<B>ABSTRACT</B><P>To study the pH dependence ofl-arabinose isomerase (AI) activity and stability, we compared homologous AIs with their chimeras. This study demonstrated that an ionizable amino acid near the catalytic site determines...
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https://www.riss.kr/link?id=A107614089
2012
-
SCI,SCIE,SCOPUS
학술저널
8813-8816(4쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
<B>ABSTRACT</B><P>To study the pH dependence ofl-arabinose isomerase (AI) activity and stability, we compared homologous AIs with their chimeras. This study demonstrated that an ionizable amino acid near the catalytic site determines...
<B>ABSTRACT</B><P>To study the pH dependence ofl-arabinose isomerase (AI) activity and stability, we compared homologous AIs with their chimeras. This study demonstrated that an ionizable amino acid near the catalytic site determines the optimal pH (pHopt) for activity, whereas the N-terminal surface R residues play an important role in determining the pHoptfor stability.</P>