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1-methylhydantoin + H2O
3-methylhydantoic acid
2-chlorobenzenehydantoin + H2O
?
2-imidazolidone + H2O
?
-
-
-
-
?
2-thiohydantoin + H2O
?
-
-
-
-
?
3-(4-nitrophenyl)-3-ureidopropanoic acid + H2O
?
3-ethylphenylhydantoin + H2O
2-phenylhydantoic acid
-
-
-
?
3-methylphenylhydantoin + H2O
2-phenylhydantoic acid
-
-
-
?
3-phenylhydantoin + H2O
2-phenylhydantoic acid
-
-
-
?
4-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
5,5-dimethylhydantoin + H2O
?
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
5,6-dihydrothymine + H2O
3-(carbamoylamino)-2-methylpropanoic acid
5,6-dihydrothymine + H2O
?
5,6-dihydrothymine + H2O
N-carbamyl-beta-aminoisobutyrate
5,6-dihydrouracil + H2O
3-ureidopropanoate
5,6-dihydrouracil + H2O
3-ureidopropionate
5,6-dihydrouracil + H2O
?
5,6-dihydrouracil + H2O
N-carbamoyl-beta-alanine
5,6-dihydrouracil + H2O
N-carbamyl-beta-alanine
5-(2-thienyl)-DL-hydantoin + H2O
N-carbamoyl-D-2-thienylglycine
-
-
-
-
?
5-(4-hydroxyphenyl) hydantoin + H2O
N-carbamoyl-D-4-hydroxyphenylglycine
5-(4-hydroxyphenyl)hydantoin + H2O
5-(4-hydroxyphenyl)-D-carbamoylate
-
-
-
-
?
5-(p-hydroxybenzyl)hydantoin + H2O
?
5-bromo-5,6-dihydrouracil + H2O
?
5-fluoro-5,6-dihydrouracil + H2O
?
5-fluorouracil + H2O
2-fluoro-3-ureidopropionic acid
5-fluorouracil + hydantoin
2-fluoro-3-ureidopropionic acid + ?
5-hydroxymethylhydantoin + H2O
?
-
-
-
-
?
5-iodo-5,6-dihydrouracil + H2O
?
-
-
-
-
?
5-leucinyl-hydantoin + H2O
?
5-phenylhydantoin + 2 H2O
D-phenylglycine + CO2 + NH3
-
-
-
-
?
5-phenylhydantoin + H2O
5-phenyl D-carbamoylate
-
-
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
6-(4-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione + H2O
?
alpha-phenylsuccinimide + H2O
2-phenylsuccinamic acid
beta-ureidoisobutyrate
dihydrothymine + H2O
-
-
-
-
r
carbamoyl beta-aminoisobutyric acid + H2O
?
D,L-benzylhydantoin + H2O
?
D-2-phenylhydantoic acid + H2O
5-phenylhydantoin
-
reverse reaction stereospecific, only D-isomer acts as substrate
-
-
r
D-5(p-hydroxybenzyl)-hydantoin + H2O
N-carbamoyl-D-tyrosine
-
-
-
-
?
D-5-(1-methylpropyl)hydantoin + H2O
N-carbamoyl-D-isoleucine
-
-
-
?
D-5-(2-methylthioethyl)hydantoin + H2O
N-carbamoyl-D-methionine
D-5-benzylhydantoin + H2O
N-carbamoyl-D-phenylalanine
D-5-butylhydantoin + H2O
?
-
-
-
-
?
D-5-ethylhydantoin + H2O
?
D-5-isobutylhydantoin + H2O
?
-
-
-
-
?
D-5-isobutylhydantoin + H2O
N-carbamoyl-D-leucine
D-5-isopropylhydantoin + H2O
?
-
-
-
-
?
D-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
D-5-methyl-thio-ethylhydantoin + H2O
?
-
-
-
-
?
D-5-methylhydantoin + H2O
N-carbamoyl-D-alanine
D-5-methylthioethylhydantoin + H2O
?
D-5-propylhydantoin + H2O
?
-
-
-
-
?
D-benzylhydantoin
D-N-carbamoylphenylalanine
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
D-methylhydantoin + H2O
?
dihydroorotic acid + H2O
?
-
-
-
-
?
dihydropyrimidine + H2O
N-carbamoyl amino acid
dihydrothymidine + H2O
?
-
-
-
-
?
dihydrothymine + H2O
N-carbamoyl-beta-aminoisobutyric acid
-
-
-
-
?
dihydrouracil + H2O
3-ureidopropionate
dihydrouracil + H2O
N-carbamoyl-beta-alanine
-
-
-
-
?
dihydrouracil + H2O
ureidopropionate
dimethylhydantoin + H2O
?
1.4% of the activity with dihydrouracil
-
-
?
DL-4-hydroxyphenylhydantoin + H2O
D-carbamoyl-4-hydroxyphenylglycine
-
-
-
-
?
DL-5(2-(methylthio)-ethyl)hydantoin + H2O
?
DL-5-(2-carboxyethyl)hydantoin + H2O
L-glutamic acid
-
-
exclusively L-form
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
DL-5-benzylhydantoin + H2O
?
DL-5-butylhydantoin
?
-
-
-
-
?
DL-5-carboxyethylhydantoin + H2O
?
-
-
-
-
?
DL-5-cyanoethylhydantoin + H2O
?
-
-
-
-
?
DL-5-indolylmethylhydantoin + H2O
L-tryptophan
DL-5-isobutyl-hydantoin + H2O
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
DL-5-methyldihydrouracil + H2O
?
-
-
-
-
?
DL-5-p-hydroxyphenylhydantoin + H2O
D-p-hydroxyphenylglycine
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
DL-5-propylhydantoin
?
-
-
-
-
?
DL-5-sec-butylhydantoin + H2O
?
DL-5-thienylmethylhydantoin + H2O
?
-
-
-
-
?
DL-6-(4-chlorophenyl)-5,6-dihydrouracil + H2O
4-chloro-N-carbamoyl-beta-phenylalanine
DL-6-isopropyldihydrouracil + H2O
?
-
-
-
-
?
DL-6-methyldihydrouracil + H2O
?
-
-
-
-
?
DL-6-phenyl-5,6-dihydrouracil + H2O
N-rac-carbamoyl-beta-phenylalanine
DL-fluorobromylhydantoin + H2O
?
-
-
-
-
?
DL-homophenylalanylhydantoin + H2O
?
DL-hydroxymethylhydantoin + H2O
?
DL-hydroxyphenylhydantoin + H2O
?
DL-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
DL-isoproylhydantoin + H2O
N-carbamoyl-D-valine
DL-methylthioethylhydantoin + H2O
?
-
D-selective for the hydrolysis
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-p-hydroxyphenylglycine
7.2% of the activity with dihydrouracil
-
-
?
DL-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
hydantoin + H2O
hydantoic acid
hydantoin + H2O
N-carbamoyl glycine
hydantoin + H2O
N-carbamoylglycine
hydantoin + H2O
ureidoacetic acid
-
-
-
-
?
hydrothymine
carbamoyl beta-aminoisobutyric acid
-
-
-
?
hydrouracil + H2O
N-carbamoyl beta-alanine
-
-
-
?
indolmethylhydantoin + H2O
tryptophan
-
-
-
?
isobutylhydantoin + H2O
N-carbamoyl-D-alpha-isoleucine
isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
?
L-5-(1-methylpropyl)hydantoin + H2O
N-carbamoyl-L-isoleucine
-
-
-
?
L-5-(2-methylthioethyl)hydantoin + H2O
N-carbamoyl-L-methionine
L-5-benzylhydantoin + H2O
N-carbamoyl-L-phenylalanine
-
-
-
?
L-5-ethylhydantoin + H2O
?
L-5-isobutylhydantoin + H2O
N-carbamoyl-L-leucine
L-5-methylhydantoin + H2O
N-carbamoyl-L-alanine
-
-
-
?
L-5-methylthioethylhydantoin + H2O
?
L-benzylhydantoin
L-N-carbamoylphenylalanine
m-chlorophenylhydantoin + H2O
?
N-carbamoyl beta-alanine + H2O
5,6-dihydrouracil
N-carbamoyl-beta-alanine + H2O
?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + ?
-
N-carbamoyl-D-tryptophan is no substrate
-
-
?
p-chlorophenylhydantoin + H2O
?
p-methoxyphenylhydantoin + H2O
?
-
-
-
-
?
p-methylphenylhydantoin + H2O
?
-
-
-
-
?
phenylmethylhydantoin + H2O
phenylhydantoic acid
-
-
-
?
rac-5-p-fluorophenylhydantoin + H2O
?
-
immobilized enzyme (linked to aminopropyl glass beads) converts 100%
-
-
?
rac-5-p-trifluoromethylphenylhydantoin + H2O
?
-
immobilized enzyme (linked to aminopropyl glass beads) converts 87%
-
-
?
rac-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
immobilized enzyme (linked to aminopropyl glass beads) converts 100%
-
-
?
thymine + H2O
?
-
-
-
-
?
uric acid + H2O
?
-
-
-
-
?
additional information
?
-
1-methylhydantoin + H2O
3-methylhydantoic acid
-
-
-
?
1-methylhydantoin + H2O
3-methylhydantoic acid
-
-
-
-
?
1-methylhydantoin + H2O
3-methylhydantoic acid
-
poor substrate
-
-
?
2-chlorobenzenehydantoin + H2O
?
-
-
-
?
