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Information on EC 3.5.1.87 - N-carbamoyl-L-amino-acid hydrolase
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3.5.1.87 N-carbamoyl-L-amino-acid hydrolaseIUBMB Comments
This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids . The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents . The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].
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Word Map
- 3.5.1.87
- hydantoinase
- arthrobacter
- hydantoin
-
biocatalyst
- racemase
- stearothermophilus
- aurescens
- synthesis
-
racemic
-
l-specific
- l-tryptophan
-
geobacillus
- kaustophilus
-
brevibacillus
- beta-alanine
- l-homophenylalanine
-
amidohydrolases
-
l-forms
- biotechnology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
l-n-carbamoylase, bslcar, l-carbamoylase, n-carbamyl-l-amino acid amidohydrolase, l-methionine-n-carbamoylase, n-carbamoyl-l-cysteine amidohydrolase, ncc amidohydrolase, l-ncc amidohydrolase, n-carbamoyl-l-amino acid amidohydrolase, smlcar, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADS79_04835
AtcC
BsLcar
carbamoylated amino acid carbamoylase
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-
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hyuC
-
gene name, from the hyu gene cluster containing four genes with novel cluster organization characteristics
L-carbamoylase
L-methionine-N-carbamoylase
L-N-carbamoylamino acid aminohydrolase
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L-N-carbamoylase
L-NCC amidohydrolase
Lnc
LNCA
N-carbamoyl-L-alpha-amino acid amidohydrolase
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-
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N-carbamoyl-L-amino acid amidohydrolase
N-carbamoyl-L-amino-acid amidohydrolase
N-carbamoyl-L-amino-acid hydrolase
N-carbamoyl-L-cysteine amidohydrolase
N-carbamyl-L-amino acid amidohydrolase
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NCC amidohydrolase
L-carbamoylase
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L-N-carbamoylase
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N-carbamoyl-L-amino acid amidohydrolase
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N-carbamoyl-L-cysteine amidohydrolase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
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an N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O = an L-2-amino acid + NH3 + CO2
recombinant BsLcar is able to hydrolyze N-acetyl and N-formyl-amino acids in addition to N-carbamoyl-amino acids, showing strict L-enantioselectivity for all the three. Additionally, the enzyme shows the fastest amidohydrolase activity on the N-formyl-amino acid followed by N-carbamoyl and N-acetyl ones
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of C-N bond
hydrolysis of C-N bond
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SYSTEMATIC NAME
IUBMB Comments
N-carbamoyl-L-amino-acid amidohydrolase
This enzyme, along with EC 3.5.1.77 (N-carbamoyl-D-amino-acid hydrolase), EC 5.1.99.5 (hydantoin racemase) and hydantoinase, forms part of the reaction cascade known as the "hydantoinase process", which allows the total conversion of D,L-5-monosubstituted hydantoins into optically pure D- or L-amino acids [3]. The enzyme from Alcaligenes xylosoxidans has broad specificity for carbamoyl-L-amino acids, although it is inactive on the carbamoyl derivatives of glutamate, aspartate, arginine, tyrosine or tryptophan. The enzyme from Sinorhizobium meliloti requires a divalent cation for activity and can hydrolyse N-carbamoyl-L-tryptophan as well as N-carbamoyl L-amino acids with aliphatic substituents [2]. The enzyme is inactive on derivatives of D-amino acids. In addition to N-carbamoyl L-amino acids, the enzyme can also hydrolyse formyl and acetyl derivatives to varying degrees [1,2].
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CAS REGISTRY NUMBER
COMMENTARY
116412-22-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an N-carbamoyl-L-2-amino acid + H2O
an L-2-amino acid + NH3 + CO2
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?
N-acetyl-L-phenylalanine + H2O
L-phenylalanine + acetate
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-
?
N-carbamoyl-DL-2-aminohexanoic acid + H2O
2-aminohexanoic acid + CO2 + NH3
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24% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-DL-aminobutyric acid + H2O
L-aminobutyric acid + CO2 + NH3
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-
-
?
N-carbamoyl-DL-aspartic acid + H2O
DL-aspartic acid + CO2 + NH3
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relative activity 7.81%
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-
?
N-carbamoyl-DL-cysteine + H2O
DL-cysteine + CO2 + NH3
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relative activity 119%
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-
?
N-carbamoyl-DL-norleucine + H2O
L-norleucine + CO2 + NH3
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-
-
?
N-carbamoyl-DL-norvaline + H2O
L-norvaline + CO2 + NH3
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-
-
?
N-carbamoyl-DL-phenylglycine + H2O
L-phenylglycine + CO2 + NH3
low activity
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-
?
N-carbamoyl-DL-serine + H2O
DL-serine + CO2 + NH3
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relative activity 37.8%
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-
?
N-carbamoyl-L-homophenylalanine + H2O
L-homophenylalanine + NH3 + CO2
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-
-
?
N-carbamoyl-L-phenylglycine + H2O
L-phenylglycine + CO2 + NH3
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-
-
-
?
N-carbamoyl-L-thienylalanine + H2O
L-thienylalanine + CO2 + NH3
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-
-
?
N-formyl-DL-2-aminobutyric acid + H2O
L-2-aminobutyric acid + CO2
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-
-
?
