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Results 1 - 10 of 25 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6753046 Carboxypeptidase D is the only enzyme responsible for antibody C-terminal lysine cleavage in Chinese hamster ovary (CHO) cells Biotechnol. Bioeng. 113 2100-2106 2016 Cricetulus griseus 26989081
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6732160 Amyloid formation by human carboxypeptidase D transthyretin-like domain under physiological conditions J. Biol. Chem. 289 33783-33796 2014 Homo sapiens 25294878
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6647192 Carboxypeptidases C and D Methods Enzymol. 244 231-248 1994 Saccharomyces cerevisiae 7845212
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6647192 Carboxypeptidases C and D Methods Enzymol. 244 231-248 1994 Triticum aestivum 7845212
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6667510 Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells Biochem. J. 390 665-673 2005 Homo sapiens 15918796
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6667510 Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells Biochem. J. 390 665-673 2005 Rattus norvegicus 15918796
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6647241 Characterization of Drosophila carboxypeptidase D J. Biol. Chem. 277 49613-49620 2002 Drosophila melanogaster 12393882
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6669448 Characterization of the molecular basis of the Drosophila mutations in carboxypeptidase D. Effect on enzyme activity and expression J. Biol. Chem. 281 13844-13852 2006 Drosophila melanogaster 16556608
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6647233 Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae Biochemistry 36 9002-9012 1997 Saccharomyces cerevisiae 9220988
Display the word mapDisplay the reaction diagram Show all sequences 3.4.16.6647236 Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae Protein Sci. 5 395-397 1996 Saccharomyces cerevisiae 8745419
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