2-chlorobenzenehydantoin + H2O
?
-
-
-
?
2-thiouracil + H2O
?
-
-
-
-
?
2-thiouracil + H2O
?
-
-
-
-
?
3-(4-nitrophenyl)-3-ureidopropanoic acid + H2O
?
NCarbpNO2betaPhe, chemically synthesized artificial substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer
-
-
?
3-(4-nitrophenyl)-3-ureidopropanoic acid + H2O
?
NCarbpNO2betaPhe, chemically synthesized artificial substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer
-
-
?
4-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
?
4-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
r
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
r
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
r
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
Streptomyces mitakaensis
-
-
-
-
?
5,6-dihydropyrimidine + H2O
beta-ureido acid
-
-
-
-
?
5,6-dihydrothymine + H2O
3-(carbamoylamino)-2-methylpropanoic acid
-
-
-
?
5,6-dihydrothymine + H2O
3-(carbamoylamino)-2-methylpropanoic acid
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
r
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
r
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
?
5,6-dihydrothymine + H2O
?
-
-
-
-
?
5,6-dihydrothymine + H2O
N-carbamyl-beta-aminoisobutyrate
-
-
-
-
?
5,6-dihydrothymine + H2O
N-carbamyl-beta-aminoisobutyrate
-
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
26% relative enzyme activity
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
26% relative enzyme activity
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropanoate
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
purified preparation demonstrates no activity on this substrate
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
purified preparation demonstrates no activity on this substrate
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
172058, 209278, 209282, 209283, 209284, 209286, 209287, 209293, 209294, 209298, 209299, 209301, 685395 -
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
Peptococcus anaerobius
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
209273, 209274, 209275, 209279, 209280, 209281, 209283, 209289, 209290, 209293, 209294, 209298, 209299, 209301, 209303, 687942 -
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
Streptomyces mitakaensis
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
r
5,6-dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
5,6-dihydrouracil + H2O
?
highest activity of the EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
5,6-dihydrouracil + H2O
?
highest activity of the EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
5,6-dihydrouracil + H2O
?
2.35fold elevated hydantoinase activity in uninduced mutant cells compared with the wild type, but equivalent enzyme activity in induced mutant and wild type cells
-
-
?
5,6-dihydrouracil + H2O
?
2.35fold elevated hydantoinase activity in uninduced mutant cells compared with the wild type, but equivalent enzyme activity in induced mutant and wild type cells
-
-
?
5,6-dihydrouracil + H2O
N-carbamoyl-beta-alanine
-
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamoyl-beta-alanine
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamoyl-beta-alanine
-
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamoyl-beta-alanine
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamoyl-beta-alanine
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamoyl-beta-alanine
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamyl-beta-alanine
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamyl-beta-alanine
-
-
-
-
?
5,6-dihydrouracil + H2O
N-carbamyl-beta-alanine
-
-
-
?
5-(4-hydroxyphenyl) hydantoin + H2O
N-carbamoyl-D-4-hydroxyphenylglycine
-
-
-
?
5-(4-hydroxyphenyl) hydantoin + H2O
N-carbamoyl-D-4-hydroxyphenylglycine
-
-
-
?
5-(p-hydroxybenzyl)hydantoin + H2O
?
-
-
-
-
?
5-(p-hydroxybenzyl)hydantoin + H2O
?
-
-
-
-
?
5-bromo-5,6-dihydrouracil + H2O
?
-
-
-
-
?
5-bromo-5,6-dihydrouracil + H2O
?
-
-
-
-
r
5-bromo-5,6-dihydrouracil + H2O
?
-
-
-
-
?
5-bromo-5,6-dihydrouracil + H2O
?
-
-
-
-
r
5-fluoro-5,6-dihydrouracil + H2O
?
-
-
-
-
?
5-fluoro-5,6-dihydrouracil + H2O
?
-
less effective substrate
-
-
?
5-fluorouracil + H2O
2-fluoro-3-ureidopropionic acid
growth of GMP1 and GMP2 mutants but not of wild-type RU-KM3S, mutants independent of inducer
-
-
?
5-fluorouracil + H2O
2-fluoro-3-ureidopropionic acid
growth of GMP1 and GMP2 mutants but not of wild-type RU-KM3S, mutants independent of inducer
-
-
?
5-fluorouracil + hydantoin
2-fluoro-3-ureidopropionic acid + ?
growth of GMP1 and GMP2 mutants and wild-type RU-KM3S
-
-
?
5-fluorouracil + hydantoin
2-fluoro-3-ureidopropionic acid + ?
growth of GMP1 and GMP2 mutants and wild-type RU-KM3S
-
-
?
5-leucinyl-hydantoin + H2O
?
-
-
-
-
?
5-leucinyl-hydantoin + H2O
?
-
-
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
5-propylhydantoin + H2O
N-carbamoyl-D-valine
low activity
-
-
?
6-(4-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione + H2O
?
pNO2PheDU, chemically synthesized artificial substrate. Recombinant Escherichia coli cells expressing the hydantoinase show degradation of the substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer
-
-
?
6-(4-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione + H2O
?
pNO2PheDU, chemically synthesized artificial substrate. Recombinant Escherichia coli cells expressing the hydantoinase show degradation of the substrate. Enantioselective reactivity, preference of the hydantoinase for the (S)-enantiomer
-
-
?
6-azauracil + H2O
?
-
-
-
-
?
6-azauracil + H2O
?
-
-
-
-
?
allantoin + H2O
?
-
-
-
-
?
allantoin + H2O
?
-
-
-
-
?
allantoin + H2O
?
-
-
-
-
?
alpha-phenylsuccinimide + H2O
2-phenylsuccinamic acid
-
-
-
-
?
alpha-phenylsuccinimide + H2O
2-phenylsuccinamic acid
-
-
-
-
?
carbamoyl beta-aminoisobutyric acid + H2O
?
-
-
-
-
?
carbamoyl beta-aminoisobutyric acid + H2O
?
-
-
-
-
?
D,L-benzylhydantoin + H2O
?
-
-
-
-
?
D,L-benzylhydantoin + H2O
?
-
-
-
-
?
D-5-(2-methylthioethyl)hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
D-5-(2-methylthioethyl)hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
?
D-5-(2-methylthioethyl)hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
D-5-benzylhydantoin + H2O
N-carbamoyl-D-phenylalanine
-
-
-
?
D-5-benzylhydantoin + H2O
N-carbamoyl-D-phenylalanine
-
-
-
-
?
D-5-ethylhydantoin + H2O
?
-
-
-
-
r
D-5-ethylhydantoin + H2O
?
-
-
-
-
r
D-5-ethylhydantoin + H2O
?
-
-
-
-
?
D-5-isobutylhydantoin + H2O
N-carbamoyl-D-leucine
-
-
-
?
D-5-isobutylhydantoin + H2O
N-carbamoyl-D-leucine
-
-
-
?
D-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
?
D-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
?
D-5-methylhydantoin + H2O
N-carbamoyl-D-alanine
-
-
-
-
?
D-5-methylhydantoin + H2O
N-carbamoyl-D-alanine
-
-
-
?
D-5-methylhydantoin + H2O
N-carbamoyl-D-alanine
-
-
-
?
D-5-methylhydantoin + H2O
N-carbamoyl-D-alanine
-
L-5-methylhydantoin is no substrate
-
-
?
D-5-methylhydantoin + H2O
N-carbamoyl-D-alanine
-
-
-
-
?
D-5-methylthioethylhydantoin + H2O
?
-
-
-
-
r
D-5-methylthioethylhydantoin + H2O
?
-
-
-
-
r
D-benzylhydantoin
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-benzylhydantoin + H2O
D-N-carbamoylphenylalanine
-
-
-
-
?
D-methylhydantoin + H2O
?
1.57fold elevated hydantoinase activity in uninduced mutant cells compared with the wild type, but equivalent enzyme activity in induced mutant and wild type cells
-
-
?
D-methylhydantoin + H2O
?
1.57fold elevated hydantoinase activity in uninduced mutant cells compared with the wild type, but equivalent enzyme activity in induced mutant and wild type cells
-
-
?
dihydropyrimidine + H2O
N-carbamoyl amino acid
-
-
-
-
r
dihydropyrimidine + H2O
N-carbamoyl amino acid
-
-
-
-
?
dihydropyrimidine + H2O
N-carbamoyl amino acid
-
-
-
-
r
dihydropyrimidine + H2O
N-carbamoyl amino acid
-
-
-
-
r
dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
dihydrouracil + H2O
3-ureidopropionate
-
-
-
-
?
dihydrouracil + H2O
ureidopropionate
-
-
-
-
?
dihydrouracil + H2O
ureidopropionate
-
-
-
-
?
dihydrouracil + H2O
ureidopropionate
-
-
-
-
?
DL-5(2-(methylthio)-ethyl)hydantoin + H2O
?
EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
DL-5(2-(methylthio)-ethyl)hydantoin + H2O
?
EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
strictly D-selective
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
the enzyme exhibits strict D-enantioselectivity for DL-5-(2-methylthioethyl)-hydantoin
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
the enzyme exhibits strict D-enantioselectivity for DL-5-(2-methylthioethyl)-hydantoin
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
steric configuration D
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
-
-
-
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O
N-carbamoyl-D-methionine
Streptomyces mitakaensis
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
produces stereospecifically D-p-hydroxyphenylglycine
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
?
DL-5-(p-hydroxyphenyl)hydantoin + H2O
N-carbamoyl-p-hydroxyphenylglycine
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
only slight activity
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-benzylhydantoin + H2O
?
