A 13C-NMR study of the role of Asn-155 in stabilizing the oxyanion of a subtilisin tetrahedral adduct.

By removing one of the hydrogen-bond donors in the oxyanion hole of subtilisin BPN, we have been able to determine how it affects the catalytic efficiency of the enzyme and the pKa of the oxyanion formed in a choloromethane inhibitor derivative. Variant 8397 of subtilisin BPN contains five mutations...

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Hauptverfasser: O'connell, T P, Day, R M, Torchilin, E V, Bachovchin, W W, Malthouse, J G
Format: Artigo
Sprache:Inglês
Veröffentlicht: 1997
Schlagworte:
Research Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1218743/
https://ncbi.nlm.nih.gov/pubmed/9307038
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