真核红藻皱波角叉菜中黄素氧还蛋白的氨基酸序列。
The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus.
作者信息
Wakabayashi S, Kimura T, Fukuyama K, Matsubara H, Rogers L J
机构信息
Department of Biology, Faculty of Science, Osaka University, Japan.
出版信息
Biochem J. 1989 Nov 1;263(3):981-4. doi: 10.1042/bj2630981.
The amino acid sequence of the constitutive flavodoxin from the red alga Chondrus crispus was determined from the analyses of peptide fragments derived by enzymic digestions of the carboxymethylated protein. This is the first sequence reported for a flavodoxin from a eukaryote. The protein is composed of 173 amino acid residues and is a member of the longer-chain group of flavodoxins. The extent of sequence homology to the three other flavodoxins in the group for which sequences are available is in the range 36-39%, with the most strongly conserved regions being those implicated in binding of the FMN, the redox-active prosthetic group. Nevertheless, Chondrus crispus flavodoxin stands apart in a number of respects, in particular the possession of an unusually high content of proline, with these residues distributed more or less regularly along the peptide chain.
通过对羧甲基化蛋白质酶解产生的肽片段进行分析，确定了红藻皱波角叉菜组成型黄素氧还蛋白的氨基酸序列。这是首次报道的真核生物黄素氧还蛋白序列。该蛋白质由173个氨基酸残基组成，是黄素氧还蛋白较长链组的成员。与该组中其他三种已知序列的黄素氧还蛋白的序列同源程度在36%-39%之间，其中保守性最强的区域是与氧化还原活性辅基FMN结合有关的区域。然而，皱波角叉菜黄素氧还蛋白在许多方面有所不同，特别是脯氨酸含量异常高，这些残基沿肽链或多或少呈规则分布。
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