-
poorly hydrolyzed
-
-
?
DL-5-benzylhydantoin + H2O
?
-
-
-
-
?
DL-5-indolylmethylhydantoin + H2O
L-tryptophan
-
strictly D-selective
-
-
?
DL-5-indolylmethylhydantoin + H2O
L-tryptophan
-
-
-
-
?
DL-5-indolylmethylhydantoin + H2O
L-tryptophan
-
-
-
-
?
DL-5-indolylmethylhydantoin + H2O
L-tryptophan
-
strictly L-selective for the cleavage
-
-
?
DL-5-indolylmethylhydantoin + H2O
L-tryptophan
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isobutyl-hydantoin + H2O
?
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
only D-isomer hydrolyzed
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
only D-isomer hydrolyzed
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
?
DL-5-isopropylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
?
DL-5-methylhydantoin
?
-
-
-
-
?
DL-5-methylhydantoin
?
-
-
-
-
?
DL-5-methylhydantoin
?
-
-
-
-
?
DL-5-methylhydantoin
?
-
-
-
-
?
DL-5-p-hydroxyphenylhydantoin + H2O
D-p-hydroxyphenylglycine
-
hydantoinase and carbamylase involved
-
-
?
DL-5-p-hydroxyphenylhydantoin + H2O
D-p-hydroxyphenylglycine
-
hydantoinase and carbamylase involved
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
45% of the activity with dihydrouracil
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
r
DL-5-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
r
DL-5-sec-butylhydantoin + H2O
?
-
-
-
-
?
DL-5-sec-butylhydantoin + H2O
?
-
-
-
-
?
DL-5-sec-butylhydantoin + H2O
?
-
-
-
-
?
DL-5-sec-butylhydantoin + H2O
?
-
-
-
-
?
DL-5-sec-butylhydantoin + H2O
?
-
-
-
-
?
DL-6-(4-chlorophenyl)-5,6-dihydrouracil + H2O
4-chloro-N-carbamoyl-beta-phenylalanine
-
-
-
-
?
DL-6-(4-chlorophenyl)-5,6-dihydrouracil + H2O
4-chloro-N-carbamoyl-beta-phenylalanine
-
-
-
-
?
DL-6-(4-chlorophenyl)-5,6-dihydrouracil + H2O
4-chloro-N-carbamoyl-beta-phenylalanine
-
-
-
-
?
DL-6-(4-chlorophenyl)-5,6-dihydrouracil + H2O
4-chloro-N-carbamoyl-beta-phenylalanine
-
-
-
-
?
DL-6-(4-chlorophenyl)-5,6-dihydrouracil + H2O
4-chloro-N-carbamoyl-beta-phenylalanine
-
-
-
-
?
DL-6-(4-chlorophenyl)-5,6-dihydrouracil + H2O
4-chloro-N-carbamoyl-beta-phenylalanine
-
-
-
-
?
DL-6-phenyl-5,6-dihydrouracil + H2O
N-rac-carbamoyl-beta-phenylalanine
-
-
27% conversion. Enzyme preferably hydrolyzes L-Phe-5,6-dihydrouracil to L-N-carbamoyl-beta-phenylalanine, 61% enantiomeric excess of L-enantiomer
-
?
DL-6-phenyl-5,6-dihydrouracil + H2O
N-rac-carbamoyl-beta-phenylalanine
-
-
27% conversion. Enzyme preferably hydrolyzes L-Phe-5,6-dihydrouracil to L-N-carbamoyl-beta-phenylalanine, 61% enantiomeric excess of L-enantiomer
-
?
DL-6-phenyl-5,6-dihydrouracil + H2O
N-rac-carbamoyl-beta-phenylalanine
-
-
enzyme does not display a significant entantioselectivity
-
?
DL-6-phenyl-5,6-dihydrouracil + H2O
N-rac-carbamoyl-beta-phenylalanine
-
-
enzyme does not display a significant entantioselectivity
-
?
DL-6-phenyl-5,6-dihydrouracil + H2O
N-rac-carbamoyl-beta-phenylalanine
-
-
enzyme does not display a significant entantioselectivity
-
?
DL-6-phenyl-5,6-dihydrouracil + H2O
N-rac-carbamoyl-beta-phenylalanine
-
-
enzyme does not display a significant entantioselectivity
-
?
DL-homophenylalanylhydantoin + H2O
?
-
the enzyme exhibits non-enantiospecificity for DL-homophenylalanylhydantoin
-
-
?
DL-homophenylalanylhydantoin + H2O
?
-
the enzyme exhibits non-enantiospecificity for DL-homophenylalanylhydantoin
-
-
?
DL-hydroxymethylhydantoin + H2O
?
-
-
-
-
?
DL-hydroxymethylhydantoin + H2O
?
-
-
-
-
?
DL-hydroxyphenylhydantoin + H2O
?
-
-
-
-
?
DL-hydroxyphenylhydantoin + H2O
?
-
-
-
-
?
DL-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
-
?
DL-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
-
?
DL-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
-
?
DL-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
-
?
DL-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
-
?
DL-isoproylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-isoproylhydantoin + H2O
N-carbamoyl-D-valine
-
-
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
?
EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
?
EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
19% relative enzyme activity
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
19% relative enzyme activity
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
the enzyme exhibits strict D-enantioselectivity for DL-p-hydroxyphenylhydantoin
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
the enzyme exhibits strict D-enantioselectivity for DL-p-hydroxyphenylhydantoin
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
?
DL-p-hydroxyphenylhydantoin + H2O
N-carbamoyl-D-hydroxyphenylglycine
-
-
-
?
DL-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
39.9% relative enzyme activity
-
-
?
DL-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
39.9% relative enzyme activity
-
-
?
DL-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
DL-phenylhydantoin + H2O
N-carbamoyl-D-phenylglycine
-
-
-
-
?
glutarimide + H2O
?
-
-
-
-
?
glutarimide + H2O
?
-
-
-
-
?
glutarimide + H2O
?
-
-
-
-
?
hydantoin + H2O
?
lowest activity of the EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
hydantoin + H2O
?
lowest activity of the EDTA-dialyzed/Co2+-substituted enzyme
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
r
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
18.7% of the activity with dihydrouracil
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
Peptococcus anaerobius
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
poorly hydrolyzed
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
hydantoic acid
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
preferred substrate, 100% relative enzyme activity
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
preferred substrate, 100% relative enzyme activity
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
172058, 209272, 209276, 209278, 209282, 209283, 209284, 209287, 209291, 209293, 209294, 209298, 209299, 209301 -
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
ir
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
r
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
Peptococcus anaerobius
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
209273, 209274, 209275, 209279, 209280, 209281, 209283, 209289, 209290, 209293, 209294, 209297, 209298, 209299, 209301, 209302, 209303, 684522 -
-
?
hydantoin + H2O
N-carbamoyl glycine
4fold elevated hydantoinase activity in uninduced mutant cells compared with the wild type, but equivalent enzyme activity in induced mutant and wild type cells
-
-
?
hydantoin + H2O
N-carbamoyl glycine
4fold elevated hydantoinase activity in uninduced mutant cells compared with the wild type, but equivalent enzyme activity in induced mutant and wild type cells
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
r
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
Streptomyces mitakaensis
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoyl glycine
-
-
-
-
?
hydantoin + H2O
N-carbamoylglycine
-
-
-
-
?
hydantoin + H2O
N-carbamoylglycine
-
-
-
?
hydantoin + H2O
N-carbamoylglycine
-
-
-
-
?
hydantoin + H2O
N-carbamoylglycine
-
-
-
-
?
hydantoin + H2O
N-carbamoylglycine
-
-
-
?
isobutylhydantoin + H2O
N-carbamoyl-D-alpha-isoleucine
-
-
-
?
isobutylhydantoin + H2O
N-carbamoyl-D-alpha-isoleucine
98.7 % enantiomeric excess (ee), isolation yield of 78.3%, and substrate to biocatalyst ratio of 15.6 in recombinant Escherichia coli
-
-
?
isobutylhydantoin + H2O
N-carbamoyl-D-alpha-isoleucine
-
-
-
?
isobutylhydantoin + H2O
N-carbamoyl-D-alpha-isoleucine
98.7 % enantiomeric excess (ee), isolation yield of 78.3%, and substrate to biocatalyst ratio of 15.6 in recombinant Escherichia coli
-
-
?
L-5-(2-methylthioethyl)hydantoin + H2O
N-carbamoyl-L-methionine
-
-
-
?
L-5-(2-methylthioethyl)hydantoin + H2O
N-carbamoyl-L-methionine
-
-
-
?
L-5-ethylhydantoin + H2O
?
-
-
-
-
r
L-5-ethylhydantoin + H2O
?
-
-
-
-
r
L-5-isobutylhydantoin + H2O
N-carbamoyl-L-leucine
-
-
-
?
L-5-isobutylhydantoin + H2O
N-carbamoyl-L-leucine
-
-
-
?
L-5-methylthioethylhydantoin + H2O
?
-
-
-
-
r
L-5-methylthioethylhydantoin + H2O
?
-
-
-
-
r
L-benzylhydantoin
L-N-carbamoylphenylalanine
-
-
-
-
?
L-benzylhydantoin
L-N-carbamoylphenylalanine
-
-
-
-
?
m-chlorophenylhydantoin + H2O
?
-
-
-
-
?
m-chlorophenylhydantoin + H2O
?
