3.5.1.87: N-carbamoyl-L-amino-acid hydrolase
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For detailed information about N-carbamoyl-L-amino-acid hydrolase, go to the full flat file.
Word Map on EC 3.5.1.87
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3.5.1.87
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hydantoinase
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arthrobacter
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hydantoin
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biocatalyst
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racemase
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stearothermophilus
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aurescens
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synthesis
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racemic
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l-specific
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l-tryptophan
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geobacillus
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kaustophilus
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brevibacillus
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beta-alanine
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l-homophenylalanine
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amidohydrolases
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l-forms
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biotechnology
- 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
Reaction
Synonyms
ADS79_04835, AtcC, BsLcar, carbamoylated amino acid carbamoylase, hyuC, immobilized L-N-carbamoylase, L-carbamoylase, L-methionine-N-carbamoylase, L-N-carbamoylamino acid aminohydrolase, L-N-carbamoylase, L-NCC amidohydrolase, Lnc, LNCA, N-carbamoyl-amino-acid amidohydrolase, N-carbamoyl-L-alpha-amino acid amidohydrolase, N-carbamoyl-L-amino acid amidohydrolase, N-carbamoyl-L-amino-acid amidohydrolase, N-carbamoyl-L-amino-acid hydrolase, N-carbamoyl-L-cysteine amidohydrolase, N-carbamoyl-L-cysteine-acid amidohydrolase, N-carbamyl-L-amino acid amidohydrolase, NCC amidohydrolase, SmLcar
ECTree
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Application
Application on EC 3.5.1.87 - N-carbamoyl-L-amino-acid hydrolase
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biotechnology
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production of optically pure L-amino acids by an enzymatic method named hydantoinase process
synthesis
additional information
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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
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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
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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
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the enzyme shows promise as a potential biocatalyst for L-alpha-amino acid production
synthesis
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the enzyme shows promise as a potential biocatalyst for L-alpha-amino acid production
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synthesis
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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
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synthesis
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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
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synthesis
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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
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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
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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
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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
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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
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additional information
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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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