X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate
X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate
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New York: Nature Publishing Group US
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English
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New York: Nature Publishing Group US
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Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues. An oxyanion hole, consisting of the peptide amide...
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X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate
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TN_cdi_proquest_journals_228338124
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_228338124
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ISSN
1072-8368,1545-9993
E-ISSN
1545-9985
DOI
10.1038/90401
