Purification and Properties of N-Benzoyl-L-alanine Amidohydrolase from Corynebacterium equi(Biological Chemistry)

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N-Benzoyl-L-alanine amidohydrolase was purified from a cell-free extract of Corynebacterium equi H-7 which was grown in a medium containing hippuric acid as the sole carbon source. The purified enzyme was homogeneous on polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The molecular weight was 230,000 and the enzyme consisted of six subunits, identical in molecular weight (approximately 40,000). The isoelectric point of the enzyme was pH 4.6. The optimum pH of the enzyme reaction was 8.0 and the enzyme was stable from pH 7.0 to 8.0. The enzyme hydrolyzed N-benzoyl-L-alanine, N-benzoylglycine, and N-benzoyl-L-aminobutyric acid. The Km values for these substrates were 4.3 mM, 6.7mM, and 4.3mM, respectively. The enzyme was activated by Co^<2+>.
社団法人日本農芸化学会の論文
1986-06-23