Kim H S, Kim B H, Cho Y D
Department of Biochemistry, College of Science, Yonsei University, Seoul, Korea.
Arch Biochem Biophys. 1998 Jun 1;354(1):40-6. doi: 10.1006/abbi.1998.0663.
Lysine decarboxylase (EC 4.1.1.18) was purified 364-fold from 2-day-old soybean (Glycine max) axes. The enzyme was a monomeric protein having a molecular mass of 95,000 Da and an isoelectric point of 4.0. The K(m) for L-lysine was 1.17 mM. The optimal temperature and pH of the enzyme were 37 degrees C and 7.5, respectively. Storage of the enzyme at temperature ranging from 0 to 4 degrees C caused a 50% loss of the activity in 24 h. The enzyme was competitively inhibited by Cl- with a Ki value of 1.46 mM. However, the activity of the purified enzyme was not inhibited by F-, Br-, I-, H2PO4-, HPO4(2-), or SO4(2-). Cadaverine at 1 mM inhibited the enzyme activity by 35%.
赖氨酸脱羧酶（EC 4.1.1.18）从2日龄大豆（Glycine max）胚轴中纯化了364倍。该酶是一种单体蛋白，分子量为95,000 Da，等电点为4.0。L-赖氨酸的K(m)为1.17 mM。该酶的最适温度和pH分别为37℃和7.5。在0至4℃的温度下储存该酶会导致其活性在24小时内丧失50%。该酶受到Cl-的竞争性抑制，Ki值为1.46 mM。然而，纯化酶的活性不受F-、Br-、I-、H2PO4-、HPO4(2-)或SO4(2-)的抑制。1 mM的尸胺抑制酶活性35%。