-
-
-
-
?
m-chlorophenylhydantoin + H2O
?
-
-
-
-
?
N-carbamoyl beta-alanine + H2O
5,6-dihydrouracil
-
-
-
-
r
N-carbamoyl beta-alanine + H2O
5,6-dihydrouracil
-
-
-
-
r
N-carbamoyl beta-alanine + H2O
5,6-dihydrouracil
-
-
-
-
r
N-carbamoyl-beta-alanine + H2O
?
-
-
-
?
N-carbamoyl-beta-alanine + H2O
?
-
-
-
?
p-chlorophenylhydantoin + H2O
?
-
-
-
-
?
p-chlorophenylhydantoin + H2O
?
-
-
-
-
?
p-chlorophenylhydantoin + H2O
?
-
-
-
-
?
phthalimide + H2O
?
-
low activity
-
-
?
phthalimide + H2O
?
-
low activity
-
-
?
phthalimide + H2O
?
-
-
-
?
phthalimide + H2O
?
-
-
-
?
phthalimide + H2O
?
-
-
-
?
phthalimide + H2O
?
-
-
-
?
phthalimide + H2O
?
-
-
-
?
phthalimide + H2O
?
-
-
-
?
phthalimide + H2O
?
-
-
-
?
phthalimide + H2O
?
-
-
-
?
succinimide + H2O
?
-
-
-
-
?
succinimide + H2O
?
-
-
-
-
r
succinimide + H2O
?
-
-
-
-
?
uracil + H2O
?
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
disubstituted hydantoins or 1-substituted hydantoins are no substrates
-
-
?
additional information
?
-
-
disubstituted hydantoins or 1-substituted hydantoins are no substrates
-
-
?
additional information
?
-
the enzyme shows activity with 6-monosubstituted dihydrouracils. The enzyme shows enantioselectivity
-
-
-
additional information
?
-
the enzyme shows activity with 6-monosubstituted dihydrouracils. The enzyme shows enantioselectivity
-
-
-
additional information
?
-
-
DL-hydroxymethylhydantoin and 5,5-disubstituted hydantoin derivatives are no substrates
-
-
?
additional information
?
-
-
DL-hydroxymethylhydantoin and 5,5-disubstituted hydantoin derivatives are no substrates
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
L-dihydroorotic acid is no substrate
-
-
?
additional information
?
-
-
L-dihydroorotic acid is no substrate
-
-
?
additional information
?
-
-
inactive with carbamoyl beta-alanine amide, barbituric acid, imidazole 4,5-dicarboxylic acid, 5-(carboxymethylidine)hydantoin, orotic acid, 4,5-aminoimidazolecarboximide, urocanic acid and 5-(diphenyl)hydantoin
-
-
?
additional information
?
-
the Brevibacillus agri strain NCHU1002 can perform the ring opening reaction of D,L-5-monosubstituted hydantoins stereoselectively to N-carbamoyl-D-amino acids. No L-form amino acid are formed in the reaction, analysis via the chiral HPLC
-
-
?
additional information
?
-
the Brevibacillus agri strain NCHU1002 can perform the ring opening reaction of D,L-5-monosubstituted hydantoins stereoselectively to N-carbamoyl-D-amino acids. No L-form amino acid are formed in the reaction, analysis via the chiral HPLC
-
-
?
additional information
?
-
-
does not hydrolyze hydantoins
-
-
?
additional information
?
-
at 0 and 0.01 mM dietary 5-fluorouracil, CRMPsup mutants emerged in numbers similar to those of CRMP+ hemizygotes, survival of CRMPsup mutants was diminished at 0.03 mM 5-fluorouracil
-
-
?
additional information
?
-
at 0 and 0.01 mM dietary 5-fluorouracil, CRMPsup mutants emerged in numbers similar to those of CRMP+ hemizygotes, survival of CRMPsup mutants was diminished at 0.03 mM 5-fluorouracil
-
-
?
additional information
?
-
-
at 0 and 0.01 mM dietary 5-fluorouracil, CRMPsup mutants emerged in numbers similar to those of CRMP+ hemizygotes, survival of CRMPsup mutants was diminished at 0.03 mM 5-fluorouracil
-
-
?
additional information
?
-
at 0 and 0.01 mM dietary 5-fluorouracil, CRMPsup mutants emerged in numbers similar to those of CRMP+ hemizygotes, survival of CRMPsup mutants was diminished at 0.03 mM 5-fluorouracil
-
-
?
additional information
?
-
at 0 and 0.01 mM dietary 5-fluorouracil, CRMPsup mutants emerged in numbers similar to those of CRMP+ hemizygotes, survival of CRMPsup mutants was diminished at 0.03 mM 5-fluorouracil
-
-
?
additional information
?
-
no substrate: diphenylhydantoin, 5-(hydroxymethyl)uracil, benzylhydantoin, isopropylhydantoin
-
-
?
additional information
?
-
-
does not hydrolyze hydantoins
-
-
?
additional information
?
-
-
5,5-dimethylhydantoin is no substrate
-
-
?
additional information
?
-
-
DL-5-phenylhydantoin is no substrate
-
-
?
additional information
?
-
-
hydantoin, urea, allantoin and dihydroorotate are no substrates
-
-
?
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
additional information
?
-
the catalytic efficiency of the enzyme toward dihydrouracil is higher than that toward phthalimide (fourfold) and 5-propylhydantoin (100fold). Therefore, this bacterial enzyme is suitably identified as a dihydropyrimidinase, not a hydantoinase. Allantoin and dihydroorotate are no substrates
-
-
-
additional information
?
-
purified D-PfHYD prefers aliphatic to aromatic 5'-monosubstituted hydantoins. 5'-Monosubstituted hydantoins give N-carbamoyl-D-alpha-amino acids
-
-
-
additional information
?
-
-
purified D-PfHYD prefers aliphatic to aromatic 5'-monosubstituted hydantoins. 5'-Monosubstituted hydantoins give N-carbamoyl-D-alpha-amino acids
-
-
-
additional information
?
-
purified D-PfHYD prefers aliphatic to aromatic 5'-monosubstituted hydantoins. 5'-Monosubstituted hydantoins give N-carbamoyl-D-alpha-amino acids
-
-
-
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
hydantoins derived from alanine, valine, leucine, serine, phenylalanine and hydroxyphenylglycine are substrates, hydantoins derived from aspartic acid, lysine, and 5,5-disubstituted hydantoins are not hydrolyzed
-
-
?
additional information
?
-
no activity towards uracil and succinimide
-
-
?
additional information
?
-
-
catalyzes the hydrolysis of 5-monosubstituted hydantoin to enantionmeric N-carbamoyl-amino acids
-
-
?
additional information
?
-
-
catalyzes the hydrolysis of 5-monosubstituted hydantoin to enantionmeric N-carbamoyl-amino acids
-
-
?
additional information
?
-
no activity towards uracil and succinimide
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
diphenylhydantoin and 5,5-disubstituted hydantoins like 5-ethyl-5-phenylhydantoin, 5,5-diphenylhydantoin, D-3-methyl-5-phenylhydantoin, D-3-ethyl-5-phenylhydantoin, alpha-methyl-alpha-phenylsuccinimide, N-methyl-alpha-phenylsuccinimide and alpha-ethyl-alpha-phenylglutarimide are no substrates
-
-
?
additional information
?
-
-
succinimide, dihydro-L-orotic-2-acid, dihydrouridine and dihydrothymidine are no substrates
-
-
?
additional information
?
-
-
diphenylhydantoin and 5,5-disubstituted hydantoins like 5-ethyl-5-phenylhydantoin, 5,5-diphenylhydantoin, D-3-methyl-5-phenylhydantoin, D-3-ethyl-5-phenylhydantoin, alpha-methyl-alpha-phenylsuccinimide, N-methyl-alpha-phenylsuccinimide and alpha-ethyl-alpha-phenylglutarimide are no substrates
-
-
?
additional information
?
-
-
enzyme presents both hydantoinase and dihydropyrimidinase activities, with higher affinity for the natural six-membered ring substrates. For the five-membered ring substrates, affinity is greater for those with aliphatic and apolar groups in the 5th carbon atom, with the highest rates of hydrolysis for D-5-methyl and D-5-ethyl hydantoin. Enzyme is enantioselective for the D-isomer of monosubstituted 5-hydantoins. Activity with substrate analogues such as allantoin, 5,5-dimethylhydantoin, 5-benzyl,5-methyl-hydantoin, succinimide, rodamine or tiazoledione is not detected under the conditions assayed
-
-
?
additional information
?
