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an N-carbamoyl-L-2-amino acid + H2O
an L-2-amino acid + NH3 + CO2
-
-
-
-
?
N-acetyl-L-alanine + H2O
L-alanine + acetate
-
-
-
-
?
N-acetyl-L-methionine + H2O
L-methionine + acetate
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
-
-
-
-
?
N-acetyl-L-tyrosine + H2O
L-tyrosine + acetate
-
-
-
-
?
N-acetyl-L-valine + H2O
L-valine + acetate
-
-
-
-
?
N-carbamoyl-D,L-serine + H2O
L-serine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-2-aminoburyric acid + H2O
L-2-aminobutyric acid + CO2 + NH3
N-carbamoyl-DL-2-aminohexanoic acid + H2O
2-aminohexanoic acid + CO2 + NH3
-
24% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-DL-alanine + H2O
L-alanine + CO2 + NH3
N-carbamoyl-DL-aminobutyric acid + H2O
L-aminobutyric acid + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-aspartic acid + H2O
DL-aspartic acid + CO2 + NH3
-
relative activity 7.81%
-
-
?
N-carbamoyl-DL-cysteine + H2O
DL-cysteine + CO2 + NH3
-
relative activity 119%
-
-
?
N-carbamoyl-DL-homophenylalanine + H2O
L-homophenylalanine + CO2 + NH3
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
N-carbamoyl-DL-norleucine + H2O
L-norleucine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-norvaline + H2O
L-norvaline + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
N-carbamoyl-DL-phenylglycine + H2O
L-phenylglycine + CO2 + NH3
low activity
-
-
?
N-carbamoyl-DL-serine + H2O
DL-serine + CO2 + NH3
-
relative activity 37.8%
-
-
?
N-carbamoyl-DL-serine + H2O
L-serine + CO2 + NH3
N-carbamoyl-DL-threonine + H2O
L-threonine + CO2 + NH3
N-carbamoyl-DL-valine + H2O
L-valine + CO2 + NH3
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
N-carbamoyl-L-asparagine + H2O
L-asparagine + CO2 + NH3
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
N-carbamoyl-L-glutamic acid + H2O
L-glutamic acid + CO2 + NH3
N-carbamoyl-L-homophenylalanine + H2O
L-homophenylalanine + NH3 + CO2
-
-
-
?
N-carbamoyl-L-isoleucine + H2O
L-isoleucine + CO2 + NH3
N-carbamoyl-L-leucine + H2O
L-leucine + CO2 + NH3
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
N-carbamoyl-L-phenylglycine + H2O
L-phenylglycine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-thienylalanine + H2O
L-thienylalanine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + CO2 + NH3
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
N-carbamoyl-L-valine + H2O
L-valine + CO2 + NH3
N-formyl-DL-2-aminobutyric acid + H2O
L-2-aminobutyric acid + CO2
-
-
-
?
N-formyl-DL-alanine + H2O
L-alanine + CO2
N-formyl-DL-aminobutyric acid + H2O
L-aminobutyric acid + CO2
-
-
-
?
N-formyl-DL-ethionine + H2O
L-ethionine + CO2
-
-
-
?
N-formyl-DL-homophenylalanine + H2O
L-homophenylalanine + CO2
-
-
-
?
N-formyl-DL-leucine + H2O
L-leucine + CO2
-
5.2% of activity with N-carbamoyl-DL-alanine
-
?
N-formyl-DL-methionine + H2O
L-methionine + CO2
N-formyl-DL-norleucine + H2O
L-norleucine + CO2
-
-
-
?
N-formyl-DL-norvaline + H2O
L-norvaline + CO2
-
-
-
?
N-formyl-DL-phenylalanine + H2O
L-phenylalanine + CO2
-
-
-
?
N-formyl-DL-phenylglycine + H2O
L-phenylglycine + CO2
-
-
-
?
N-formyl-DL-tryptophan + H2O
L-tryptophan + CO2
N-formyl-L-alanine + H2O
L-alanine + CO2
-
-
-
-
?
N-formyl-L-methionine + H2O
L-methionine + HCOOH
N-formyl-L-phenylalanine + H2O
L-phenylalanine + CO2
-
-
-
-
?
N-formyl-L-tyrosine + H2O
L-tyrosine + CO2
-
-
-
-
?
N-formyl-L-valine + H2O
L-valine + CO2
-
-
-
-
?
additional information
?
-
N-acetyl-L-methionine + H2O
L-methionine + acetate
-
-
-
-
?
N-acetyl-L-methionine + H2O
L-methionine + acetate
-
-
-
-
?
