Effects of pH on carboxypeptidase-Y-catalyzed hydrolysis and aminolysis reactions
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چکیده
منابع مشابه
Carboxypeptidase S-1 from Penicillium janthinellum: enzymatic properties in hydrolysis and aminolysis reactions.
Carboxypeptidase S-1 from Penicillium janthinellum has been isolated by affinity chromatography and characterized. The enzyme activity is unusually stable in organic solvents, e.g. 80% methanol. The hydrolysis of peptide substrates is apparently dependent on three ionizable groups. One group, with pKa of 4.0-4.5, is a catalytically essential residue in its deprotonated form, and another group w...
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Malt carboxypeptidase catalyzes the formation of peptide bonds using N-benzoyl-arginine esters as acyl components and amino acid amides or amino acid methyl esters as nucleophiles. With seven different nucleophiles yields of 5095% were obtained while no aminolysis was observed with H-Pro-NH2 and H-GIu-a-NH2. The enzyme is easily saturated with nucleophile indicating the formation of a complex b...
متن کاملEnzymatic Peptide Synthesis. Carboxypeptidase Y Catalyzed Formation of Peptide Bonds
It is demonstrated that carboxypeptidase Y from Saccharomyces cerevisiae can catalyze the formation of peptide bonds using N-acylamino acid esters as substrates and free amino acids or amino acid amides as nucleophiles, The coupling yields observed with free amino acids were max. 60 % for alanine and lysine and they depended strongly on the reaction parameters; viz. pH, temperature and concentr...
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this study compared the different effects of form-focused guided planning vs. meaning-focused guided planning on iranian pre-intermediate students’ task performance. the study lasted for three weeks and concentrated on eight english structures. forty five pre-intermediate iranian students were randomly assigned to three groups of guided planning focus-on-form group (gpfg), guided planning focus...
15 صفحه اولRegulation of carboxypeptidase E. Effect of pH, temperature and Co2+ on kinetic parameters of substrate hydrolysis.
Carboxypeptidase E is a member of the carboxypeptidase A and B gene family, with many of the putative active-site and substrate-binding residues conserved between these enzymes. However, the pH optimum of carboxypeptidase E is substantially lower than that of carboxypeptidases A and B. To evaluate whether the difference in the pH optima of these carboxypeptidases reflects fundamental difference...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1994
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1994.tb18609.x