Substrate recognition mechanism of carboxypeptidase Y

To clarify the substrate-recognition mechanism of carboxypeptidase Y, Fmoc-(Glu) sub(n)Ala-OH (n = 1 to 6), Fmoc-(Glu) sub(n )Ala-NH2 (1 to 5), and Fmoc-Lys(Glu) sub(3) Ala-NH2 were synthesized, and kinetic parameters for these substrates were measured. K sub(m) for Fmoc-peptides significantly decre...

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Veröffentlicht in:	Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2001-11, Vol.65 (11), p.2465-2471
Hauptverfasser:	Nakase, H. (Kyoto Univ. (Japan)), Murata, S, Ueno, H, Hayashi, R
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - chemistry Binding Sites Biological and medical sciences Biotechnology carboxypeptidase Y Carboxypeptidases - genetics Carboxypeptidases - metabolism Cathepsin A ENZYME ACTIVITY Fluorenes - chemistry Fmoc-peptide Fmoc-peptide amide Fundamental and applied biological sciences. Psychology Kinetics Mutagenesis, Site-Directed Oligopeptides - chemistry PEPTIDES PROTEASES SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Spectrometry, Fluorescence subsite affinity substrate recognition mechanism Substrate Specificity
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