-
-
one zinc ion is sufficient to stabilize Lys carbamylation in Tetraodon nigroviridis dihydropyrimidinase (DHPase)
-
-
-
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0.005
-
strain 30207, isopropylhydantoin as substrate
0.006
-
strain 30201, isopropylhydantoin as substrate
0.007
-
strain 30205, isopropylhydantoin as substrate
0.009
-
strain 30199, isopropylhydantoin as substrate
0.01
-
strain 50106, isopropylhydantoin as substrate
0.011
-
strain 2005, isopropylhydantoin as substrate
0.013
-
strain 30150, isopropylhydantoin as substrate
0.015
-
strain 50090, incubated with hydantoin, isopropylhydantoin as substrate
0.019
-
strain 50154, isopropylhydantoin as substrate
0.021
-
strain 30204, isopropylhydantoin as substrate
0.022
-
strain 2005, isopropylhydantoin as substrate
0.023
-
strain 30147, isopropylhydantoin as substrate
0.034
-
strain 291, isopropylhydantoin as substrate
0.038
-
strain 84, isopropylhydantoin as substrate
0.049
-
strain 549, isopropylhydantoin as substrate
0.051
-
strain 291, incubated with hydantoin, isopropylhydantoin as substrate
0.059
-
strain 11291, dihydrouracil as substrate
0.07
-
substrate D-benzylhydantoin
0.084
-
DL-5-p-hydroxyphenylhydantoin conversion
0.085
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-(1-methylpropyl)hydantoin
0.091
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-hydantoin-5-acetic acid
0.094
-
strain 11291, incubated with hydantoin
0.1
-
10 mM dihydrouracil as substrate
0.112
-
strain 30205, dihydrouracil as substrate
0.127
-
strain 549, incubated with hydantoin, isopropylhydantoin as substrate
0.128
-
strain 30150, dihydrouracil as substrate
0.15
-
strain 2005, dihydrouracil as substrate
0.17
EDTA-dialyzed/Co2+-substituted enzyme incubated with hydantoin as substrate
0.185
-
strain 84, incubated with hydantoin, isopropylhydantoin as substrate
0.19
-
strain 50154, dihydrouracil as substrate
0.193
-
strain 30204, dihydrouracil as substrate
0.194
-
strain 50090, dihydrouracil as substrate
0.212
-
strain 30147, dihydrouracil as substrate
0.216
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-methylhydantoin
0.225
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-hydroxymethylhydantoin
0.299
-
strain 30155, dihydrouracil as substrate
0.31
-
strain 50106, dihydrouracil as substrate
0.317
-
strain 30208, dihydrouracil as substrate
0.36
EDTA-dialyzed enzyme incubated with Fe2+ with DL-p-hydroxyphenylhydantoin as substrate
0.37
-
substrate L-benzylhydantoin
0.377
-
DL-5-p-hydroxyphenylhydantoin conversion induced by hydantoin
0.385
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-p-hydroxyphenylhydantoin
0.4
-
10 mM dihydrothymine as substrate
0.425
-
strain 30207, dihydrouracil as substrate
0.46
EDTA-dialyzed enzyme incubated with Ca2+ with DL-p-hydroxyphenylhydantoin as substrate
0.49
EDTA-dialyzed enzyme incubated with Ni2+ with DL-p-hydroxyphenylhydantoin as substrate
0.5
-
strain 291, dihydrouracil as substrate
0.52
EDTA-dialyzed enzyme with D,L-p-hydroxyphenylhydantoin as substrate
0.53
-
strain 50108, dihydrouracil as substrate
0.54
EDTA-dialyzed enzyme incubated with Mg2+ with DL-p-hydroxyphenylhydantoin as substrate
0.562
-
strain 30206, dihydrouracil as substrate
0.6
-
DL-methylhydantoin, 57 mM
0.635
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-phenylhydantoin
0.68
EDTA-dialyzed enzyme incubated with Cu2+ with DL-p-hydroxyphenylhydantoin as substrate
0.74
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Cd2+
0.78
-
dihydrouracil as substrate
0.81
-
strain 50154, incubated with hydantoin, dihydrouracil as substrate
0.826
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-phenylpropylhydantoin
0.89
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-methylthiethylhydantoin
0.91
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Ni2+
0.98
-
strain 50108, incubated with hydantoin, dihydrouracil as substrate
1.11
-
strain 50106, incubated with hydantoin, dihydrouracil as substrate
1.128
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-isobutylhydantoin
1.14
-
strain 30155, dihydrouracil as substrate
1.2
-
strain 549, dihydrouracil as substrate
1.286
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-benylhydantoin
1.4
-
strain 50090, incubated with hydantoin, dihydrouracil as substrate
1.44
-
DL-hydantoin as substrate
1.5
-
L-methylthioethylhydantoin, 2 mM
1.591
-
DL-5-p-hydroxyphenylhydantoin conversion induced by DL-5-(2-indolymethyl)hydantoin
1.67
-
DL-5-methylhydantoin as substrate
1.69
EDTA-dialyzed/Co2+-substituted enzyme incubated with DL-p-hydroxyphenylhydantoin as substrate
1.72
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Mn2+
1.9
-
strain 549, incubated with hydantoin, dihydrouracil as substrate
10.65
after 3.4fold purification, using DL-5-phenylhydantoin as a substrate, in 50 mM Tris-HCl buffer, pH 8.0
10.9
-
isopropylhydantoin as substrate
101.5
-
hydantoin as substrate
103.6
-
after 334fold purification, at 25°C and pH 7.5
11.84
after 3.4fold purification, using DL-p-hydroxyphenylhydantoin as a substrate, in 50 mM Tris-HCl buffer, pH 8.0
12
-
L-methylthioethylhydantoin, 20 mM
13
-
DL-5-indolylmethylhydantoin as substrate
14.3
crude extract, using DL-hydantoin as a substrate, in 50 mM Tris-HCl buffer, pH 8.0
2.25
-
incubated with hydantoin
2.38
EDTA-dialyzed enzyme incubated with Mn2+ with DL-p-hydroxyphenylhydantoin as substrate
2.9
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Zn2+
20.9
purified recombinant enzyme, pH 9.0, 45°C
216
-
DL-5-phenylhydantoin as substrate
236.9
-
phenylhydantoin as substrate
27.5
-
dihydrouracil as substrate
3.1
after 3.4fold purification
3.56
EDTA-dialyzed/Co2+-substituted enzyme incubated with dihydrouracil as substrate
3.6
EDTA-dialyzed enzyme incubated with Co2+ with DL-p-hydroxyphenylhydantoin as substrate
30
-
DL-methylthioethylhydantoin, 40 mM
37
-
D-methylthioethylhydantoin, 20 mM
48.5
after 3.4fold purification, using DL-hydantoin as a substrate, in 50 mM Tris-HCl buffer, pH 8.0
5.34
crude enzyme, pH 9.0, 45°C, substrate isobutylhydantoin
5.4
-
D-methylthioethylhydantoin, 2 mM
5.79
purified recombinant His-tagged enzyme, pH 8.0, 50°C
5.8 - 5.9
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Co2+
5.93
purified recombinant enzyme from Escherichia coli JM109pJAVI2
6.6
-
mutant P477, free enzyme
600.8
after 3.4fold purification, using 5,6-dihydrouracil as a substrate, in 50 mM Tris-HCl buffer, pH 8.0
613
-
mutant P475, free enzyme
70
-
L-5-indolylmethylhydantoin as substrate
76.6
-
DL-fluorobromylhydantoin as substrate
8.1
-
mutant P476, free enzyme
9.32
-
mutant P478, ifree enzyme
91.6
-
hydroxyphenylhydantoin as substrate
0.014
-
strain 50106, incubated with hydantoin, isopropylhydantoin as substrate
0.014
-
strain 50108, isopropylhydantoin as substrate
0.016
-
strain 11291, isopropylhydantoin as substrate
0.016
-
strain 50090, isopropylhydantoin as substrate
0.033
-
strain 30201, dihydrouracil as substrate
0.033
-
strain 50108, isopropylhydantoin as substrate
0.3
-
crude extract, at 25°C and pH 7.5
0.3
-
DL-phenylhydantoin, 50 mM
0.62
EDTA-dialyzed/Co2+-substituted enzyme incubated with DL-5(2-(methylthio)-ethyl)hydantoin as substrate
0.62
-
strain 2005, incubated with hydantoin, dihydrouracil as substrate
0.73
EDTA-dialyzed enzyme incubated with Zn2+ with DL-p-hydroxyphenylhydantoin as substrate
0.73
-
strain 549, incubated with hydantoin, dihydrouracil as substrate
0.82
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in absence of metal ion
0.82
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Ca2+
0.82
substrate 5,6-dihydrouracil, pH 8.0, 25°C, purified recombinant enzyme in presence of 1 mM Mg2+
10.75
-
purified wild type enzyme, at 37°C
10.75
-
mutant P479, free enzyme
8.41
-
purified mutant enzyme R479D, at 37°C
8.41
-
mutant R479D, free enzyme
additional information
hydantoinase in recombinant Escherichia coli cells has a specific activity of 0.326 mU/mgcdw with 6-(4-nitrophenyl)dihydropyrimidine-2,4(1H,3H)-dione
additional information
-
0.01 U/ml cells, mutant DELTA474-479
additional information
-
0.06 U/ml cells, mutant R479A
additional information
-
1.32 U/ml cells, mutant DELTA477-479
additional information
-
1.33 U/ml cells, mutant DELTA478-479
additional information
-
1.40 U/ml cells, mutant DELTA475-479
additional information
-
1.48 U/ml cells, mutant DELTA476-479
additional information
-
1.73 U/ml cells, mutant R479D
additional information
-
2.12 U/ml cells, mutant DELTA479
additional information
-
no activity in mutant P474, free enzyme
additional information
-
no activity in mutant R479A, free enzyme
additional information
-
only the last four residues can be deleted without significantly affecting the enzyme activity
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evolution
te enzyme belongs to the urease family
evolution
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
evolution
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
evolution
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
evolution
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
evolution
several hydrolases have been reported with hydantoin hydrolysis activity, including amidohydrolase, dihydropyrimidase/hydantoinase, allantoinase, and dihydroorotase, which belong to the cyclic amidase superfamily containing 22 potential subfamilies. According to the phylogenetic tree, D-PfHYD displays a close relationship to dihydropyrimidase/hydantoinase, whereas it is distinct from allantoinase (ALN, AllB, LhyD, and FeAllB) and dihydroorotase (PyrC, Ura4). Phylogenetic analysis and tree, overview
evolution
-
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
-
evolution
-
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
-
evolution
-
te enzyme belongs to the urease family
-
evolution
-
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
-
evolution
-
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
-
evolution
-
several hydrolases have been reported with hydantoin hydrolysis activity, including amidohydrolase, dihydropyrimidase/hydantoinase, allantoinase, and dihydroorotase, which belong to the cyclic amidase superfamily containing 22 potential subfamilies. According to the phylogenetic tree, D-PfHYD displays a close relationship to dihydropyrimidase/hydantoinase, whereas it is distinct from allantoinase (ALN, AllB, LhyD, and FeAllB) and dihydroorotase (PyrC, Ura4). Phylogenetic analysis and tree, overview
-
evolution
-
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
-
evolution
-
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
-
evolution
-
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
-
evolution
-
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
-
evolution
-
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
-
evolution
