss of wild-type activity
M31L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 8% for mutant enzyme, compared to 21% for wild-type enzyme
M5L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 51% for mutant enzyme, compared to 21% for wild-type enzyme
M73L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 84% for mutant enzyme, compared to 21% for wild-type enzyme
N173A
-
KM-value for N-carbamoyl-D-p-hydroxyphenylglycine is 40% of the wild-type value. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 5.5fold lower than wild-type ratio. Tm is 68°C compared to 63° for wild-type enzyme
P178C
-
half-life at 50°C is nearly identical to wild-type enzyme
P295C/F304C
-
107.3% of wild-type activity, temperature-optimum is 5°C higher than that of wild-type enzyme, half-life at 50°C is 2fold higher than that of wild-type enzyme. 2.5fold increase in kcat/Km at 65°C, 1.1fold increase at 55°C and at 37°C
Q23L
-
81% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 63.9% compared to 5% for the wild-type enzyme
Q23L/V40A/H58Y/G75S/M184L/T262A
-
mutant enzyme with improved oxidative and thermostability, 79.3% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 72.4% of the wild-type ratio
R175A
-
inactive mutant enzyme
R175K
-
KM-value for N-carbamoyl-D-p-hydroxyphenylglycine is 2.5fold higher than the wild-type value. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 4706fold lower than wild-type ratio. Tm is 65°C compared to 63° for wild-type enzyme
R176A
-
inactive mutant enzyme
R176K
-
KM-value for N-carbamoyl-D-p-hydroxyphenylglycine is 4.2fold higher than the wild-type value. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 364fold lower than wild-type ratio. Tm is 65°C compared to 63° for wild-type enzyme
V237A/C279S
-
mutant, thermal stability 22.4%, wild-type 3.0%, oxidative stability 31.2%, wild-type 5.0%
V40A/G75S/V237A
-
mutant, thermal stability 68.4%, wild-type 3.0%, oxidative stability 80.3%, wild-type 5.0%
V40A/G75S/V237A/I286V/F287A
-
mutant, thermal stability 72.3%, wild-type 3.0%, oxidative stability 83.1%, wild-type 5.0%
M184L
-
80% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 20% compared to 5% for the wild-type enzyme
-
M184L/T262A
-
46% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 54.8% compared to 5% for the wild-type enzyme. The ratio of turnover number to Km-value for N-carbamoyl-D-p-hydroxyphenylglycine is 58.6% of the wild-type ratio
-
Q23L
-
81% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 63.9% compared to 5% for the wild-type enzyme
-
C172A
-
mutant enzyme Cys172Ala or Cys172Ser is completely inactive. Substitution of any of the other Cys has no effect on enzyme activity
-
C172S
-
mutant enzyme Cys172Ala or Cys172Ser is completely inactive. Substitution of any of the other Cys has no effect on enzyme activity
-
A164T
-
mutant, screening for thermostable enzyme
A18T/Y30N/K34E
-
kinetic properties and thermodynamic parameters of the mutant enzyme are identical with those of the wild-type enzyme. More than 80% improve in solubility compared to wild-type enzyme
A36E
-
mutant, screening for thermostable enzyme
A36V
-
mutant, screening for thermostable enzyme
H248Q
-
mutant, screening for thermostable enzyme
H248Q/T262A
-
the mutant displays a T50 value of 65°C and a DELTAT50 enhancement of 8°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
H58Y
-
mutant, screening for thermostable enzyme
K34D
-
mutant has higher solubility than wild-type enzyme
K34E
-
mutant has higher solubility than wild-type enzyme
Q12A
-
saturation mutagenesis at position Gln12, thermostability 13.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12C
-
saturation mutagenesis at position Gln12, thermostability 9.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12D
-
saturation mutagenesis at position Gln12, thermostability 8.9%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12E
-
saturation mutagenesis at position Gln12, thermostability 9.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12F
-
saturation mutagenesis at position Gln12, thermostability 14.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12G
-
saturation mutagenesis at position Gln12, thermostability 20.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12H
-
saturation mutagenesis at position Gln12, thermostability 12.8%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12I
-
saturation mutagenesis at position Gln12, thermostability 14.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12K
-
saturation mutagenesis at position Gln12, thermostability 11.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12L/Q23L/H248Q/T262A/T263S
-
the mutant exhibits an increase of 10°C in thermostability compared with the parental enzyme M3
Q12L/Q23L/H248Q/T262A/T263S/A273K
-
the mutant displays a T50 value of 69°C and a DELTAT50 enhancement of 12°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/E266D
