Prolyl Isomerases Show Low Sequence Specificity toward the Residue Following the Proline

Philipp A. M. Schmidpeter Gunther Jahreis Anne-Juliane Geitner and Franz X. Schmid

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Prolyl Isomerases Show Low Sequence Specificity toward the Residue Following the Proline

机译：脯氨酰异构酶对脯氨酸后的残基显示较低的序列特异性

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Prolyl isomerases catalyze the cis/trans isomerization of peptidenbonds preceding proline. Previously, we had determined the speciﬁcity towardnthe residue before the proline for cyclophilin-, FKBP-, and parvulin-type prolylnisomerases by using proline-containing oligopeptides and refolding proteins asnmodel substrates. Here, we report the speciﬁcities of members of these three prolylnisomerase families for the residue following the proline, again in short peptide and innrefolding protein chains. Human cyclophilin 18 and parvulin 10 from Escherichia colinshow high activity, but low speciﬁcity, with respect to the residue following thenproline.Human FKBP12 prefers hydrophobic residues at this position in the peptidenassays and shows a very low activity in the protein folding assays. This activity was strongly improved, and the sequence speciﬁcitynwas virtually eliminated after the insertion of a chaperone domain into the prolyl isomerase domain of human FKBP12.

机译：脯氨酰异构酶催化脯氨酸之前的肽键的顺式/反式异构化。以前，我们已经通过使用含脯氨酸的寡肽和可折叠蛋白作为模型的底物，确定了脯氨酸对亲环蛋白，FKBP和小白蛋白型脯氨酸异构酶的残基特异性。在这里，我们报告了这三个脯氨酰异构酶家族成员对脯氨酸后，短肽和未折叠蛋白链中残基的特异性。大肠杆菌中的人亲环蛋白18和小白蛋白10相对于脯氨酸后的残基表现出高活性，但特异性低。人FKBP12在肽分析中此位置偏爱疏水性残基，在蛋白质折叠分析中显示出非常低的活性。在将伴侣结构域插入人FKBP12的脯氨酰异构酶结构域后，该活性得到了极大的改善，并且几乎消除了序列特异性。

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《Biochemistry》 |2011年第21期|p.4796-4803|共8页
作者
Philipp A. M. Schmidpeter Gunther Jahreis Anne-Juliane Geitner and Franz X. Schmid;
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†Laboratorium f€ ur Biochemie und Bayreuther Zentrum f€ ur Molekulare Biowissenschaften, Universit€ at Bayreuth, D-95440 Bayreuth,Germany‡Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany;

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1. Prolyl Isomerases Show Low Sequence Specificity toward the Residue Following the Proline [J] . Philipp A. M. Schmidpeter, Gunther Jahreis, Anne-Juliane Geitner, Biochemistry . 2011,第21期

机译：脯氨酸异构酶显示脯氨酸后残留物的低序列特异性
2. Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues [J] . Scholz C., Rape M., Pecht A., Journal of Molecular Biology . 1998,第3期

机译：脯氨酰异构酶触发因子对蛋白质底物的识别与脯氨酸残基无关
3. CHARACTERIZATION OF THE SLOW FOLDING REACTIONS OF TRP APOREPRESSOR FROM ESCHERICHIA COLI BY MUTATIONAL ANALYSIS OF PROLINES AND CATALYSIS BY A PEPTIDYL-PROLYL ISOMERASE [J] . Mann CJ., Matthews CR., Shao X. Biochemistry . 1995,第44期

机译：脯氨酸的突变分析和肽基-脯氨酸异构酶催化表征大肠杆菌中TRP阻抑剂的慢折叠反应
4. Molecular Cloning and Sequence Analysis of the Carotenoid Isomerase Gene in Yellow-Flower Chinese Kale [C] . Min Jiang, Qiao Yuan, Hao Zheng, International Conference on Frontiers of Biological Sciences and Engineering . 2019

机译：黄花羽衣甘蓝类胡萝卜素异构酶基因的分子克隆及序列分析
5. Bioinformatics driven studies of aspartate aminotransferase substrate specificity and distal residues in triosephosphate isomerase [D] . Mertz, Robert Wesley 2015

机译：生物信息学驱动的三糖磷酸异构酶中天冬氨酸转氨酶底物特异性和末端残基的研究
6. Proline substitutions in a Mip-like peptidyl-prolyl cis-trans isomerase severely affect its structure stability shape and activity [O] . Soumitra Polley, Devlina Chakravarty, Gopal Chakrabarti, 2015

机译：Mip样肽基脯氨酰顺反异构酶中的脯氨酸取代严重影响其结构稳定性形状和活性
7. Proline substitutions in a Mip-like peptidyl-prolyl cis-trans isomerase severely affect its structure, stability, shape and activity [O] . Soumitra Polley, Devlina Chakravarty, Gopal Chakrabarti, 2015

机译：mip样肽基 - 脯氨酰顺反异构酶中的脯氨酸取代严重影响其结构，稳定性，形状和活性

Prolyl Isomerases Show Low Sequence Specificity toward the Residue Following the Proline

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