维生素K依赖蛋白C中的β-羟基天冬氨酸
beta-Hydroxyaspartic acid in vitamin K-dependent protein C.
作者信息
Drakenberg T, Fernlund P, Roepstorff P, Stenflo J
出版信息
Proc Natl Acad Sci U S A. 1983 Apr;80(7):1802-6. doi: 10.1073/pnas.80.7.1802.
Abstract
Previous work has shown that the light chain of protein C, an anticoagulant plasma protein, contains an unusual amino acid [Fernlund, P. & Stenflo, J. (1982) J. Biol. Chem. 257, 12170-12179]. To determine the structure of this amino acid a heptapeptide, CMCys-Ile-X-Gly-Leu-Gly-Gly (residues 69-75 in the light chain), was isolated from enzymatic digests of the light chain. According to automatic Edman sequence analysis, 1H NMR spectroscopy, and mass spectrometry the heptapeptide had beta-hydroxyaspartic acid in its third position, which corresponds to position 71 in the light chain of protein C. Analysis of acid and aminopeptidase M hydrolysates of the heptapeptide showed the beta-hydroxyaspartic acid to be the erythro form. Acid hydrolysis of protein C released approximately equal to 1 mol of beta-hydroxyaspartic acid per mol of protein. The function of this amino acid, which, to the best of our knowledge, has not been found previously in proteins, is unknown.
摘要
先前的研究表明，抗凝血浆蛋白C的轻链含有一种不寻常的氨基酸[费恩隆德，P. & 斯滕弗洛，J. (1982) 《生物化学杂志》257, 12170 - 12179]。为了确定这种氨基酸的结构，从该轻链的酶解产物中分离出一种七肽，即CMCys-Ile-X-Gly-Leu-Gly-Gly（轻链中的第69 - 75位残基）。根据自动埃德曼序列分析、1H核磁共振光谱和质谱分析，该七肽的第三位含有β-羟基天冬氨酸，这与蛋白C轻链中的第71位相对应。对该七肽的酸水解产物和氨肽酶M水解产物的分析表明，β-羟基天冬氨酸为赤藓糖型。蛋白C的酸水解每摩尔蛋白释放出约1摩尔的β-羟基天冬氨酸。据我们所知，这种氨基酸此前在蛋白质中从未被发现，其功能尚不清楚。
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