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/M31L
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/M31L/N242G
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/M31L/Q207E
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N242G
-
the mutant displays a T50 value of 69°C and a DELTAT50 enhancement of 12°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N242G/A273P
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N242G/T271I/A273P
-
the mutant displays a T50 value of 72°C and a DELTAT50 enhancement of 15°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/N93Y
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/Q207E
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/Q207E/N242G
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/T271I
-
the mutant displays a T50 value of 69°C and a DELTAT50 enhancement of 12°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/H248Q/T262A/T263S/T271I/A273K
-
the mutant displays a T50 value of 71°C and a DELTAT50 enhancement of 14°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
Q12L/Q23L/Q207E/N242G/H248Q/T262A/T263S/E266D/T271I/A273P
-
the mutant displays a T50 value of 73°C and a DELTAT50 enhancement of 16°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%). The mutant retains over 50% of its initial activity after heat treatment at 57°C for at least 100 min
Q12M
-
saturation mutagenesis at position Gln12, thermostability 9.2%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12N
-
saturation mutagenesis at position Gln12, thermostability 15.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12P
-
saturation mutagenesis at position Gln12, thermostability 12.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12R
-
saturation mutagenesis at position Gln12, thermostability 9.2%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12S
-
saturation mutagenesis at position Gln12, thermostability 12.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12T
-
saturation mutagenesis at position Gln12, thermostability 14.8%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12V
-
saturation mutagenesis at position Gln12, thermostability 20.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12W
-
saturation mutagenesis at position Gln12, thermostability 16.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12Y
-
saturation mutagenesis at position Gln12, thermostability 11.9%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T262A
-
mutant, screening for thermostable enzyme
T263A
-
saturation mutagenesis at position Thr263, thermostability 8.6%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263C
-
saturation mutagenesis at position Thr263, thermostability 13.2%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263D
-
saturation mutagenesis at position Thr263, thermostability 10.3%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263E
-
saturation mutagenesis at position Thr263, thermostability 12.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263F
-
saturation mutagenesis at position Thr263, thermostability 13.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263G
-
saturation mutagenesis at position Thr263, thermostability 15.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263H
-
saturation mutagenesis at position Thr263, thermostability 15.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263I
-
saturation mutagenesis at position Thr263, thermostability 14.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263K
-
saturation mutagenesis at position Thr263, thermostability 11.8%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263L
-
saturation mutagenesis at position Thr263, thermostability 10.4%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263M
-
saturation mutagenesis at position Thr263, thermostability 23.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263N
-
saturation mutagenesis at position Thr263, thermostability 14.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263P
-
saturation mutagenesis at position Thr263, thermostability 14.6%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263Q
-
saturation mutagenesis at position Thr263, thermostability 10.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263R
-
saturation mutagenesis at position Thr263, thermostability 9.6%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263V
-
saturation mutagenesis at position Thr263, thermostability 8.7%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263W
-
saturation mutagenesis at position Thr263, thermostability 9.5%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
T263Y
-
saturation mutagenesis at position Thr263, thermostability 12.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
V237A
-
mutant, screening for thermostable enzyme
H248Q/T262A
-
the mutant displays a T50 value of 65°C and a DELTAT50 enhancement of 8°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
