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Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae.
Shilton BH, Li Y, Tessier D, Thomas DY, Cygler M. Shilton BH, et al. Protein Sci. 1996 Feb;5(2):395-7. doi: 10.1002/pro.5560050225. Protein Sci. 1996. PMID: 8745419 Free PMC article.
Molecular replacement models have been built based on the structures of wheat serine carboxypeptidase (CPDW-II; Liao DI et al., 1992, Biochemistry 31:9796-9812) and yeast carboxypeptidase Y....
Molecular replacement models have been built based on the structures of wheat serine carboxypeptidase (CPDW-II; Liao DI et al., 19
Effects of pH on carboxypeptidase-Y-catalyzed hydrolysis and aminolysis reactions.
Christensen U. Christensen U. Eur J Biochem. 1994 Feb 15;220(1):149-53. doi: 10.1111/j.1432-1033.1994.tb18609.x. Eur J Biochem. 1994. PMID: 8119282 Free article.
The results reveal two catalytically important ionizing groups of the enzyme with rather similar pK values (5-6), the active site His397 and a possibly Glu residue, which is not only important in interactions with carboxylic groups of substrates and nucleophiles [Liao, D.- …
The results reveal two catalytically important ionizing groups of the enzyme with rather similar pK values (5-6), the active site His397 and …