H. Hagino, K. Nakayama
Jun 1, 1968
Citations
1
Influential Citations
8
Citations
Journal
Agricultural and biological chemistry
Abstract
3-Methylthiopropylamine (MTPA) formation from L-methionine in Streptomyces sp. K37 was studied in detail. The reaction was confirmed to be catalyzed by the decarboxylase of L-methionine. The properties of the enzyme were studied in detail using acetone dried cells or cell-free extract. The enzyme was specific for L-methionine. Pyridoxal phosphate stimulated the reaction and protected the enzyme against heat inactivation. The optimum pH for the reaction was 6.0-8.0 and the optimum temperature was about 40°C. Carbonyl reagents (10-2-..10-3 M) inhibited the reaction completely, and silver nitrate and mercuric chloride (10-3•`10-4M) markedly inhibited the reaction. Km value for the reaction was 1.21 X 10-5 M. L-Methionine assay using the decarboxylase was attempted and was found to be applicable to practical use.