-
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
-
evolution
-
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
-
evolution
-
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
-
evolution
-
dihydropyrimidinase, a tetrameric metalloenzyme, is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase (DHPase) is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase (DHOase), hydantoinase, and imidase. Almost all of these zinc metalloenzymes possess a binuclear metal center in which two metal ions are bridged by a post-translational carbamylated Lys
-
evolution
-
enzyme dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase
-
evolution
-
dihydropyrimidinase is a member of the cyclic amidohydrolase family, which also includes allantoinase, dihydroorotase, hydantoinase, and imidase. These metalloenzymes possess very similar active sites and may use a similar mechanism for catalysis
-
metabolism
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
metabolism
-
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
-
metabolism
-
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
-
metabolism
-
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
-
metabolism
-
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
-
metabolism
-
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
-
metabolism
-
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
-
metabolism
-
dihydropyrimidinase is a key enzyme for pyrimidine catabolism, it catalyzes the reversible cyclization of dihydrouracil to N-carbamoyl-beta-alanine in the second step of the pyrimidine degradation pathway
-
physiological function
hydantoinase and L-carbamoylase are involved in the conversion of DL-5-substituted hydantoins to an N-carbamyl intermediate that is subsequently converted to L-alpha-amino acids
physiological function
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
physiological function
-
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
-
physiological function
-
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
-
physiological function
-
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
-
physiological function
-
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
-
physiological function
-
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
-
physiological function
-
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
-
physiological function
-
dihydropyrimidinase can detoxify xenobiotics with an imide functional group, ranging from linear imides to heterocyclic imides. Homologous enzymes from microorganisms are known as hydantoinase, used as biocatalyst for hydrolysis of 5-monosubstituted hydantoins in the synthesis of D- and L-amino acids
-
additional information
structure-activity relationship analysis
additional information
-
structure-activity relationship analysis
additional information
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
additional information
the catalytic residues are conserved in D-PfHYD, including His59, His61, Lys150, His183, His239, and Asp 316, which participate in the hydrolysis reaction by interaction with metal ions and hydantoin substrates through the carbamate group, amide nitrogen and carbonyl oxygen
additional information
-
the catalytic residues are conserved in D-PfHYD, including His59, His61, Lys150, His183, His239, and Asp 316, which participate in the hydrolysis reaction by interaction with metal ions and hydantoin substrates through the carbamate group, amide nitrogen and carbonyl oxygen
additional information
the enzyme contains a carboxylated lysine within the active site
additional information
-
the enzyme contains a carboxylated lysine within the active site
additional information
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
structure-activity relationship analysis
-
additional information
-
the enzyme contains a carboxylated lysine within the active site
-
additional information
-
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
structure-activity relationship analysis
-
additional information
-
the enzyme contains a carboxylated lysine within the active site
-
additional information
-
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
-
additional information
-
the catalytic residues are conserved in D-PfHYD, including His59, His61, Lys150, His183, His239, and Asp 316, which participate in the hydrolysis reaction by interaction with metal ions and hydantoin substrates through the carbamate group, amide nitrogen and carbonyl oxygen
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
structure-activity relationship analysis
-
additional information
-
the enzyme contains a carboxylated lysine within the active site
-
additional information
-
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
structure-activity relationship analysis
-
additional information
-
the enzyme contains a carboxylated lysine within the active site
-
additional information
-
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
structure-activity relationship analysis
-
additional information
-
the enzyme contains a carboxylated lysine within the active site
-
additional information
-
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
structure-activity relationship analysis
-
additional information
-
the enzyme contains a carboxylated lysine within the active site
-
additional information
-
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
structure-activity relationship analysis
-
additional information
-
the enzyme contains a carboxylated lysine within the active site
-
additional information
-
enzyme structure homology modeling, determination and analysis of active site residues of dihydropyrimidinase, overview
-
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oligomer
-
2 * 60000 + 2 * 62000 + 1 * 110000, room temperature, 2-mercaptoethanol, SDS-PAGE
dimer
-
-
dimer
-
2 * 54000, SDS-PAGE
dimer
-
2 * 51100, mass spectrometric analysis
dimer
-
2 * 54000, SDS-PAGE
-
dimer
-
2 * 51100, mass spectrometric analysis
-
dimer
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
-
in contrast to all dihydropyrimidinases, Pseudomonas aeruginosa dihydropyrimidinase forms a dimer, rather than a tetramer, both in the crystalline state and in the solution. Structural comparison of the C-terminal region and the dimer-dimer interface between Pseudomonas aeruginosa dihydropyrimidinase and Thermus sp. dihydropyrimidinase reveals that enzyme cannot be a tetramer, detailed overview
-
dimer
2 * 54000, SDS-PAGE
dimer
-
wild-type P479, determined by gel filtration
dimer
-
wild-type P479, determined by gel filtration
-
dimer
-
2 * 54000, SDS-PAGE
-
dimer
-
2 * 52000, reducing and nonreducing SDS-PAGE
dimer
-
2 * 52253, mass spectrometric analysis
dimer
-
2 * 50000, SDS-PAGE
dimer or tetramer
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
dimer or tetramer
-
pH-dependent oligomerization of dihydropyrimidinase. Unlike all known dihydropyrimidinases, which are tetrameric, pseudomonal dihydropyrimidinase forms a dimer at neutral pH 7.5. Gel filtration chromatographic analysis of purified dihydropyrimidinase reveals a mixture of dimers and tetramers at pH 5.9, with mainly tetramers
-
homodimer
2 * 52000, SDS-PAGE
homodimer
-
2 * 54000, SDS-PAGE
homodimer
-
2 * 54000, SDS-PAGE
-
homodimer
-
2 * 52000, SDS-PAGE
-
homotetramer
-
-
homotetramer
-
4 * 52000
-
homotetramer
-
4 * 62300, His8-tagged protein
homotetramer
structure solved by molecular replacement, corresponding to the native state of the enzyme in solution
homotetramer
4 * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE, 4 * 54400, about, sequence calculation
homotetramer
-
4 * 55000, recombinant N-terminally His-tagged enzyme, SDS-PAGE, 4 * 54400, about, sequence calculation
-
monomer
-
recombinant enzyme expressed in Escherichia coli
monomer
-
recombinant enzyme expressed in Escherichia coli
-
monomer
-
mutant enzymes R479D, P478, P477, P476, P475, and P474, determined by size-exclusion chromatography
monomer
-
mutant enzymes R479D, P478, P477, P476, P475, and P474, determined by size-exclusion chromatography
-
tetramer
-
-
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 55000-62000
tetramer
-
4 * 55000-62000
-
tetramer
-
purified enzyme from the native Bacillus sp. AR9 by gel filtration
tetramer
-
purified enzyme from the native Bacillus sp. AR9 by gel filtration
-
tetramer
-
4 * 56500, SDS-PAGE
tetramer
x-ray crystallography
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 86000, artificial fusion protein, SDS-PAGE
tetramer
-
4 * 52000, recombinant enzyme, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
-
tetramer
-
4 * 86000, artificial fusion protein, SDS-PAGE
-
tetramer
-
4 * 56000, SDS-PAGE
tetramer
-
4 * 86000, artificial fusion protein, SDS-PAGE
tetramer
-
4 * 56000, SDS-PAGE
-
tetramer
-
4 * 86000, artificial fusion protein, SDS-PAGE
-
tetramer
4 * 56000, His-tagged recombinant protein
tetramer
x-ray crystallography
tetramer
-
4 * 53000, SDS-PAGE
tetramer
-
4 * 54000, gel filtration, denaturing conditions
tetramer
each subunit of the tetrameric enzyme consists of an elliptically distorted (alpha/beta)8-barrel domain
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 54000, SDS-PAGE
tetramer
x-ray crystallography
tetramer
-
in the absence of Zn2+, the protein acquires a tetrameric functional structure at pH 6.0, which is stable up to pH 9
tetramer
-
x-ray crystallography
-
tetramer
-
4 * 54000, SDS-PAGE
additional information
enzyme structure homology modeling
additional information
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
additional information
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
enzyme structure homology modeling
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
enzyme structure homology modeling
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
enzyme structure homology modeling
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
enzyme structure homology modeling
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
enzyme structure homology modeling
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
enzyme structure homology modeling
-
additional information
-
the overall structure of each Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The architecture of the dihydropyrimidinase monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain. The overall structure and architecture of the active site of Pseudomonas aeruginosa dihydropyrimidinase are similar to those of other dihydropyrimidinases
-
additional information
-
Pseudomonas aeruginosa dihydropyrimidinase unit consists of 17 alpha-helices, 19 beta-sheets, and two zinc ions. The enzyme monomer consists of two domains, namely, a large domain with a classic (beta/alpha)8-barrel structure core embedding the catalytic dimetal center and a small beta-sandwich domain
