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Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

This paper reports that the acetylation of lysine ε-NH(3) (+) groups of α-amylase—one of the most important hydrolytic enzymes used in industry—produces highly negatively charged variants that are enzymatically active, thermostable, and more resistant than the wild-type enzyme to irreversible inacti...

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Bibliografski detalji
Glavni autori: Shaw, Bryan F., Schneider, Gregory F., Bilgiçer, Başar, Kaufman, George K., Neveu, John M., Lane, William S., Whitelegge, Julian P., Whitesides, George M.
Format: Artigo
Jezik:Inglês
Izdano: Cold Spring Harbor Laboratory Press 2008
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2492826/
https://ncbi.nlm.nih.gov/pubmed/18451358
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.035154.108
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