N-carbamoyl-DL-2-aminoburyric acid + H2O
L-2-aminobutyric acid + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-2-aminoburyric acid + H2O
L-2-aminobutyric acid + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-homophenylalanine + H2O
L-homophenylalanine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-homophenylalanine + H2O
L-homophenylalanine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
4.5% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
25% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
enzyme seems to be selective for aromatic amino acids
-
?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-serine + H2O
L-serine + CO2 + NH3
-
19% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-DL-serine + H2O
L-serine + CO2 + NH3
-
86% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-DL-threonine + H2O
L-threonine + CO2 + NH3
-
8.8% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-DL-threonine + H2O
L-threonine + CO2 + NH3
-
94% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-DL-valine + H2O
L-valine + CO2 + NH3
-
28% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-DL-valine + H2O
L-valine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-valine + H2O
L-valine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-valine + H2O
L-valine + CO2 + NH3
-
-
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
-
75% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
-
71% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
-
relative activity 72.4%
-
-
?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
-
relative activity 41.2%
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-asparagine + H2O
L-asparagine + CO2 + NH3
-
64% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-L-asparagine + H2O
L-asparagine + CO2 + NH3
-
52% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
-
relative activity 100%
-
-
?
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-glutamic acid + H2O
L-glutamic acid + CO2 + NH3
-
56% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-L-glutamic acid + H2O
L-glutamic acid + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-isoleucine + H2O
L-isoleucine + CO2 + NH3
-
5.3% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-L-isoleucine + H2O
L-isoleucine + CO2 + NH3
-
55% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-L-isoleucine + H2O
L-isoleucine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-isoleucine + H2O
L-isoleucine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-leucine + H2O
L-leucine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-leucine + H2O
L-leucine + CO2 + NH3
-
9.1% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-L-leucine + H2O
L-leucine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-leucine + H2O
L-leucine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
12% of activity with N-carbamoyl-L-alanine
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
L-stereospecific enzyme
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
preferred substrate
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
preferred substrate
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
preferred substrate
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
L-stereospecific enzyme
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
L-stereospecific enzyme
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
L-stereospecific enzyme
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
relative activity 44.4%
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
L-stereospecific enzyme
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
activity assay
-
-
?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
-
kinetic assay
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
the recombinant L-carbamoylase from Escherichia coli harboring the pET-Case is L-stereospecific
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + CO2 + NH3
-
-
-
?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
-
3% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
-
-
-
?
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-valine + H2O
L-valine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-valine + H2O
L-valine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-valine + H2O
L-valine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-valine + H2O
L-valine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-valine + H2O
L-valine + CO2 + NH3
-
-
-
-
?
N-formyl-DL-alanine + H2O
L-alanine + CO2
-
13% of activity with N-carbamoyl-DL-alanine
-
?
N-formyl-DL-alanine + H2O
L-alanine + CO2
-
-
-
?
N-formyl-DL-alanine + H2O
L-alanine + CO2
-
-
-
?
N-formyl-DL-methionine + H2O
L-methionine + CO2
-
5.4% of activity with N-carbamoyl-DL-alanine
-
?
N-formyl-DL-methionine + H2O
L-methionine + CO2
-
-
-
?
N-formyl-DL-methionine + H2O
L-methionine + CO2
-
-
-
?
N-formyl-DL-tryptophan + H2O
L-tryptophan + CO2
-
-
-
?
N-formyl-DL-tryptophan + H2O
L-tryptophan + CO2
-
-
-
?
N-formyl-DL-tryptophan + H2O
L-tryptophan + CO2
-
-
-
?
N-formyl-L-methionine + H2O
L-methionine + HCOOH
-
-
-
-
?
N-formyl-L-methionine + H2O
L-methionine + HCOOH
-
-
-
-
?
additional information
?
-
-
the enzyme shows stereospecificity and a broad substrate specificity. No or poor activitz with N-carbamoyl-alpha-alanine, N-carbamoyl-glycine, N-carbamoyl-beta-alanine, and N-carbamoyl-alpha-aminoisobutyrate
-
-
?
additional information
?
-
-
the enzyme shows stereospecificity and a broad substrate specificity. No or poor activitz with N-carbamoyl-alpha-alanine, N-carbamoyl-glycine, N-carbamoyl-beta-alanine, and N-carbamoyl-alpha-aminoisobutyrate
-
-
?
additional information
?
-
-
the enzyme in this study is strigently L-specific
-
-
?
additional information
?
