Journal article
Evaluation of the Ser-His Dipeptide, a Putative Catalyst of Amide and Ester Hydrolysis.
- MacDonald MJ Department of Chemistry, University of Wisconsin-Madison , Wisconsin 53706, United States.
- Lavis LD Janelia Research Campus, Howard Hughes Medical Institute , Ashburn, Virginia 20147, United States.
- Hilvert D Laboratory of Organic Chemistry, ETH Zürich , 8093 Zürich, Switzerland.
- Gellman SH Department of Chemistry, University of Wisconsin-Madison , Wisconsin 53706, United States.
- 2016-07-12
Published in:
- Organic letters. - 2016
English
Efficient hydrolysis of amide bonds has long been a reaction of interest for organic chemists. The rate constants of proteases are unmatched by those of any synthetic catalyst. It has been proposed that a dipeptide containing serine and histidine is an effective catalyst of amide hydrolysis, based on an apparent ability to degrade a protein. The capacity of the Ser-His dipeptide to catalyze the hydrolysis of several discrete ester and amide substrates is investigated using previously described conditions. This dipeptide does not catalyze the hydrolysis of amide or unactivated ester groups in any of the substrates under the conditions evaluated.
- Language
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- English
- Open access status
- closed
- Identifiers
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- DOI 10.1021/acs.orglett.6b01279
- PMID 27400366
- Persistent URL
- https://sonar.ch/global/documents/140270
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