N‐Carbamoyl‐d‐amino acid amidohydrolase from Comamonas sp. E222c Purification and characterization
作者： Jun OGAWA , Sakayu SHIMIZU , Hideaki YAMADA
DOI: 10.1111/J.1432-1033.1993.TB17706.X
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摘要: N‐Carbamoyl‐d‐amino acid amidohydrolase was purified 119‐fold, with 36% overall recovery from a cell‐free extract of Comamonas sp. E222c. The purified enzyme was homogeneous as judged by SDS/PAGE. The relative molecular mass of the native enzyme was 120 000 and that of the subunit was 40 000. The purified enzyme hydrolyzed various N‐carbamoyl‐d‐amino acids to d‐amino acids, ammonia and carbon dioxide. N‐Carbamoyl‐d‐amino acids having hydrophobic groups served as good substrates for the enzyme. The Km …
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