-
catalytic promiscuity of L-N-carbamoylase from Geobacillus stearothermophilus CECT43, substrate specificity with different N-formyl- and N-carbamoyl-DL-amino acids, overview. No N-formyl-DL-tert-leucine
-
-
?
additional information
?
-
the enzyme is a strict enantiospecific L-N-carbamoylase. Development of a bienzymatic system comprising an N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264 and the enantiospecific L-N-carbamoylase from Geobacillus stearothermophilus CECT43. The biocatalyst system is able to produce optically pure natural and non-natural L-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate is found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and the an N-succinylamino acid racemase proves to be the limiting stepof the system due to its lower specific activity, overview
-
-
?
additional information
?
-
catalytic promiscuity of L-N-carbamoylase from Geobacillus stearothermophilus CECT43, substrate specificity with different N-formyl- and N-carbamoyl-DL-amino acids, overview. No N-formyl-DL-tert-leucine
-
-
?
additional information
?
-
-
catalytic promiscuity of L-N-carbamoylase from Geobacillus stearothermophilus CECT43, substrate specificity with different N-formyl- and N-carbamoyl-DL-amino acids, overview. No N-formyl-DL-tert-leucine
-
-
?
additional information
?
-
the enzyme is a strict enantiospecific L-N-carbamoylase. Development of a bienzymatic system comprising an N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264 and the enantiospecific L-N-carbamoylase from Geobacillus stearothermophilus CECT43. The biocatalyst system is able to produce optically pure natural and non-natural L-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate is found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and the an N-succinylamino acid racemase proves to be the limiting stepof the system due to its lower specific activity, overview
-
-
?
additional information
?
-
-
strictly specific for the L-form of N-carbamoyl-amino acids as substrates and exhibits high activity in the hydrolysis of N-carbamoyl-L-cysteine as substrate
-
-
?
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1,10-phenanthroline
-
54% inhibition at 2 mM
2-mercaptoethanol
-
10 mM causes 29% inhibition, suggesting that no cysteine residue is crucial for enzyme activity, although they might have a structural role
4-chloromercuribenzoic acid
-
-
4-hydroxymercuribenzoate
-
complete inhibition at 1 mM
5,5'-dithiobis(2-nitrobenzoic acid)
5,5'-dithiobis-(2-nitrobenzoic acid)
-
specific activity 0.39, relative activity 58%
8-hydroxyquinoline
-
2 mM, 65% inhibition
8-Hydroxyquinoline-5-sulfonic acid
-
10 mM, decreases the activity to 13%
alpha,alpha'-dipyridyl
-
2.5 mM, 26% inhibition
ATP
-
0.5 mM, approximately 50% inhibition, 1.5 mM, approximately 85% inhibition
beta-mercaptoethanol
-
specific activity 0.44, relative activity 66%
Cd2+
-
2 mM, 86% inhibition
Cs+
-
2 mM, slight inhibition
diisopropyl fluorophosphate
-
5 mM, 18% inhibition
dithiothreitol
-
10 mM causes 41% inhibition, suggesting that no cysteine residue is crucial for enzyme activity, although they might have a structural role
Fe2+
-
2 mM, strong inhibition
iodoacetate
-
2 mM, 43% inhibitiion
K+
-
2 mM, specific activity 0.56, relative activity 84%
Mercuric chloride
-
complete inhibition at 1 mM
Mg2+
-
slightly inhibited activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme and HQSA pretreated enzyme
N-bromosuccinimide
-
complete inhibition at 1 mM
N-ethylmaleimide
-
2 mM, 100% inhibitiion
NaAsO2
-
5 mM, 20% inhibition
o-phenanthroline
-
10 mM, 47% inhibition
p-chloromercuribenzoic acid
phenylhydrazine
-
5 mM, 48% inhibition
phenylmethylsulfonyl fluoride
-
5 mM, 31% inhibition
sodium propionate
-
10 mM, 20% inhibition, competitive inhibition of N-carbamoyl-L-alanine hydrolysis
5,5'-dithiobis(2-nitrobenzoic acid)
-
2 mM, 100% inhibition
5,5'-dithiobis(2-nitrobenzoic acid)
-
2 mM, slight inhibition
Cu2+
-
2 mM, 85% inhibition
Cu2+
-
2 mM, specific activity 0.2, relative activity 30%
EDTA
-
10 mM, 22% inhibition
EDTA
-
15% inhibition at 5 mM, 27% at 10 mM
EDTA
-
10 mM, decreases the activity to 15%
EDTA
-
10 mM, specific activity 0, relative activity 0%
