Investigations on the Enzyme Specificity of Clostripain: A New Efficient Biocatalyst for the Synthesis of Peptide Isosteres-Reference-Cited by-同舟云学术

Investigations on the Enzyme Specificity of Clostripain: A New Efficient Biocatalyst for the Synthesis of Peptide Isosteres

Published:2000-03-01 Issue:6 Volume:65 Page:1672-1679
ISSN:0022-3263
Container-title:The Journal of Organic Chemistry
language:en
Short-container-title:J. Org. Chem.

Author:

Günther Robert¹,Stein Anja¹,Bordusa Frank¹

Affiliation:

1. Max-Planck Society, Research Unit “Enzymology of Protein Folding”, Weinbergweg 22, D-06120 Halle/Saale, Germany, and Department of Biochemistry, Faculty of Biosciences, Pharmacy and Psychology, University of Leipzig, Talstrasse 33, D-04103 Leipzig, Germany

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jo991302q

Reference38 articles.

1. Proteasekatalysierte kinetisch kontrollierte Peptidsynthese

2. Enzymatic Catalysts in Organic Synthesis

3. A Designed Peptide Ligase for Total Synthesis of Ribonuclease A with Unnatural Catalytic Residues

4. (d) Wong, C.H.; Whitesides, G. M.Enzymes inSynthetic Organic Chemistry; Pergamon: Oxford, 1994; pp 41−130 and references therein.

5. Influence of the structure of amine components on carboxypeptidase Y catalyzed amide bond formation

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