Replacement of C305 in heart/ muscle-type isozyme of human carnitine palmitoyltransferase I with aspartic acid and other amino acids
Replacement of C305 in heart/ muscle-type isozyme of human carnitine palmitoyltransferase I with aspartic acid and other amino acids
复制标题
用天冬氨酸和其他氨基酸替代人肉碱棕榈酰转移酶 I 心脏/肌肉型同工酶中的 C305
DOI：
10.1007/s10528-009-9301-z
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发表时间：
2010
期刊：
影响因子：
2.4
通讯作者：
Shinohara Y
中科院分区：
文献类型：
--
作者：
Matsuo T;Yamamoto A;Yamamoto T;Otsuki K;Yamazaki N;Kataoka M;Terada H;Shinohara Y
肝和心脏/肌肉型的人肉毒碱棕榈酰转移酶I（L-和M-CPTI，分别）的同工酶显示在其氨基酸序列的一定的相似性，和这两种同工酶之间的保守氨基酸的突变研究往往显示基本上相同的影响，其酶的性质。早期对人M-CPTI中C305及其对应残基C304的突变研究显示了突变的不同影响，特别是在酶稳定性方面;然而，对L-和M-CPTI之间保守Cys残基的这些影响进行简单比较是困难的，因为这些研究是使用不同的表达系统和不同的氨基酸作为替代进行的。本研究以COS细胞为表达系统，对人M-CPTI基因C305进行了突变研究。我们的研究结果表明，C305是可替换的天冬氨酸，但与其他氨基酸的取代引起功能丧失和表达减少。
Liver- and heart/muscle-type isozymes of human carnitine palmitoyltransferase I (L- and M-CPTI, respectively) show a certain similarity in their amino acid sequences, and mutation studies on the conserved amino acids between these two isozymes often show essentially the same effects on their enzymatic properties. Earlier mutation studies on C305 in human M-CPTI and its counterpart residue, C304, in human L-CPTI showed distinct effects of the mutations, especially in the aspect of enzyme stability; however, simple comparison of these effects on the conserved Cys residue between L- and M-CPTI was difficult, because these studies were carried out using different expression systems and distinct amino acids as replacements. In the present study, we carried out mutation studies on the C305 in human M-CPTI using COS cells for the expression system. Our results showed that C305 was replaceable with aspartic acid but that substitution with other amino acids caused both loss of function and reduced expression.