Fe3+
-
2 mM, strong inhibition
Fe3+
-
2 mM, specific activity 0.44, relative activity 66%
Hg2+
-
2 mM, 100% inhibition
Hg2+
-
2 mM, strong inhibition
Hg2+
-
strongly inhibits the activity
Hg2+
-
2 mM, specific activity 0, relative activity 0%
iodoacetic acid
-
IAA
N-ethyl-maleimide
-
NEM
Na+
-
2 mM, slight inhibition
Na+
-
2 mM, specific activity 0.57, relative activity 85%
p-chloromercuribenzoic acid
-
2 mM, 100% inhibitiion
p-chloromercuribenzoic acid
-
PCMB
Pb2+
-
2 mM, slight inhibition
Pb2+
-
2 mM, specific activity 0.39, relative activity 58%
Zn2+
-
2 mM, 85% inhibition
Zn2+
-
weak inhibition at 1 mM
Zn2+
-
2 mM, specific activity 0.29, relative activity 43%
additional information
-
not inhibited by 5 mM NaCN, NaF, NaN3, NH2OH, semicarbazide, (NH4)2SO4, NaCO3, N-carbamoyl-D-valine, N-carbamoyl-D-alanine or L-alanine
-
additional information
-
no inhibition by PMSF and DTT
-
additional information
-
no substrate inhibition is observed
-
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36.12
N-acetyl-L-alanine
-
pH 7.5, 65°C, preincubation with CoCl2
5.5 - 12.66
N-acetyl-L-methionine
12.9
N-acetyl-L-phenylalanine
-
pH 7.5, 65°C, preincubation with CoCl2
116
N-acetyl-L-tyrosine
-
pH 7.5, 65°C, preincubation with CoCl2
13.92
N-acetyl-L-valine
-
pH 7.5, 65°C, preincubation with CoCl2
0.85
N-carbamoyl-DL-2-aminohexanoic acid
-
-
3.2
N-carbamoyl-DL-methionine
-
-
10
N-carbamoyl-DL-serine
-
-
0.94 - 4.19
N-carbamoyl-L-alanine
1.5
N-carbamoyl-L-asparagine
-
-
4.91
N-carbamoyl-L-cysteine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
51.23
N-carbamoyl-L-glutamic acid
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
0.31
N-carbamoyl-L-isoleucine
-
-
0.86
N-carbamoyl-L-leucine
-
-
0.2 - 17.8
N-carbamoyl-L-methionine
0.92 - 5.82
N-carbamoyl-L-phenylalanine
0.65
N-carbamoyl-L-tryptophan
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
4.8 - 12.99
N-carbamoyl-L-tyrosine
0.4 - 34.47
N-carbamoyl-L-valine
6.6
N-Carbamoylglycine
-
-
16
N-formyl-DL-alanine
-
-
5
N-formyl-L-alanine
-
pH 7.5, 65°C, preincubation with CoCl2
9.77 - 12.9
N-formyl-L-methionine
13.82
N-formyl-L-phenylalanine
-
pH 7.5, 65°C, preincubation with CoCl2
23.78
N-Formyl-L-tyrosine
-
pH 7.5, 65°C, preincubation with CoCl2
6.75
N-formyl-L-valine
-
pH 7.5, 65°C, preincubation with CoCl2
5.5
N-acetyl-L-methionine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
12.66
N-acetyl-L-methionine
-
pH 7.5, 65°C, preincubation with CoCl2
0.94
N-carbamoyl-L-alanine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
3
N-carbamoyl-L-alanine
-
-
4.19
N-carbamoyl-L-alanine
-
pH 7.5, 65°C, preincubation with CoCl2
0.2
N-carbamoyl-L-methionine
-
SmLcar mutant E132D
0.2
N-carbamoyl-L-methionine
-
SmLcar mutant E132Q
0.6
N-carbamoyl-L-methionine
-
SmLcar mutant E132H
0.69
N-carbamoyl-L-methionine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
0.7
N-carbamoyl-L-methionine
-
SmLcar wild type
1
N-carbamoyl-L-methionine
-
SmLcar mutant H230A
2.8
N-carbamoyl-L-methionine
-
SmLcar mutant N279A
2.9
N-carbamoyl-L-methionine
-
pH 7.5, 65°C, preincubation with CoCl2
13.5
N-carbamoyl-L-methionine
-
pH 7.5, 40°C
17.8
N-carbamoyl-L-methionine
-
pH 7.5, 40°C
0.92
N-carbamoyl-L-phenylalanine
-
-
2.61
N-carbamoyl-L-phenylalanine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
5.82
N-carbamoyl-L-phenylalanine
-
pH 7.5, 65°C, preincubation with CoCl2
4.8
N-carbamoyl-L-tyrosine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
12.99
N-carbamoyl-L-tyrosine
-
pH 7.5, 65°C, preincubation with CoCl2
0.4
N-carbamoyl-L-valine
-
-
3.29
N-carbamoyl-L-valine
-
pH 7.5, 65°C, preincubation with CoCl2
34.47
N-carbamoyl-L-valine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
9.77
N-formyl-L-methionine
-
pH 7.5, 65°C, preincubation with CoCl2
12.9
N-formyl-L-methionine
-
determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+
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0.66
-
N-carbamoyl-L-methionine
10
-
pH 8.0, 50°C, free enzyme
111.3
-
Ni2+, 333.96% relative activity of 8-hydroxyquinoline-5-sulfonic acid (HQSA) pretreated enzyme compared to activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme without addition of any effectors, pH 7.5, 65°C
