LIPOYLATION OF H-PROTEIN OF THE GLYCINE CLEAVAGE SYSTEM - THE EFFECT OF SITE-DIRECTED MUTAGENESIS OF AMINO-ACID-RESIDUES AROUND THE LIPOYLLYSINE RESIDUE ON THE LIPOATE ATTACHMENT
LIPOYLATION OF H-PROTEIN OF THE GLYCINE CLEAVAGE SYSTEM - THE EFFECT OF SITE-DIRECTED MUTAGENESIS OF AMINO-ACID-RESIDUES AROUND THE LIPOYLLYSINE RESIDUE ON THE LIPOATE ATTACHMENT
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DOI：
10.1016/0014-5793(91)81164-4
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发表时间：
1991-11-18
期刊：
影响因子：
3.5
通讯作者：
MOTOKAWA, Y
中科院分区：
文献类型：
--
作者：
FUJIWARA, K;OKAMURAIKEDA, K;MOTOKAWA, Y
甘氨酸裂解系统的 H 蛋白的 Lys59 残基上含有硫辛酸。 对不同来源的H蛋白和α-酮酸脱氢酶复合物的酰基转移酶的硫辛酸附着位点周围的氨基酸序列进行比较表明，牛H蛋白的Gly43、Glu56、Glu63和Gly70在这些蛋白中高度保守。 通过定点诱变对这些保守残基的修饰表明 Glu56 和 Gly70 对于 H 蛋白的脂酰化很重要，并表明硫辛酸附着位点周围的正确构象对于 H 蛋白与负责脂酰化的酶的结合是必需的。
H-protein of the glycine cleavage system has lipoic acid on the Lys59 residue. Comparison of amino acid sequences around the lipoate attachment site of H-proteins from various sources and acyltransferases of alpha-keto acid dehydrogenase complexes indicated that Gly43, Glu56, Glu63 and Gly70 of bovine H-protein are highly conserved among these proteins. Modification of these conserved residues by site-directed mutagenesis indicated that Glu56 and Gly70 are important for the lipoylation of H-protein and suggested that the proper conformation around the lipoic acid attachment site is required for the association of H-protein to the enzyme responsible for the lipoylation.