descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1994 English Publisher:Elsevier BVJournal:International Journal of Biochemistry, volume 26, pages 35-42 (issn: 0020-711X,

Authors: Mahmoud Balbaa; Max Blum; Theo Hofmann;

doi: 10.1016/0020-711x(94)90192-9

pmid: 8138045

Mechanism of pepsin-catalyzed aminotranspeptidation reactions

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Abstract

1. The tetrapeptide Ala2-Nph2 (where Nph = p-nitrophenylalanyl) is treated by porcine pepsin to study the mechanism of aminotranspeptidation reactions. 2. The major initial product is Ala2-Nph and the major transpeptidation products are Nph2 and Nph3 accompanied by some Nph, a little Nph4, Ala2-Nph3 and Ala2-Nph4. 3. Oligomers of Nph greater than tetramers are formed near the end of the reaction. 4. In presence of [3H]Nph, no incorporation of Nph into the transpeptidation products is observed. 5. 18O-labeling shows extensive incorporation of 18O atoms from [18O]water in the carbonyl oxygens of Nph residues.

Related Organizations

University of Toronto
Canada
Alexandria University
Egypt

Keywords

Swine, Phenylalanine, Molecular Sequence Data, Animals, Amino Acid Sequence, Amino Acids, Oxygen Isotopes, Catalysis, Chromatography, High Pressure Liquid, Pepsin A

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