114
-
Ni2+, 341.94% relative activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme compared to activity without addition of any effectors, pH 7.5, 65°C
145
-
purified enzyme, pH 7.5, 40°C
15.9
-
protein recovered from inclusion bodies
179
-
Co2+, 536.91% relative activity of 8-hydroxyquinoline-5-sulfonic acid (HQSA) pretreated enzyme pretreated enzyme compared to activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme without addition of any effectors, pH 7.5, 65°C
2.91
-
pH 8.0, 50°C, immobilized enzyme
21.5
-
at pH 7.5 and 42°C
221.4
-
Co2+, 663.89% relative activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme compared to activity without addition of any effectors, pH 7.5, 65°C
33.34
-
activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme, pH 7.5, 65°C
40.2
-
120% relative activity of 8-hydroxyquinoline-5-sulfonic acid (HQSA) pretreated enzyme compared to activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme, pH 7.5, 65°C
65.69
-
Mn2+, 197% relative activity of 8-hydroxyquinoline-5-sulfonic acid (HQSA) pretreated enzyme compared to activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme without addition of any effectors, pH 7.5, 65°C
95.67
-
Mn2+, 286.93% relative activity of non 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme compared to activity without addition of any effectors, pH 7.5, 65°C
23.2
-
-
23.2
-
pH 9.0, 50°C, last purification step
additional information
-
0.00000162 mol/ml, enzyme activity in cell extracts of wild-type cells
additional information
-
0.00001174 mol/ml, enzyme activity in cell extracts of wild-type cells induced with 2-thiouracil
additional information
-
0.00000804 mol/ml, enzyme activity in cell extracts of inducer-independent mutant
additional information
-
0.00000778 mol/ml, enzyme activity in cell extracts of inducer-independent mutants induced with 2-thiouracil
additional information
-
overview of effect of metal ions and other chemical agents on the enzyme activity of 8-hydroxyquinoline-5-sulfonic acid (HQSA) treated enzyme and the HQSA pretreated enzyme
additional information
-
the activity of the recombinant enzyme is lower than the wild-type strain MH602. The expressed proteins are mainly present in the insoluble fraction, indicating the formation of inclusion bodies
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biotechnology
-
production of optically pure L-amino acids by an enzymatic method named hydantoinase process
synthesis
-
production of a cell biocatalyst for the production of L-homophenylalanine from D,L-homophenylalanylhydantoin by coexpression of the pydB gene and a thermostable L-N-carbamoylase gene from Bacillus kaustophilus CCRC11223 in Escherichia coli JM109. The expression levels of dihydropyrimidinase and l-N-carbamoylase in the recombinant Escherichia coli cells are estimated to be about 20% of the respective total soluble proteins. When 1% (w/v) isopropyl-beta-D-thiogalactopyranoside-induced cells are used as biocatalysts, a conversion yield of 49% for D,L-homophenylalanylhydantoin with more than 99% enantiomeric excess can be reached in 16 h at pH 7.0 from 10 mM D,L-homophenylalanylhydantoin. The cells can be reused for at least eight cycles at a conversion yield of more than 43%. Coexpression of pydB and lnc in Escherichia coli might be a potential biocatalyst for production of L-homophenylalanylhydantoin
synthesis
-
to develop a recombinant Escherichia coli whole cell system for the conversion of racemic N-carbamoyl-L-homophenylalanine to L-homophenylalanine, naaar gene from Deinococcus radiodurans and L-N-carbamoylase gene from Bacillus kaustophilus BCRC11223 are cloned and coexpressed in Escherichia coli cells. Recombinant cells treated with 0.5% toluene at 30°C for 30 min exhibit enhanced N-acylamino acid racemase and L-N-carbamoylase activities, which are about 20fold and 60fold, respectively, higher than those of untreated cells. Using toluene-permeabilized recombinant Escherichia coli cells, a maximal productivity of 7.5 mmol L-homophenylalanine/l h with more than 99% yield could be obtained from 150 mmol racemic N-carbamoyl-D-homophenylalanine. Permeabilized cells show considerable stability in the bioconversion process using 10 mmol racemic N-carbamoyl-D-homophenylalanine as substrate, no significantly decrease in conversion yield for L-homophenylalanine is found in the eight cycles
