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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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Glavni autori: | , , , , , , , |
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Format: | Artigo |
Jezik: | Inglês |
Izdano: |
Cold Spring Harbor Laboratory Press
2008
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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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