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- W2022365595 abstract "A thermostable N-carbamoyl-d-amino acid amidohydrolase was found in the cells of newly isolated bacterium, Blastobacter sp. A17p-4. The bacterium also showed d-specific hydantoinase activity. The N-carbamoyl-d-amino acid amidohydrolase activity of the cells exhibited a temperature optimum at 50–55°C, and was stable up to 50°C. The N-carbamoyl-d-amino acid amidohydrolase of Blastobacter sp. A17p-4 was purified to homogeneity and characterized. It has a relative molecular weight of about 120 000 and consists of three identical subunits with a relative molecular weight of about 40 000. N-Carbamoyl-d-amino acids having hydrophobic groups served as good substrates for the enzyme. It has been suggested that d-amino acid production from dl-5-substituted hydantoin involves the action of a series of enzymes involved in pyrimidine degradation, namely amide-ring opening enzyme, dihydropyrimidinase, and N-carbamoylamide hydrolyzing enzyme, β-ureidopropionase. However, the purified enzyme did not hydrolyze β-ureidopropionate; suggesting that the N-carbamoyl-d-amino acid amidohydrolase coexisting with d-specific hydantoinase, probably dihydropyrimidinase, in Blastobacter sp. A17p-4 is different from β-ureidopropionase." @default.
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- W2022365595 date "1994-11-01" @default.
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- W2022365595 title "Thermostable N- acid amidohydrolase: screening, purification and characterization" @default.
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- W2022365595 doi "https://doi.org/10.1016/0168-1656(94)90143-0" @default.
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