-
Q12L
-
the mutant displays a T50 value of 63°C and a DELTAT50 enhancement of 6°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
-
Q12L/Q23L/H248Q/T262A/T263S
-
the mutant exhibits an increase of 10°C in thermostability compared with the parental enzyme M3
-
Q12L/Q23L/H248Q/T262A/T263S/M31L
-
the mutant displays a T50 value of 68°C and a DELTAT50 enhancement of 11°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
-
Q12L/Q23L/Q207E/N242G/H248Q/T262A/T263S/E266D/T271I/A273P
-
the mutant displays a T50 value of 73°C and a DELTAT50 enhancement of 16°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%). The mutant retains over 50% of its initial activity after heat treatment at 57°C for at least 100 min
-
C172A
-
mutant enzyme Cys172Ala or Cys172Ser is completely inactive. Substitution of any of the other Cys has no effect on enzyme activity
C172A
-
inactive mutant enzyme
C172S
-
mutant enzyme Cys172Ala or Cys172Ser is completely inactive. Substitution of any of the other Cys has no effect on enzyme activity
C172S
-
less than 0.1% of the wild-type enzyme
M184L
-
80% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 20% compared to 5% for the wild-type enzyme
M184L
-
residual activity after treatment with 0.5 mM H2O2 for 15 min is 57% for mutant enzyme, compared to 21% for wild-type enzyme
T262A
-
49% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 40.9% compared to 5% for the wild-type enzyme
T262A
-
1.5fold increased activity, improvement in expression levels, mutation results in a significant improvement in both oxidative stability and thermostability, increases stability of N-carbamoylase in vivo, thereby preventing it from degradation by cellular proteases
V40A
-
93% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 20.6% compared to 5% for the wild-type enzyme
V40A
-
2fold increased activity, improvement in expression levels, mutation mainly gives rise to the increase in oxidative stability rather than thermostability
T262A
-
49% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 40.9% compared to 5% for the wild-type enzyme
-
T262A
-
1.5fold increased activity, improvement in expression levels, mutation results in a significant improvement in both oxidative stability and thermostability, increases stability of N-carbamoylase in vivo, thereby preventing it from degradation by cellular proteases
-
V40A
-
93% loss of activity of mutant enzyme M184L after 30 min at 70°C, compared to 90% loss of wild-type enzyme. Residual activity after incubation with 0.2 mM H2O2 for 30 min at 25°C is 20.6% compared to 5% for the wild-type enzyme
-
V40A
-
2fold increased activity, improvement in expression levels, mutation mainly gives rise to the increase in oxidative stability rather than thermostability
-
Q12L
-
mutant, screening for thermostable enzyme
Q12L
-
saturation mutagenesis at position Gln12, thermostability 47.2%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
Q12L
-
the mutant displays a T50 value of 63°C and a DELTAT50 enhancement of 6°C compared with CDase-M3 (T50 is defined as the temperature at which heat treatment for 15 min reduces the initial activity by 50%)
T263S
-
mutant, screening for thermostable enzyme
T263S
-
saturation mutagenesis at position Thr263, thermostability 25.0%, wild-type 12.3%, incubation at various temperatures, residual activity is calculated relative to the activity of the non-heat treated enzyme
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
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
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
-
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Ogawa, J.; Shimizu, S.; Yamada, H.
N-Carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c. Purification and characterization
Eur. J. Biochem.
212
685-691
1993
Comamonas sp., Comamonas sp. E222c
brenda
Grifantini, R.; Pratesi, C.; Galli, G.; Grandi, G.
Topological mapping of the cysteine residues of N-carbamoyl-D-amino-acid amidohydrolase and their role in enzymatic activity
J. Biol. Chem.
271
9326-9331
1996
Agrobacterium tumefaciens, Agrobacterium tumefaciens NTRRL B11291
brenda
Nanba, H.; Ikenaka, Y.; Yamada, Y.; Yajima, K.; Takano, M.; Takahashi, S.
Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme
Biosci. Biotechnol. Biochem.
62
875-881
1998
Agrobacterium sp., Agrobacterium sp. KNK712
brenda
Ogawa, J.; Chung, M.C.M.; Hida, S.; Yamada, H.; Shimizu, S.
Thermostable N-carbamoyl-D-amino acid amidohydrolase: screening, purification and characterization
J. Biotechnol.
38
11-19
1994
Blastobacter sp.
brenda
Ikenaka, Y.; Nanba, H.; Yajima, K.; Yamada, Y.; Takano, M.; Takahashi, S.
Relationship between an increase in thermostability and amino acid substitution in N-carbamyl-D-amino acid amidohydrolase
Biosci. Biotechnol. Biochem.
62
1672-1675
1998
Agrobacterium sp.
brenda
Ikenaka, Y.; Nanba, H.; Yajima, K.; Yamada, Y.; Takano, M.; Takahashi, S.
