Assembly of an active enzyme by the linkage of two protein modules

A. E. Nixon; M. S. Warren; S. J. Benkovic

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Assembly of an active enzyme by the linkage of two protein modules

机译：通过两个蛋白质模块的连接来组装活性酶

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The feasibility of creating new enzyme activ- ities from enzymes of known function has precedence in view of protein evolution based on the concepts of molecular recruitment and exon shuffling. The enzymes encoded by the Escherichia coli genes purU and purN, N~10-formyltetrahydro- folate hydrolase and glycinamide ribonucleotide (GAR) trans- formylase, respectively, catalyze similiar yet distinct reactions. N~10-formyltetrahydrofolate hydrolase uses water to cleave N~10-formyltetrahydrofolate into tetrahydrofolate and for- mate, whereas GAR transformylase catalyses the transfer of formyl from N~10-formyltetrahydrofolate to GAR to yield formyl-GAR and tetrahydrofolate.

机译：考虑到基于分子募集和外显子改组的蛋白质进化，从已知功能的酶产生新的酶活性的可行性优先。大肠杆菌基因purU和purN，N〜10-甲酰基四氢叶酸水解酶和甘氨酰胺核糖核苷酸（GAR）转甲酰化酶编码的酶分别催化相似但截然不同的反应。 N〜10-甲酰基四氢叶酸水解酶用水将N〜10-甲酰基四氢叶酸裂解为四氢叶酸并形成甲酸酯，而GAR转化酶则催化甲酰基从N〜10-甲酰基四氢叶酸向GAR的转移，生成甲酰基-GAR和四氢叶酸。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1997年第4期|p.1069-1073|共5页
作者
A. E. Nixon; M. S. Warren; S. J. Benkovic;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类自然科学总论;
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Assembly of an active enzyme by the linkage of two protein modules

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