synthesis
-
a bi-enzyme process for the synthesis of L-homophenylalanine from N-carbamoyl-D-homophenylalanine with immobilized N-acylamino acid racemase and immobilized L-N-carbamoylase. In batch operation, quantitative conversion is achieved. It is a promising alternative for the synthesis of L-homophenylalanine from racemate of N-carbamoyl-DL-homophenylalanine
synthesis
development of a bienzymatic biocatalyst system comprising an N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264 and the enantiospecific L-N-carbamoylase from Geobacillus stearothermophilus CECT43. The biocatalyst system is able to produce optically pure natural and non-natural L-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate is found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and the an N-succinylamino acid racemase proves to be the limiting step of the system due to its lower specific activity, overview
synthesis
production of different optically pure L-alpha-amino acids starting from different racemic N-formyl- and N-carbamoyl-amino acids using a dynamic kinetic resolution approach with immobilized L-N-carbamoylase and N-succinyl-amino acid racemase as biocatalysts, the system is effective for the biosynthesis of natural and unnatural L-amino acids (enantiomeric excess over 99.5%), overview
synthesis
-
the enzyme shows promise as a potential biocatalyst for L-alpha-amino acid production
synthesis
-
the enzyme shows promise as a potential biocatalyst for L-alpha-amino acid production
-
synthesis
-
production of different optically pure L-alpha-amino acids starting from different racemic N-formyl- and N-carbamoyl-amino acids using a dynamic kinetic resolution approach with immobilized L-N-carbamoylase and N-succinyl-amino acid racemase as biocatalysts, the system is effective for the biosynthesis of natural and unnatural L-amino acids (enantiomeric excess over 99.5%), overview
-
synthesis
-
development of a bienzymatic biocatalyst system comprising an N-succinylamino acid racemase from Geobacillus kaustophilus CECT4264 and the enantiospecific L-N-carbamoylase from Geobacillus stearothermophilus CECT43. The biocatalyst system is able to produce optically pure natural and non-natural L-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate is found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and the an N-succinylamino acid racemase proves to be the limiting step of the system due to its lower specific activity, overview
-
synthesis
-
to develop a recombinant Escherichia coli whole cell system for the conversion of racemic N-carbamoyl-L-homophenylalanine to L-homophenylalanine, naaar gene from Deinococcus radiodurans and L-N-carbamoylase gene from Bacillus kaustophilus BCRC11223 are cloned and coexpressed in Escherichia coli cells. Recombinant cells treated with 0.5% toluene at 30°C for 30 min exhibit enhanced N-acylamino acid racemase and L-N-carbamoylase activities, which are about 20fold and 60fold, respectively, higher than those of untreated cells. Using toluene-permeabilized recombinant Escherichia coli cells, a maximal productivity of 7.5 mmol L-homophenylalanine/l h with more than 99% yield could be obtained from 150 mmol racemic N-carbamoyl-D-homophenylalanine. Permeabilized cells show considerable stability in the bioconversion process using 10 mmol racemic N-carbamoyl-D-homophenylalanine as substrate, no significantly decrease in conversion yield for L-homophenylalanine is found in the eight cycles
-
synthesis
-
production of a cell biocatalyst for the production of L-homophenylalanine from D,L-homophenylalanylhydantoin by coexpression of the pydB gene and a thermostable L-N-carbamoylase gene from Bacillus kaustophilus CCRC11223 in Escherichia coli JM109. The expression levels of dihydropyrimidinase and l-N-carbamoylase in the recombinant Escherichia coli cells are estimated to be about 20% of the respective total soluble proteins. When 1% (w/v) isopropyl-beta-D-thiogalactopyranoside-induced cells are used as biocatalysts, a conversion yield of 49% for D,L-homophenylalanylhydantoin with more than 99% enantiomeric excess can be reached in 16 h at pH 7.0 from 10 mM D,L-homophenylalanylhydantoin. The cells can be reused for at least eight cycles at a conversion yield of more than 43%. Coexpression of pydB and lnc in Escherichia coli might be a potential biocatalyst for production of L-homophenylalanylhydantoin
