新生原胶原蛋白中的β-转角是脯氨酸翻译后酶促羟化的位点。
Beta-turns in nascent procollagen are sites of posttranslational enzymatic hydroxylation of proline.
作者信息
Brahmachari S K, Ananthanarayanan V S
出版信息
Proc Natl Acad Sci U S A. 1979 Oct;76(10):5119-23. doi: 10.1073/pnas.76.10.5119.
Abstract
The selective hydroxylation of proline residues in nascent procollagen chains by prolyl hydroxylase (EC 1.14.11.2) can be understood in terms of the conformational feature of the -Pro-Gly-segments in linear peptides and globular proteins. The folded beta-turn conformation in such segments appears to be the conformational requirement for proline hydroxylation. The available data on the hydroxylation of native and synthetic substrates of prolyl hydroxylase are explained on the basis of the extent of beta-turn formation in them. Taken in conjunction with the conformational features of the hydroxyproline residue, our results bring out the conformational reason for the posttranslational proline hydroxylation which, it is proposed, leads to the "straightening" of the beta-turn segments into the linear triple-helical conformation.
摘要
脯氨酰羟化酶（EC 1.14.11.2）对新生原胶原链中脯氨酸残基的选择性羟基化作用，可以根据线性肽和球状蛋白中-Pro-Gly-片段的构象特征来理解。此类片段中折叠的β-转角构象似乎是脯氨酸羟基化的构象要求。脯氨酰羟化酶天然底物和合成底物羟基化的现有数据，是根据它们中β-转角形成的程度来解释的。结合羟脯氨酸残基的构象特征，我们的结果揭示了翻译后脯氨酸羟基化的构象原因，据推测，这种羟基化会导致β-转角片段“伸直”成为线性三螺旋构象。
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