CRYSTALLIZATION AND SOME PROPERTIES OF ACETYLPOLYAMINE AMIDOHYDROLASE FROM MYCOPLANA-BULLATA
CRYSTALLIZATION AND SOME PROPERTIES OF ACETYLPOLYAMINE AMIDOHYDROLASE FROM MYCOPLANA-BULLATA
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DOI：
10.1016/s0006-291x(88)80997-5
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发表时间：
1988-12-30
影响因子：
3.1
通讯作者：
UWAJIMA, T
中科院分区：
文献类型：
--
作者：
FUJISHIRO, K;ANDO, M;UWAJIMA, T
在研究微生物分解乙酰多胺的过程中，我们发现大麦霉菌BP-1845产生乙酰多胺氨基水解酶，并从无细胞提取液中分离出结晶形式的乙酰多胺酰胺水解酶。该酶表观分子量为67 kDa，由两个相同的亚基组成。0-羟基喹啉对该酶有抑制作用，结晶酶的每个亚基含有一个锌原子。该酶以乙酰腐胺为底物，最适pH为8.0左右，对多种乙酰多胺如乙酰腐胺、乙酰尸胺、乙酰亚精胺和乙酰精胺具有广泛的底物专一性和较高的亲和力。
During the course of investigations on the catabolism of acetylpolyamines by microorganisms, we found that acetylpolyamine amidohydrolase was produced by Mycoplana bullata FERM BP-1845 and isolated the enzyme from the cell-free extract in crystalline form. The enzyme had an apparent molecular weight of 67 kDa and was composed of two identical subunits. The enzyme activity was inhibited by 0-oxyquinoline and the crystalline enzyme contained one zinc atom per each subunit. The enzyme had an optimal pH around 8.0 with acetylputrescine as substrate and showed broad substrate specificity and high affinity towards various acetylpolyamines, such as acetylputrescine, acetylcadaverine, acetylspermidine, and acetylspermine.