-
additional information
enzyme immobilization on solid matrix results in a great enhancement of the enzyme activity toward N-formyl-tryptophan, the reaction can be repeated for several cycles, method optimization, overview
additional information
-
immobilization of the enzyme by covalent coupling to a solid support material including additional cross-linking with polyaldehyde-dextran, method development, overview. Temperature and pH optima of immobilized enzyme are increased by 10°C and 0.5 unit, respectively. The enzyme is significantly stabilized, it is recycled nine times with about 100% conversion efficiency when batch experiments are carried out at 35°C, pH 7.5, for the 180 min cycle
additional information
-
immobilization of the enzyme by covalent coupling to a solid support material including additional cross-linking with polyaldehyde-dextran, method development, overview. Temperature and pH optima of immobilized enzyme are increased by 10°C and 0.5 unit, respectively. The enzyme is significantly stabilized, it is recycled nine times with about 100% conversion efficiency when batch experiments are carried out at 35°C, pH 7.5, for the 180 min cycle
-
additional information
-
enzyme immobilization on solid matrix results in a great enhancement of the enzyme activity toward N-formyl-tryptophan, the reaction can be repeated for several cycles, method optimization, overview
-
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Ishikawa, T.; Mukohara, Y.; Watabe, K.; Kobayashi, S.; Nakamura, H.
Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Bacillus stearothermophilus NS1122A
Biosci. Biotechnol. Biochem.
58
265-270
1994
Geobacillus stearothermophilus, Geobacillus stearothermophilus NS1122A
-
brenda
Ogawa, J.; Miyake, H.; Shimizu, S.
Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans
Appl. Microbiol. Biotechnol.
43
1039-1043
1995
Achromobacter xylosoxidans
brenda
Ishikawa, T.; Watabe, K.; Mukohara, Y.; Nakamura, H.
N-carbamyl-L-amino acid amidohydrolase of Pseudomonas sp. strain NS671: purification and some properties of the enzyme expressed in Escherichia coli
Biosci. Biotechnol. Biochem.
60
612-615
1996
Pseudomonas sp., Pseudomonas sp. NS671
brenda
Ishikawa, T.; Watabe, K.; Mukohara, Y.; Nakamura, H.
Mechanism of stereospecific conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Pseudomonas sp. strain NS671
Biosci. Biotechnol. Biochem.
61
185-187
1997
Pseudomonas sp.
brenda
Wilms, B.; Wiese, A.; Syldatk, C.; Mattes, R.; Altenbuchner, J.; Pietzsch, M.
Cloning, nucleotide sequence and expression of a new L-N-carbamoylase gene from Arthrobacter aurescens DSM 3747 in E. coli
J. Biotechnol.
68
101-113
1999
Paenarthrobacter aurescens
brenda
Pietzsch, M.; Wiese, a.; Ragnitz, K.; wilms, B.; Altenbuchner, J.; Mattes, R.; Syldatk, C.
Purification of recombinant hydantoinase and L-N-carbamoylase from Arthrobacter aurescens expressed in Escherichia coli: comparison of wild-type and genetically modified proteins
J. Chromatogr.
737
179-186
2000
Paenarthrobacter aurescens
brenda
Hartley, C.J.; Manford, F.; Burton, S.G.; Dorrington, R.A.
Over-production of hydantoinase and N-carbamoylamino acid amidohydrolase enzymes by regulatory mutants of Agrobacterium tumefaciens
Appl. Microbiol. Biotechnol.
57
43-49
2001
Agrobacterium tumefaciens
brenda
Ohmachi, T.; Narita, M.; Kawata, M.; Bizen, A.; Tamura, Y.; Asada, Y.
A novel N-carbamoyl-L-amino acid amidohydrolase of Pseudomonas sp. strain ON-4a: purification and characterization of N-carbamoyl-L-cysteine amidohydrolase expressed in Escherichia coli
Appl. Microbiol. Biotechnol.
65
686-693
2004
Pseudomonas sp.
brenda
Martinez-Rodriguez, S.; Andujar-Sanchez, M.; Clemente Jimenez, J.M.; Jara-Perez, V.; Rodriguez-Vico, F.; Las Heras-Vazquez, F.J.
