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Catalytic and substrate promiscuity: Distinct multiple chemistries catalyzed by the phosphatase domain of receptor protein tyrosine phosphatase
The presence of latent activities in enzymes is posited to underlie the natural evolution of new catalytic functions. However, the prevalence and extent of such substrate and catalytic ambiguity in evolved enzymes is difficult to address experimentally given the order-of-magnitude difference in the...
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| 出版年: | Biochem J |
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| 主要な著者: | , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2016
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| 主題: | |
| オンライン・アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5049700/ https://ncbi.nlm.nih.gov/pubmed/27208174 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BCJ20160289 |
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