节杆菌K1108乙内酰脲酶三维结构的模建和分析  

Homology modeling and analysis of three-dimensional structure of Arthrobacter K1108 hydantoinase

作　　者：岳俊杰[1] 王月兰[1] 周秀菊[1] 张惟材[1] 梁龙[1] 黄培堂[1] 

机构地区：[1]军事医学科学院生物工程研究所,北京100071

出　　处：《生物技术通讯》2003年第3期182-184,共3页Letters in Biotechnology

摘　　要：利用同源模建技术,以节杆菌DSM3745乙内酰脲酶的晶体结构为模板,模建了节杆菌K1108乙内酰脲酶的三维结构。模建的节杆菌K1108乙内酰脲酶结构由一个中心的(α/β)8桶状结构域和富含β-折叠的结构域两个区域组成,富含β-折叠的结构域在中心(α/β)8桶状结构域的侧面,由分子的N端和C端组成。根据K1108乙内酰脲酶和其它酶在结构和活性部位的保守性,确定了K1108乙内酰脲酶的底物结合部位,并对酶的活性中心的特征进行了分析,对L-Hyd的底物选择性进行了解释。We propose a model for the L-hydantoinase(L-Hyd)from Arthrobacter K1108,based on homology model-ing using the L-Hyd from Arthrobacter aurescens as a template.The built model consists of two domains,the cen-tral is a(α/β) 8 domain,which is flanked by aβ-sheet rich domain,theβ-sheet rich domain comprises both N-and the C-terminus.The strong homology to other related enzymes both in fold and in active site is exploited for i-dentification of substrate binding site of Arthrobacter K1108L-Hyd.We made a preliminary analysis of the charac-teristic of the active sites for this enzyme and provided an explanation for different substrate selectives of L-Hyd.

关 键 词：节杆菌 乙内酰脲酶 三维结构 活性部位 

分 类 号：Q55[生物学—生物化学] Q936