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Figure 1
The suggested catalytic mechanism of endothiapepsin. A water molecule bound to Asp32 and Asp215 nucleophilically attacks the scissile-bond carbonyl. A tetrahedral intermediate is then generated and stabilized by hydrogen bonds. The C—N bond is cleaved by transferring a proton to the amino group. Hydrogen bonds are indicated by dotted lines.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 70| Part 1| December 2014| Pages 30-33
doi:10.1107/S2053230X13032974
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