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...

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Detalles Bibliográficos
Autores principales: Akparov, Valery Kh., Timofeev, Vladimir I., Konstantinova, Galina E., Khaliullin, Ilyas G., Kuranova, Inna P., Rakitina, Tatiana V., Švedas, Vytas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6937156/
https://www.ncbi.nlm.nih.gov/pubmed/31887148
http://dx.doi.org/10.1371/journal.pone.0226636

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6937156/
https://www.ncbi.nlm.nih.gov/pubmed/31887148
http://dx.doi.org/10.1371/journal.pone.0226636

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