%0 Journal Article
%T Molecular form and stability of D-hydantoinase deleted at C-terminal residue Arg<br>C-末端残基Arg缺失的D-海因酶的分子形式与稳定性
%A NIU Li-xi
%A ZHANG Xue-yao
%A SHI Ya-wei
%A YUAN Jing-ming
%A <br>钮利喜
%A 张学尧
%A 石亚伟
%A 袁静明
%J 微生物学报
%D 2006
%I 
%X This report is about only deleting one C-terminal residue of D-hydantoinase to result in obvious changes on its molecular form and stability. A recombinant D-hydantoinase (P479) and its mutant enzyme deleted at C-terminal residue Arg (P478) were prepared by methods of gene cloning, expression and purification. Results show that the subunit molecular weight of P479 and P478 is the same (54kDa) as determined by SDS-PAGE, whilst the molecular form of native P479 and P478 is a dimer and a monomer respectively in the completely operative conditions. Compared with P479, the enzymatic activity of P478 for substrate hydantoin maintained about 40% and pH stability was obviously increased, at the alkaline side in particular, as well as the anti-SDS ability was also raised. However, the thermal stability for P478 was clearly lowed as compared to P479. It implies from above data that the C-terminal residue Arg of the D-hydantoinase is a crucial one for subunit dissociation, but non-essential for catalysis.
%K D-hydantoinase
%K Mutant D-hydantoinase
%K Molecular form
%K Stability<br>重组D-海因酶
%K 突变酶
%K 分子形式
%K 稳定性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=99EA98822AD5B83C&yid=37904DC365DD7266&vid=D997634CFE9B6321&iid=B31275AF3241DB2D&sid=512771C17A2FFC1B&eid=5E7C14876566242F&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=12