Increase in thermostability of N-carbamyl-D-amino acid amidohydrolase on amino acid substitutions
Biosci. Biotechnol. Biochem.
62
1668-1671
1998
Agrobacterium sp., Agrobacterium sp. KNK712
brenda
Nanba, H.; Ikenaka, Y.; Yamada, Y.; Yajima, K.; Takano, M.; Ohkubo, K.; Hiraishi, Y.; Yamada, K.; Takahashi, S.
Immobilization of N-carbamyl-D-amino acid amidohydrolase
Biosci. Biotechnol. Biochem.
62
1839-1844
1998
Agrobacterium sp., Agrobacterium sp. KNK712, Pseudomonas sp.
brenda
Louwrier, A.; Knowles, C.J.
The purification and characterization of a novel D(-)-specific carbamoylase enzyme from an Agrobacterium sp.
Enzyme Microb. Technol.
19
562-571
1996
Agrobacterium sp.
-
brenda
Olivieri, R.; Fascetti, E.; Angelini, L.; Degen, L.
Enzymatic conversion of N-carbamoyl-D-amino acids to D-amino acids
Enzyme Microb. Technol.
1
201-204
1979
Agrobacterium tumefaciens, Agrobacterium tumefaciens NTRRL B11291
-
brenda
Kim, G.J.; Kim, H.S.
Optimization of the enzymatic synthesis of D-p-hydroxyphenylglycine from DL-5-substituted hydantoin using D-hydantoinase and N-carbamoylase
Enzyme Microb. Technol.
17
63-67
1995
Agrobacterium sp., Agrobacterium sp. 1-671
-
brenda
Hsu, W.H.; Chien, F.T.; Hsu, C.L.; Wang, T.C.; Yuan, H.S.; Wang, W.C.
Expression, crystallization and preliminary x-ray diffraction studies of N-carbamyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter
Acta Crystallogr. Sect. D
D55
694-695
1999
Agrobacterium tumefaciens, Agrobacterium tumefaciens CCRC 14924
brenda
Chien, H.C.R.; Hsu, C.L.; Hu, H.Y.; Wang, W.C.; Hsu, W.H.
Enhancing oxidative resistance of Agrobacterium radiobacter N-carbamoyl D-amino acid amidohydrolase by engineering solvent-accessible methionine residues
Biochem. Biophys. Res. Commun.
297
282-287
2002
Agrobacterium tumefaciens
brenda
Chen, C.Y.; Chiu, W.C.; Liu, J.S.; Hsu, W.H.; Wang, W.C.
Structural basis for catalysis and substrate specificity of Agrobacterium radiobacter N-carbamoyl-D-amino acid amidohydrolase
J. Biol. Chem.
278
26194-26201
2003
Agrobacterium tumefaciens
brenda
Wang, W.C.; Hsu, W.H.; Chien, F.T.; Chen, C.Y.
Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft
J. Mol. Biol.
306
251-261
2001
Agrobacterium tumefaciens
brenda
Oh, K.H.; Nam, S.H.; Kim, H.S.
Improvement of oxidative and thermostability of N-carbamyl-D-amino acid amidohydrolase by directed evolution
Protein Eng.
15
689-695
2002
Agrobacterium tumefaciens, Agrobacterium tumefaciens NRRL B11291
brenda
Nakai, T.; Hasegawa, T.; Yamashita, E.; Yamamoto, M.; Kumasaka, T.; Ueki, T.; Nanba, H.; Ikenaka, Y.; Takahashi, S.; Sato, M.; Tsukihara, T.
Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases
Structure
8
729-738
2000
Agrobacterium sp., Agrobacterium sp. KNK712
brenda
Wu, S.; Liu, Y.; Zhao, G.; Wang, J.; Sun, W.
Thermostable D-carbamoylase from Sinorhizobium morelens S-5: purification, characterization and gene expression in Escherichia coli
Biochimie
88
237-244
2006
Ensifer adhaerens (Q5S260), Ensifer adhaerens S-5 (Q5S260)
brenda
Chiu, W.C.; You, J.Y.; Liu, J.S.; Hsu, S.K.; Hsu, W.H.; Shih, C.H.; Hwang, J.K.; Wang, W.C.
