Hemiacetal stabilization in a chymotrypsin inhibitor complex and the reactivity of the hydroxyl group of the catalytic serine residue of chymotrypsin

The aldehyde inhibitor Z-Ala-Ala-Phe-CHO has been synthesized and shown by (13)C-NMR to react with the active site serine hydroxyl group of alpha-chymotrypsin to form two diastereomeric hemiacetals. For both hemiacetals oxyanion formation occurs with a pK(a) value of ~ 7 showing that chymotrypsin re...

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Vydáno v:Biochim Biophys Acta Proteins Proteom
Hlavní autoři: Cleary, Jennifer A., Doherty, William, Evans, Paul, Malthouse, J.Paul G.
Médium: Artigo
Jazyk:Inglês
Vydáno: Elsevier B.V. 2014
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Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC7185751/
https://ncbi.nlm.nih.gov/pubmed/24657307
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbapap.2014.03.008
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