Thermodynamic and mutational studies of l-N-carbamoylase from Sinorhizobium meliloti CECT 4114 catalytic centre
Biochimie
88
837-847
2006
Sinorhizobium meliloti
brenda
Martinez-Rodriguez, S.; Clemente-Jimenez, J.M.; Rodriguez-Vico, F.; Las Heras-Vazquez, F.J.
Molecular cloning and biochemical characterization of L-N-carbamoylase from Sinorhizobium meliloti CECT4114
J. Mol. Microbiol. Biotechnol.
9
16-25
2005
Sinorhizobium meliloti
brenda
Kao, C.H.; Lo, H.H.; Hsu, S.K.; Hsu, W.H.
A novel hydantoinase process using recombinant Escherichia coli cells with dihydropyrimidinase and L-N-carbamoylase activities as biocatalyst for the production of L-homophenylalanine
J. Biotechnol.
134
231-239
2008
Geobacillus kaustophilus, Geobacillus kaustophilus CCRC 11223
brenda
Hsu, S.; Lo, H.; Lin, W.; Chen, I.; Kao, C.; Hsu, W.
Stereoselective synthesis of L-homophenylalanine using the carbamoylase method with in situ racemization via N-acylamino acid racemase
Process Biochem.
42
856-862
2007
Geobacillus kaustophilus, Geobacillus kaustophilus BCRC11223
-
brenda
Martinez-Rodriguez, S.; Garcia-Pino, A.; Las Heras-Vazquez, F.J.; Clemente-Jimenez, J.M.; Rodriguez-Vico, F.; Loris, R.; Garcia-Ruiz, J.M.; Gavira, J.A.
Crystallization and preliminary crystallographic studies of the recombinant L-N-carbamoylase from Geobacillus stearothermophilus CECT43
Acta Crystallogr. Sect. F
64
1135-1138
2008
Geobacillus stearothermophilus, Geobacillus stearothermophilus CECT43
brenda
Martnez-Rodrguez, S.; Martnez-Gmez, A.I.; Rodrguez-Vico, F.; Clemente-Jimnez, J.M.; Las Heras-Vzquez, F.J.
Carbamoylases: characteristics and applications in biotechnological processes
Appl. Microbiol. Biotechnol.
85
441-458
2010
Pseudomonas sp. ON4a
brenda
Pozo-Dengra, J.; Martinez-Gomez, A.I.; Martinez-Rodriguez, S.; Clemente-Jimenez, J.M.; Rodriguez-Vico, F.; Las Heras-Vazquez, F.J.
Evaluation of substrate promiscuity of an L-carbamoyl amino acid amidohydrolase from Geobacillus stearothermophilus CECT43
Biotechnol. Prog.
26
954-959
2010
Geobacillus stearothermophilus
brenda
Mei, Y.Z.; Wan, Y.M.; He, B.F.; Ying, H.J.; Ouyang, P.K.
New gene cluster from the thermophile Bacillus fordii MH602 in the conversion of DL-5-substituted hydantoins to L-amino acids
J. Microbiol. Biotechnol.
19
1497-1505
2009
Siminovitchia fordii
brenda
Yen, M.; Hsu, W.; Lin, S.
Synthesis of L-homophenylalanine with immobilized enzymes
Process Biochem.
45
667-674
2010
Geobacillus kaustophilus
-
brenda
Soriano-Maldonado, P.; Las Heras-Vazquez, F.J.; Clemente-Jimenez, J.M.; Rodriguez-Vico, F.; Martinez-Rodriguez, S.
Enzymatic dynamic kinetic resolution of racemic N-formyl- and N-carbamoyl-amino acids using immobilized L-N-carbamoylase and N-succinyl-amino acid racemase
Appl. Microbiol. Biotechnol.
99
283-291
2015
Geobacillus stearothermophilus (Q53389), Geobacillus stearothermophilus CECT43 (Q53389), Geobacillus stearothermophilus CECT43
brenda
Nandanwar, H.S.; Vohra, R.M.; Hoondal, G.S.
Trimeric l-N-carbamoylase from newly isolated Brevibacillus reuszeri HSN1: a potential biocatalyst for production of l-?-amino acids
Biotechnol. Appl. Biochem.
60
219-230
2013
Brevibacillus reuszeri, Brevibacillus reuszeri HSN1
brenda
Nandanwar, H.; Vohra, R.; Hoondal, G.
Enhanced stability of newly isolated trimeric L-methionine-N-carbamoylase from Brevibacillus reuszeri HSN1 by covalent immobilization
Biotechnol. Appl. Biochem.
60
305-315
2013
Brevibacillus reuszeri, Brevibacillus reuszeri HSN1
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