The nature of the ligand's side chain interacting with the S1'-subsite of metallocarboxypeptidase T (from Thermoactinomyces vulgaris) determines the geometry of the tetrahedral transition complex.
The carboxypeptidase T (CPT) from Thermoactinomyces vulgaris has an active site structure and 3D organization similar to pancreatic carboxypeptidases A and B (CPA and CPB), but differs in broader substrate specificity. The crystal structures of CPT complexes with the transition state analogs N-sulfa...
Main Authors: | , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2019-01-01
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Series: | PLoS ONE |
Online Access: | https://doi.org/10.1371/journal.pone.0226636 |