%0 Journal Article
%T A Dicarboxylate Monoamide Amidohydrolase (Half-Amidase) from Alcaligenes eutrophus 112R4<br>真养产碱杆菌112R4的二羧酸单酰胺酰胺水解酶
%A Zhang Yingzi
%A Wang Yu
%A Yu Zhihua
%A Liu Yangjian
%A Wang Jiang
%A Ding Jiuyuan
%A =
%A <br>张英姿
%A 王宇
%A 余志华
%A 刘阳剑
%A 王绛
%A 丁久元
%J 微生物学报
%D 2003
%I 
%X A dicarboxylate monoamide amidohydrolase (half-amidase) was identified from a cyclic-imide-metabolizing microorganism, Alcaligenes eutrophus 112R 4. The enzyme catalyzed the hydrolysis of monoamidated dicarboxylates, which were the hydrolyzing products of cyclic imides by imidase, to dicarboxylates and ammonia. The enzyme showed high catalytic activity to succinamic acid, but no obvious activity to aliphatic amides, amino acid amides, N-carbamoyl amino acids and urea was observed. The productions of half-amidase and imidase were correlative in Alcaligenes eutrophus 112R 4, in that succinimide and succinamic acid enhanced the expressions of these two enzymes simultaneously, while free ammonia repressed their expressions. Succinate showed regulation effects on either synthesis or activities of half-amidase and imidase. The characteristics of half-amidase were investigated by using the crude extract of recombined E. coli cell. The fact that cobalt ion stimulated the activity of half-amidase by a coefficient of 3.37, implied that half-amidase was probably a metal-binding enzyme.
%K Dicarboxylate monoamide amidohydrolase
%K half-amidase
%K Metabolism of cyclic imide
%K Imidase
%K Alcaligenes eutrophus<br>二羧酸单酰胺酰胺水解酶，半酰胺酶，环酰亚胺代谢，酰亚胺酶，真养产碱杆菌
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=4CA8B2C21F1CC3E0&yid=D43C4A19B2EE3C0A&vid=BE33CC7147FEFCA4&iid=CA4FD0336C81A37A&sid=117F81797AB182FC&eid=39EEF47180459690&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=14