N-formyl-DL-aminobutyric acid + H2O
L-aminobutyric acid + CO2
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-
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?
N-formyl-DL-ethionine + H2O
L-ethionine + CO2
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-
-
?
N-formyl-DL-homophenylalanine + H2O
L-homophenylalanine + CO2
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-
-
?
N-formyl-DL-leucine + H2O
L-leucine + CO2
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5.2% of activity with N-carbamoyl-DL-alanine
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?
N-formyl-DL-norleucine + H2O
L-norleucine + CO2
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-
-
?
N-formyl-DL-norvaline + H2O
L-norvaline + CO2
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-
-
?
N-formyl-DL-phenylalanine + H2O
L-phenylalanine + CO2
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-
-
?
N-formyl-DL-phenylglycine + H2O
L-phenylglycine + CO2
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-
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?
N-formyl-L-phenylalanine + H2O
L-phenylalanine + CO2
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-
-
-
?
N-carbamoyl-DL-2-aminoburyric acid + H2O
L-2-aminobutyric acid + CO2 + NH3
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-
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?
N-carbamoyl-DL-2-aminoburyric acid + H2O
L-2-aminobutyric acid + CO2 + NH3
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?
N-carbamoyl-DL-alanine + H2O
L-alanine + CO2 + NH3
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-
-
?
N-carbamoyl-DL-homophenylalanine + H2O
L-homophenylalanine + CO2 + NH3
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-
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?
N-carbamoyl-DL-homophenylalanine + H2O
L-homophenylalanine + CO2 + NH3
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-
-
?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
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?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
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?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
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?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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4.5% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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25% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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enzyme seems to be selective for aromatic amino acids
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?
N-carbamoyl-DL-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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?
N-carbamoyl-DL-serine + H2O
L-serine + CO2 + NH3
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19% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-DL-serine + H2O
L-serine + CO2 + NH3
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86% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-DL-threonine + H2O
L-threonine + CO2 + NH3
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8.8% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-DL-threonine + H2O
L-threonine + CO2 + NH3
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94% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-DL-valine + H2O
L-valine + CO2 + NH3
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28% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-DL-valine + H2O
L-valine + CO2 + NH3
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?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
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75% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
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71% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-glycine + H2O
glycine + CO2 + NH3
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relative activity 72.4%
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?
N-carbamoyl-L-alanine + H2O
L-alanine + CO2 + NH3
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relative activity 41.2%
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?
N-carbamoyl-L-asparagine + H2O
L-asparagine + CO2 + NH3
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64% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-L-asparagine + H2O
L-asparagine + CO2 + NH3
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52% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-L-cysteine + H2O
L-cysteine + CO2 + NH3
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relative activity 100%
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?
N-carbamoyl-L-glutamic acid + H2O
L-glutamic acid + CO2 + NH3
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56% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-L-glutamic acid + H2O
L-glutamic acid + CO2 + NH3
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?
N-carbamoyl-L-isoleucine + H2O
L-isoleucine + CO2 + NH3
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5.3% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-L-isoleucine + H2O
L-isoleucine + CO2 + NH3
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55% of activity with N-carbamoyl-DL-alanine
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?
N-carbamoyl-L-leucine + H2O
L-leucine + CO2 + NH3
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9.1% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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12% of activity with N-carbamoyl-L-alanine
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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L-stereospecific enzyme
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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preferred substrate
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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preferred substrate
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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preferred substrate
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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L-stereospecific enzyme
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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L-stereospecific enzyme
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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L-stereospecific enzyme
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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relative activity 44.4%
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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L-stereospecific enzyme
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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activity assay
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?
N-carbamoyl-L-methionine + H2O
L-methionine + CO2 + NH3
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kinetic assay
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?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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-
-
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?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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-
-
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?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
-
-
-
?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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-
-
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?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
-
the recombinant L-carbamoylase from Escherichia coli harboring the pET-Case is L-stereospecific
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?
N-carbamoyl-L-phenylalanine + H2O
L-phenylalanine + CO2 + NH3
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-
-
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?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + CO2 + NH3
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-
-
-
?
N-carbamoyl-L-tryptophan + H2O
L-tryptophan + CO2 + NH3
-
-
-
?
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
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3% of activity with N-carbamoyl-DL-alanine
-
?
N-carbamoyl-L-tyrosine + H2O
L-tyrosine + CO2 + NH3
-
-
-
?
N-formyl-DL-alanine + H2O
L-alanine + CO2
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13% of activity with N-carbamoyl-DL-alanine
-
?
N-formyl-DL-alanine + H2O
L-alanine + CO2
-
-
-
?
N-formyl-DL-methionine + H2O
L-methionine + CO2
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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
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-
-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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the enzyme in this study is strigently L-specific
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?
additional information
?
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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
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-
?
additional information
?
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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
?
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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
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-
?
additional information
?
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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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an N-carbamoyl-L-2-amino acid + H2O
an L-2-amino acid + NH3 + CO2
-
-
-
-
?
N-carbamoyl-L-homophenylalanine + H2O
L-homophenylalanine + NH3 + CO2
-
-
-
?
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
-
-
?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
?
N-carbamoyl-DL-methionine + H2O
L-methionine + CO2 + NH3
-
-
-
?