Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins.
Glutathione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins.
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谷胱甘肽依赖性前列腺素 D 合酶作为设计新功能蛋白的先导分子。
DOI：
10.1093/protein/9.12.1067
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
O. Hayaishi
中科院分区：
文献类型：
--
作者：
Hiroyuki Toh;Hideo Kubodera;Nobuyuki Nakajima;Tetsuo Sekiya;N. Eguchi;Toshiki Tanaka;Yoshihiro Urade;O. Hayaishi
The functional and structural information of a protein is encoded by its amino acid sequence. One of the goals of protein engineering is to establish methods to design amino acid sequences that exert desired catalytic functions. To this end, numerous attempts have been made, but the rational design of catalytic function is far from becoming a practical application.On the other hand, living organisms have a wide variety of proteins with various functions, which are considered to have been generated from small numbers of ancestral genes by gene duplication and subsequent functional divergence during the course of molecular evolution. The presence of an additional copy of a gene generated by gene duplication would have allowed either the original or the copy to accept mutations that would have been deleterious for the single gene. Most of the changes in the mutated gene would have prevented expression of the gene product, ie a pseudogene would have been formed. A small number of them, however, would have been involved in the creation of new functions, and the trial and error process would have brought about a functional variety of present day proteins.