Structure-stability-activity relationship in covalently cross-linked N-carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase
J. Mol. Biol.
359
741-753
2006
Agrobacterium tumefaciens
brenda
Nozaki, H.; Kira, I.; Watanabe, K.; Yokozeki, K.
Purification and properties of D-hydantoin hydrolase and N-carbamoyl-D-amino acid amidohydrolase from Flavobacterium sp. AJ11199 and Pasteurella sp. AJ11221
J. Mol. Catal. B
32
205-211
2005
Flavobacterium sp., Pasteurella sp., Pasteurella sp. AJ11221, Flavobacterium sp. AJ11199
-
brenda
Nozaki, H.; Takenaka, Y.; Kira, I.; Watanabe, K.; Yokozeki, K.
D-Amino acid production by E. coli co-expressed three genes encoding hydantoin racemase, D-hydantoinase and N-carbamoyl-D-amino acid amidohydrolase
J. Mol. Catal. B
32
213-218
2005
Escherichia coli
-
brenda
Park, H.; Oh, K.; Kim, H.
Improving the functional expression of N-carbamoylase by directed evolution using the green fluorescent protein fusion reporter system
Methods Enzymol.
388
187-195
2004
Agrobacterium tumefaciens, Agrobacterium tumefaciens NRRL B11291
brenda
Chen, H.; Lin, K.; Lu, C.
Refolding and activation of recombinant N-carbamoyl-D-amino acid amidohydrolase from Escherichia coli inclusion bodies
Process Biochem.
40
2135-2141
2005
Agrobacterium tumefaciens
-
brenda
Jiang, S.; Li, C.; Zhang, W.; Cai, Y.; Yang, Y.; Yang, S.; Jiang, W.
Directed evolution and structural analysis of N-carbamoyl-D-amino acid amidohydrolase provide insights into recombinant protein solubility in Escherichia coli
Biochem. J.
402
429-437
2007
Ralstonia pickettii
brenda
Yu, H.; Li, J.; Zhang, D.; Yang, Y.; Jiang, W.; Yang, S.
Improving the thermostability of N-carbamyl-D-amino acid amidohydrolase by error-prone PCR
Appl. Microbiol. Biotechnol.
82
279-285
2009
Ralstonia pickettii
brenda
Chiang, C.J.; Chern, J.T.; Wang, J.Y.; Chao, Y.P.
Facile immobilization of evolved agrobacterium radiobacter carbamoylase with high thermal and oxidative stability
J. Agric. Food Chem.
56
6348-6354
2008
Agrobacterium tumefaciens
brenda
Zhang, D.; Zhu, F.; Fan, W.; Tao, R.; Yu, H.; Yang, Y.; Jiang, W.; Yang, S.
Gradually accumulating beneficial mutations to improve the thermostability of N-carbamoyl-D-amino acid amidohydrolase by step-wise evolution
Appl. Microbiol. Biotechnol.
90
1361-1371
2011
Ralstonia pickettii, Ralstonia pickettii CGMCC1596
brenda
Liu, Y.; Xu, G.; Han, R.; Dong, J.; Ni, Y.
Identification of D-carbamoylase for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity
Biores. Technol.
249
720-728
2018
Arthrobacter crystallopoietes (Q84FR7), Arthrobacter crystallopoietes, Arthrobacter crystallopoietes CGMCC1.1926 (Q84FR7)
brenda
Bellini, R.G.; Coronado, M.A.; Paschoal, A.R.; Gaudencio do Rego, T.; Hungria, M.; Ribeiro de Vasconcelos, A.T.; Nicolas, M.F.
Structural analysis of a novel N-carbamoyl-D-amino acid amidohydrolase from a Brazilian Bradyrhizobium japonicum strain in silico insights by molecular modelling, docking and molecular dynamics
J. Mol. Graph. Model.
86
35-42
2019
Bradyrhizobium japonicum (A0A023XI92), Bradyrhizobium japonicum, Bradyrhizobium japonicum CPAC 15 (A0A023XI92), Bradyrhizobium japonicum SEMIA 5079 (A0A023XI92)
brenda