-
additional information
-
enzyme structure homology modeling
-
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F159A
-
turnover number for hydantoin is 10% of that of the wild-type enzyme, Km-value for hydantoin is 4.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 6.1fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
F159I
-
turnover number for hydantoin is 61% of that of the wild-type enzyme, Km-value for hydantoin is 1.9fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.6fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
F159L
-
turnover number for hydantoin 64% of the turnover number of the wild-type enzyme, Km-value for hydantoin is 90% of the value of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 61% of that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.5fold lower than that of the wild-type enzyme
F159V
-
turnover number for hydantoin is 22% of that of the wild-type enzyme, Km-value for hydantoin is 1.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.8fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
L65F/F159A F159A
-
turnover number for hydantoin is 10.9% of that of the wild-type enzyme, Km-value for hydantoin is 4.8fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 11fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
M63A
120% of wild-type activity
M63A/F159S
411% of wild-type activity
M63F/L65V F159A
-
turnover number for hydantoin is 9.5% of that of the wild-type enzyme, Km-value for hydantoin is 2.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 10fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 4.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
M63H/F159N
450% of wild-type activity
M63H/F159R
168% of wild-type activity
M63H/F159S
353% of wild-type activity
M63I
108% of wild-type activity
M63I/F159A
374% of wild-type activity
M63I/F159S
540% of wild-type activity
M63I/F159T
411% of wild-type activity
M63Q/F159N
213% of wild-type activity
F159A
-
turnover number for hydantoin is 10% of that of the wild-type enzyme, Km-value for hydantoin is 4.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 6.1fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.4fold higher than that of the wild-type enzyme. Specificity of the mutant enzyme towards aromatic substrate hydroxyphenylhydantoin is enhanced by 200fold compared with that of the wild-type enzyme
-
F159I
-
turnover number for hydantoin is 61% of that of the wild-type enzyme, Km-value for hydantoin is 1.9fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.6fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
-
F159L
-
turnover number for hydantoin 64% of the turnover number of the wild-type enzyme, Km-value for hydantoin is 90% of the value of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 61% of that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 2.5fold lower than that of the wild-type enzyme
-
F159S
-
turnover number for hydantoin is 4.7% of that of the wild-type enzyme, Km-value for hydantoin is 4fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 15.5fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 5fold higher than that of the wild-type enzyme
-
F159V
-
turnover number for hydantoin is 22% of that of the wild-type enzyme, Km-value for hydantoin is 1.6fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 2.8fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 1.5fold lower than that of the wild-type enzyme
-
F150C
about 5% of wild-type activity
F150D
about 5% of wild-type activity
F150E
about 5% of wild-type activity
F150G
about 8% of wild-type activity
F150H
about 5% of wild-type activity
F150I
about 10% of wild-type activity
F150K
about 5% of wild-type activity
F150L
about 10% of wild-type activity
F150M
about 15% of wild-type activity
F150N
about 5% of wild-type activity
F150P
about 5% of wild-type activity
F150Q
about 5% of wild-type activity
F150R
about 5% of wild-type activity
F150S
about 5% of wild-type activity
F150T
about 5% of wild-type activity
F150V
about 5% of wild-type activity
F150W
about 5% of wild-type activity
F150Y
about 18% of wild-type activity
F63C
about 75% of wild-type activity
F63D
about 15% of wild-type activity
F63E
about 10% of wild-type activity
F63G
about 50% of wild-type activity
F63H
about 115% of wild-type activity
F63I
about 80% of wild-type activity
F63K
about 35% of wild-type activity
F63L
about 105% of wild-type activity
F63M
about 95% of wild-type activity
F63N
about 110% of wild-type activity
F63P
about 10% of wild-type activity
F63Q
about 25% of wild-type activity
F63R
about 30% of wild-type activity
F63S
about 75% of wild-type activity
F63T
about 70% of wild-type activity
F63V
about 70% of wild-type activity
F63W
about 95% of wild-type activity
F63Y
about 125% of wild-type activity
L157A
33.6% of wild-type activity
L157D
11% of wild-type activity
L157I
94.0% of wild-type activity
L157V
98.3% of wild-type activity
L92C
about 25% of wild-type activity
L92D
about 10% of wild-type activity
L92E
about 10% of wild-type activity
L92F
about 95% of wild-type activity
L92G
about 10% of wild-type activity
L92H
about 15% of wild-type activity
L92I
about 120% of wild-type activity
L92K
about 20% of wild-type activity
L92M
about 115% of wild-type activity
L92N
about 10% of wild-type activity
L92P
about 5% of wild-type activity
L92Q
about 15% of wild-type activity
L92R
about 5% of wild-type activity
L92S
about 10% of wild-type activity
L92T
about 35% of wild-type activity
L92V
about 70% of wild-type activity
L92W
about 10% of wild-type activity
L92Y
about 5% of wild-type activity
D316A
site-directed mutagenesis, inactive mutant
H183A
site-directed mutagenesis, inactive mutant
H239A
site-directed mutagenesis, inactive mutant
H59A
site-directed mutagenesis, inactive mutant
H61A
site-directed mutagenesis, inactive mutant
K150A
site-directed mutagenesis, inactive mutant
N337A
site-directed mutagenesis, the mutant enzyme is active, but its activity is about 20fold less than that of the wild-type dihydropyrimidinase
S289A
site-directed mutagenesis, inactive mutant
Y155A
site-directed mutagenesis, inactive mutant
D316A
-
site-directed mutagenesis, inactive mutant
-
H183A
-
site-directed mutagenesis, inactive mutant
-
H61A
-
site-directed mutagenesis, inactive mutant
-
K150A
-
site-directed mutagenesis, inactive mutant
-
Y155A
-
site-directed mutagenesis, inactive mutant
-
D316A
-
site-directed mutagenesis, inactive mutant
-
H183A
-
site-directed mutagenesis, inactive mutant
-
H61A
-
site-directed mutagenesis, inactive mutant
-
K150A
-
site-directed mutagenesis, inactive mutant
-
Y155A
-
site-directed mutagenesis, inactive mutant
-
D316A
-
site-directed mutagenesis, inactive mutant
-
H183A
-
site-directed mutagenesis, inactive mutant
-
H61A
-
site-directed mutagenesis, inactive mutant
-
K150A
-
site-directed mutagenesis, inactive mutant
-
Y155A
-
site-directed mutagenesis, inactive mutant
-
D316A
-
site-directed mutagenesis, inactive mutant
-
H183A
-
site-directed mutagenesis, inactive mutant
-
H61A
-
site-directed mutagenesis, inactive mutant
-
K150A
-
site-directed mutagenesis, inactive mutant
-
Y155A
-
site-directed mutagenesis, inactive mutant
-
D316A
-
site-directed mutagenesis, inactive mutant
-
H183A
-
site-directed mutagenesis, inactive mutant
-
H61A
-
site-directed mutagenesis, inactive mutant
-
K150A
-
site-directed mutagenesis, inactive mutant
-
Y155A
-
site-directed mutagenesis, inactive mutant
-
D316A
-
site-directed mutagenesis, inactive mutant
-
H183A
-
site-directed mutagenesis, inactive mutant
-
H61A
-
site-directed mutagenesis, inactive mutant
-
K150A
-
site-directed mutagenesis, inactive mutant
-
Y155A
-
site-directed mutagenesis, inactive mutant
-
D316A
-
site-directed mutagenesis, inactive mutant
-
H183A
-
site-directed mutagenesis, inactive mutant
-
H61A
-
site-directed mutagenesis, inactive mutant
-
K150A
-
site-directed mutagenesis, inactive mutant
-
Y155A
-
site-directed mutagenesis, inactive mutant
-
DELTA474-479
-
C-terminally truncated mutant, expressed in the form of random aggregates without any activity
DELTA475-479
-
C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
DELTA476-479
-
C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
DELTA477-479
-
C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
DELTA478-479
-
C-terminally truncated mutant, dissociated into the monomeric state, the activity is largely retained
R474
-
mutant is expressed in the form of random aggregates without any activity
F159S
-
turnover number for hydantoin is 4.7% of that of the wild-type enzyme, Km-value for hydantoin is 4fold higher than that of the wild-type enzyme, turnover-number for DL-hydroxyphenylhydantoin is 15.5fold higher than that of the wild-type enzyme, Km-value for DL-hydroxyphenylhydantoin is 5fold higher than that of the wild-type enzyme
F159S
400% of wild-type activity
R412M
-
inactive
R412M
-
inactive enzyme, missense mutation causing dihydropyrimidase deficiency
W360R
-
inactive
W360R
-
inactive enzyme, missense mutation causing dihydropyrimidase deficiency
R479A
-
mutant is expressed in the form of random aggregates without any activity
R479A
-
expressed in the form of random aggregates without any activity
R479A
-
the mutant is expressed in the form of random aggregates without any activity, the relative activity of mutant is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
R479D
-
dissociates into the monomeric state but 78.2% retains activity of the wild type enzyme
R479D
-
dissociated into the monomeric state, activity is largely retained
R479D
-
the C-terminal-substituted enzyme is dissociated into the monomeric state, but the activity is largely retained, the relative activity of mutant is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
R479A
-
mutant is expressed in the form of random aggregates without any activity
-
R479A
-
expressed in the form of random aggregates without any activity
-
additional information
immobilization of the purified recombinant enzyme on N-carbamoyl-D-4-hydroxyphenylglycine in batch reactions, method optimization: 0.155 mM enzyme/disc, in 0.1 M Tris-HCl, pH 8, and 0.8 M sodium chloride, 14 h, overview. 99% enzyme activity remains after 15 reaction cycles. The immobilized DHTase membrane can achieve a larger pH and thermal tolerant range than that of free enzyme
additional information
-
immobilization of the purified recombinant enzyme on N-carbamoyl-D-4-hydroxyphenylglycine in batch reactions, method optimization: 0.155 mM enzyme/disc, in 0.1 M Tris-HCl, pH 8, and 0.8 M sodium chloride, 14 h, overview. 99% enzyme activity remains after 15 reaction cycles. The immobilized DHTase membrane can achieve a larger pH and thermal tolerant range than that of free enzyme
