A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase

The active sites of aminopeptidase A (PepA) from Escherichia coli and leucine aminopeptidase from bovine lens are isostructural, as shown by x-ray structures at 2.5 Å and 1.6 Å resolution, respectively. In both structures, a bicarbonate anion is bound to an arginine side chain (Arg-356 in PepA and A...

Полное описание

Библиографические подробности

Опубликовано в::	Proc Natl Acad Sci U S A
Главные авторы:	Sträter, Norbert, Sun, Lee, Kantrowitz, E. R., Lipscomb, William N.
Формат:	Artigo
Язык:	Inglês
Опубликовано:	National Academy of Sciences 1999
Предметы:	Biological Sciences
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC18002/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10500145/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.20.11151
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