Determination of the Structure of Tetrahedral Transition State Analogues Bound at the Active Site of Chymotrypsin Using 18O and 2H Isotope Shifts in the 13C NMR Spectra of Glyoxal Inhibitors-Reference-Cited by-同舟云学术

Determination of the Structure of Tetrahedral Transition State Analogues Bound at the Active Site of Chymotrypsin Using 18O and 2H Isotope Shifts in the 13C NMR Spectra of Glyoxal Inhibitors

Published:2007-10-10 Issue:44 Volume:46 Page:12868-12874
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Spink Edward¹,Hewage Chandralal¹,Malthouse J. Paul G.¹

Affiliation:

1. UCD School of Biomolecular and Biomedical Science, Centre for Synthesis and Chemical Biology, UCD Conway Institute, University College Dublin, Dublin 4, Ireland

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi701212u

Reference25 articles.

1. 13C-NMR study of the inhibition of δ-chymotrypsin by a tripeptide-glyoxal inhibitor

2. A 13C-NMR study of the inhibition of papain by a dipeptide-glyoxal inhibitor

3. A study of the stabilization of tetrahedral adducts by trypsin and δ-chymotrypsin

4. 13C- and 1H-NMR studies of oxyanion and tetrahedral intermediate stabilization by the serine proteinases: optimizing inhibitor warhead specificity and potency by studying the inhibition of the serine proteinases by peptide-derived chloromethane and glyoxal inhibitors

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