-
additional information
HYDc1 with the C-terminal Arg deletion retains 43% activity, while HYDn1 with the N-terminal Ser deletion has no activity using DL-hydantoin as substrate
additional information
-
the truncated mutants P478, P477, P476, and P475 are dissociated into the monomeric state, but their activities are largely retained (86.7-57.0% of wild type activity)
additional information
-
the flexibility of the non-conservative region at the C-terminus is quite limited implying that the intact enzyme structure is essential for enzyme activity
additional information
-
several truncated mutants (P478, P477, P476, and P475) are dissociated into the monomeric state as well, but their activities are largely retained, the relative activities of mutants is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
additional information
-
the truncated mutants P478, P477, P476, and P475 are dissociated into the monomeric state, but their activities are largely retained (86.7-57.0% of wild type activity)
-
additional information
-
the flexibility of the non-conservative region at the C-terminus is quite limited implying that the intact enzyme structure is essential for enzyme activity
-
additional information
-
several truncated mutants (P478, P477, P476, and P475) are dissociated into the monomeric state as well, but their activities are largely retained, the relative activities of mutants is about twice as that of the wild type enzyme at pH 6.0 and pH 10.0
-
additional information
-
HYDc1 with the C-terminal Arg deletion retains 43% activity, while HYDn1 with the N-terminal Ser deletion has no activity using DL-hydantoin as substrate
-
additional information
-
whole-cell immobilization on calcium alginate of D-hydantoinase-engineered Escherichia coli strain BL21(DE3) for D-carbamoyl-4-hydroxyphenylglycine (D-CpHPG) biosynthesis. Whole-cell immobilization method involves addition of 3.0% w/v alginate, 1.5% w/v diatomite, 0.05% w/v CaCl2, and 1.0 mM MnCl2. The optimized diameter of immobilized beads for the whole-cell biosynthesis is 2.60 mm. The maximized production rates of D-CpHPG are up to 76%, and the immobilized beads can be reused for 12 batches. Method optimization and evaluation, overview
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industry
-
production of optically pure D-amino acids that are key intermediates in the synthesis of commercial products such as beta-lactam semisynthetic antibiotics, peptides, hormones, pyretroids and pesticides
industry
-
production of optically pure D-amino acids that are key intermediates in the synthesis of commercial products such as beta-lactam semisynthetic antibiotics, peptides, hormones, pyretroids and pesticides
-
medicine
-
-
medicine
-
D-amino acids for preparation of beta-lactam antibiotics like semisynthetic penicillins and cephalosporins such as ampicillin, amoxicillin and cefadroxyl, peptide hormones and pesticides
medicine
-
D-amino acids for preparation of beta-lactam antibiotics like semisynthetic penicillins and cephalosporins such as ampicillin, amoxicillin and cefadroxyl, peptide hormones and pesticides
medicine
-
D-amino acids for preparation of beta-lactam antibiotics like semisynthetic penicillins and cephalosporins such as ampicillin, amoxicillin and cefadroxyl, peptide hormones and pesticides
medicine
-
industrial production of L-amino acids
medicine
-
development of the enzymatic process for production of D-p-hydroxyphenylglycine from DL-5-hydroxyphenylhydantoin, new drugs based on p-hydroxyphenylglycine like aspoxicillin, cefbuperazine and cepyramide expected to be marketed in near future
medicine
-
D-amino acids for preparation of beta-lactam antibiotics like semisynthetic penicillins and cephalosporins such as ampicillin, amoxicillin and cefadroxyl, peptide hormones and pesticides
-
medicine
-
development of the enzymatic process for production of D-p-hydroxyphenylglycine from DL-5-hydroxyphenylhydantoin, new drugs based on p-hydroxyphenylglycine like aspoxicillin, cefbuperazine and cepyramide expected to be marketed in near future
-
medicine
-
D-amino acids for preparation of beta-lactam antibiotics like semisynthetic penicillins and cephalosporins such as ampicillin, amoxicillin and cefadroxyl, peptide hormones and pesticides
-
medicine
-
development of the enzymatic process for production of D-p-hydroxyphenylglycine from DL-5-hydroxyphenylhydantoin, new drugs based on p-hydroxyphenylglycine like aspoxicillin, cefbuperazine and cepyramide expected to be marketed in near future
-
nutrition
-
-
nutrition
-
useful for production of D-amino acids, microbial hydantoinases used industrially to produce N-carbamoyl-D-hydroxyphenylglycine
nutrition
-
useful for production of D-amino acids, microbial hydantoinases used industrially to produce N-carbamoyl-D-hydroxyphenylglycine
nutrition
-
no degradative activity for L-tryptophan, method for L-tryptophan production is very promising as a commercial process
synthesis
-
-
synthesis
-
artificial fusion enzyme useful as potential biocatalyst for production of nonnatural amino acids
synthesis
-
artificial fusion enzyme useful as potential biocatalyst for production of nonnatural amino acids
synthesis
-
artificial fusion enzyme useful as potential biocatalyst for production of nonnatural amino acids
synthesis
-
artificial fusion enzyme useful as potential biocatalyst for production of nonnatural amino acids
synthesis
-
production of enantiomeric pure nonproteinogenic amino acids, currently under investigation in bioprocess scale for industrial application
synthesis
-
production of enantiomeric pure nonproteinogenic amino acids, currently under investigation in bioprocess scale for industrial application
synthesis
-
used technically in combination with carbamoylases for production of D-amino acids and non-proteinogenic L-amino acids
synthesis
-
commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
synthesis
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commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
synthesis
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commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
synthesis
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commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
synthesis
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thermostable enzyme with great biotechnological potential
synthesis
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industrial enzyme, that is widely used in the production of D-amino acids which are precursors for semisynthesis of antibiotics, peptides, and pesticides
synthesis
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production of D-N-carbamoyl amino acid
synthesis
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encapsulation of a crude cell extract from Agrobacterium radiobacter containing D-hydantoinase and D-carbamoylase activities into alginate-chitosan polyelectrolyte complexes with negligible leakage from the formed capsules. The most suitable biocatalysts are prepared using a chitosan with a medium molecular weight of 600 kDa and a degree of deacetylation of 0.9. For all of the preparation conditions under study, an encapsulation yield of around 60% was achieved and the enzymatic activity yields ranged from 30 to 80% for D-hydantoinase activity and from 40 to 128% for D-carbamoylase activity relative to the activities of the soluble extract. All of the biocatalysts are able to hydrolyze LD-hydroxyphenylhydantoin into p-hydroxyphenylglycine with yields ranging from 30 to 80%
synthesis
to produce optically pure D-amino acids, microbial D-hydantoinase is used for stereospecific hydrolysis of chemically synthesized cyclic hydantoins
synthesis
the D-hydantoinase is an important enzyme capable of a reversible enantioselective ring-opening hydrolysis of hydantoins being applied for the efficient production of D-form amino acids which are key compounds applicable for the production of antibiotics, peptide hormones, pyrethroids, and pesticides in industry
synthesis
recombinant D-PfHYD can potentially be applied in the synthesis of D-amino acids
synthesis
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the D-hydantoinase is an important enzyme capable of a reversible enantioselective ring-opening hydrolysis of hydantoins being applied for the efficient production of D-form amino acids which are key compounds applicable for the production of antibiotics, peptide hormones, pyrethroids, and pesticides in industry
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synthesis
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artificial fusion enzyme useful as potential biocatalyst for production of nonnatural amino acids
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synthesis
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recombinant D-PfHYD can potentially be applied in the synthesis of D-amino acids
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synthesis
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to produce optically pure D-amino acids, microbial D-hydantoinase is used for stereospecific hydrolysis of chemically synthesized cyclic hydantoins
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synthesis
-
commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
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synthesis
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artificial fusion enzyme useful as potential biocatalyst for production of nonnatural amino acids
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synthesis
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commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
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synthesis
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commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
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synthesis
-
commercial production of optically pure amino acids for synthesis of antibiotics, pharmaceuticals, artificial sweeteners and biologically active peptides, food ingredients, pyrethroids, pesticides, antimicrobial and antiviral agents and other agrochemicals
-
synthesis
-
thermostable enzyme with great biotechnological potential
-
synthesis
-
artificial fusion enzyme useful as potential biocatalyst for production of nonnatural amino acids
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additional information
useful for industrial production of enantiomerically pure D-amino acids
additional information
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useful for industrial production of enantiomerically pure D-amino acids
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