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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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Detalhes bibliográficos
Publicado no:Biochem J
Main Authors: Srinivasan, Bharath, Marks, Hanna, Mitra, Sreyoshi, Smalley, David M., Skolnick, Jeffrey
Formato: Artigo
Idioma:Inglês
Publicado em: 2016
Assuntos:
Acesso em linha: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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