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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General Information
General Information on EC 3.5.1.87 - N-carbamoyl-L-amino-acid hydrolase
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metabolism
additional information
horseradish peroxidase (EC 1.11.1.7) and N-carbamoyl-L-amino acid amidohydrolase (L-N-carbamoylase, EC 3.5.1.87) are used as model proteins to investigate the effect of pegylationon enzyme activity and stability. Pegylation of enzymes, pegylation of L-N-carbamoylase with activated PEG2000, method evaluation, overview. Decline in activity for the pegylated L-N-carbamoylase. The modulation of enzyme activity and stability upon pegylation is generally mediated by the PEG domains in protecting active sites from freeradicals and/or in limiting the accessibility of substrates. Upon pegylation with lower molecular weight PEG the thermostability of HRP increases significantly. The enhancement in thermostability exhibited by PEG2000-HRP can thus be attributed to the stabilizing effect exhibited by the hydrophilic PEG domains of PEG-HRP conjugates in reducing aggregation of enzyme
the enzyme is involved in the (N-carbamoyl-L-cysteine) pathway (L-NCC pathway) converting DL-2-amino-DELTA2-thiazoline-4-carboxylic acid to L-cysteine
metabolism
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the enzyme is involved in the (N-carbamoyl-L-cysteine) pathway (L-NCC pathway) converting DL-2-amino-DELTA2-thiazoline-4-carboxylic acid to L-cysteine
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