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  • 1
    Electronic Resource
    Electronic Resource
    Model studies on carboxypeptidase Y catalyzed peptide synthesis in an aqueous-organic two-phase system (1983)
    Springer
    Monatshefte für Chemie 114 (1983), S. 343-347 
    Details
    ISSN: 1434-4475
    Keywords: Carboxypeptidase Y catalyzed peptide bond formation ; Enzymic synthesis in biphasic systems ; Peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung Carboxypeptidase Y katalysiert in einem Zweiphasensystem aus Tetrachlormethan und Carbonatpuffer die Reaktion vonZ-Phe-OMe und verschiedenenZ- undBoc-geschützten Dipeptidmethylestern mit Val-NH2 bzw. Leu-NH2. Nach diesem Verfahren werden die entsprechenden N-geschützen Tripeptidamide in präparativem Maßstab hergestellt. Bei einem Substrat-Nucleophil-Verhältnis von nur 1:2 oder 1:3 erhält man die Peptidderivate in Ausbeuten von 56–97%.
    Notes: Abstract Carboxypeptidase Y catalyzes in a biphasic system containing carbon tetrachloride and carbonate buffer the reaction ofZ-Phe-OMe and variousZ-andBoc-protected dipeptide methyl esters with Val-NH2 and Leu-NH2, respectively. This method has been applied to the synthesis of the corresponding N-protected tripeptide amides on a preparative scale. Using a substrate—nucleophile ratio of only 1:2 or 1:3 the peptide derivatives are obtained in yields of 56–97%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00798957
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  • 2
    Electronic Resource
    Electronic Resource
    Protease-catalyzed peptide synthesis using inverse substrates: The influence of reaction conditions on the trypsin acyl transfer efficiency (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 104-108 
    Details
    ISSN: 0006-3592
    Keywords: protease ; acyl transfer ; nucleophile efficiency ; inverse substrates ; trypsin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Benzyloxycarbonyl-L-alanine p-guanidinophenyl ester behaves as a trypsin “inverse substrate,” i.e., a cationic center is included in the leaving group instead of being in the acyl moiety. Using this substrate as an acyl donor, trypsin catalyzes the synthesis of peptide bonds that cannot be split by this enzyme. An optimal acyl transfer efficiency was achieved between pH 8 and 9 at 30°C.The addition of as much as 50% cosolvent was shown to be of minor influence on the acyl transfer efficiency, whereas the reaction velocity decreases by more than one order of magnitude. The efficiency of H-Leu-NH2 and H-Val-NH2 in deacylation is almost the same for “inverse” and normal type substrates.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260380114
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Protease-catalyzed peptide synthesis using inverse substrates: The synthesis of Pro-Xaa-bonds by trypsin (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 319-321 
    Details
    ISSN: 0006-3592
    Keywords: Protease ; acyl transfer ; nucleophile efficiency ; inverse substrates ; trypsin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Benzyloxycarbonyl-L-proline p-guanidinophenyl ester is an “inverse substrate” for trypsin; i.e., the cationic center is included in the leaving group instead of being in the acyl moiety. This substrate can be used in trypsin-catalyzed acyl-transfer reactions leading to the synthesis of Pro-Xaa peptide bonds. The reaction proceeds about 20 times slower than reaction with similar alanine-containing substrates, but the ratio between synthesis and hydrolysis is more favorable. The investigation of a series of nucleophiles led to information about the specificity of the process. Nucleophiles differing only in the P1′-position show an increasing acyl transfer efficiency in the order Phe 〈 Gly 〈 Ley 〈 Ser 〈 Ala 〈 lle. C terminal elongation of the nucleophiles is of minor influence on their efficiency. The formation of an H bond between the acyl-enzyme and the nucleophile seems to play an important role in the aminolysis of the acyl-enzyme.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260380314
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    Paper (German National Licenses)
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