<P><B>Abstract</B></P><P>In <I>Arabidopsis</I>, there are at least seven class I acylhydrolase members, which have a putative N-terminal chloroplast-targeting signal. Here, we show that all seven class I prote...
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https://www.riss.kr/link?id=A107602229
2009
-
SCOPUS,SCIE
학술저널
2301-2307(7쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
<P><B>Abstract</B></P><P>In <I>Arabidopsis</I>, there are at least seven class I acylhydrolase members, which have a putative N-terminal chloroplast-targeting signal. Here, we show that all seven class I prote...
<P><B>Abstract</B></P><P>In <I>Arabidopsis</I>, there are at least seven class I acylhydrolase members, which have a putative N-terminal chloroplast-targeting signal. Here, we show that all seven class I proteins are localized to the chloroplasts and hydrolyze phosphatidylcholine at the <I>sn</I>-1 position. However, based on their activities toward various lipids, <I>Arabidopsis</I> class I enzymes could be further divided into three sub-groups by substrate specificity, one with phospholipase-specific activity, another with phospholipase and galactolipase activities, and the other with broad lipolytic activity toward phosphatidylcholine, galactolipids, and triacylglycerol. These results suggest that the three sub-groups of class I acylhydrolases have specific roles in chloroplasts.</P>
Subcellular localization of rice histone deacetylases in organelles