Purification and properties of N-carbamylputrescine amidohydrolase from maize shoots
Purification and properties of N-carbamylputrescine amidohydrolase from maize shoots
复制标题
玉米芽中 N-氨甲酰腐胺酰胺水解酶的纯化及性质
DOI：
10.1016/0031-9422(82)85177-7
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发表时间：
1982
期刊：
影响因子：
3.8
通讯作者：
Yonezo Suzuki
中科院分区：
文献类型：
--
作者：
H. Yanagisawa;Yonezo Suzuki
纯化N-氨甲酰腐胺(NCP)酰胺水解酶c．玉米芽的 70 倍。该酶存在于细胞质和选择性中。 pH值为6.5-7.0。该酶具有较高的底物特异性，NCP 的 Km 为 9 X 10-5 M。活化能为 11.7 kcal/mol。分子。重量。通过凝胶过滤估计酶的浓度为125 000。Cu2+、Zn2+和对羟基汞苯甲酸盐是该酶的抑制剂。
N-carbamylputrescine (NCP) amidohydrolase was purified c. 70-fold from maize shoots. The enzyme was present in the cytosol and the opt. pH was 6.5-7.0. The enzyme had a high substrate specificity and the Km for NCP was 9 X 10-5 M. The energy of activation was 11.7 kcal/mol. The mol. wt. of the enzyme estimated by gel filtration was 125 000. Cu2+, Zn2+ and p-hydroxymercuribenzoate were inhibitors of the enzyme.