Substrate Specificities of Porcine and Bovine Enteropeptidases toward the Peptide Val-(Asp)4-Lys-Ile-Val-Gly and Its Analogs

Yong-Tae KIM; Wataru NISHII; Masashi MATSUSHIMA; Hideshi INOUE; Hisashi ITO; Sun Joo PARK; Kenji TAKAHASHI

doi:10.1271/bbb.70732

This article has now been updated. Please use the final version.

Substrate Specificities of Porcine and Bovine Enteropeptidases toward the Peptide Val-(Asp)₄-Lys-Ile-Val-Gly and Its Analogs

Yong-Tae KIM, Wataru NISHII, Masashi MATSUSHIMA, Hideshi INOUE, Hisashi ITO, Sun Joo PARK, Kenji TAKAHASHI

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Keywords: enteropeptidase, substrate specificity, synthetic peptide substrates, trypsinogen activation peptide

JOURNAL FREE ACCESS Advance online publication

Article ID: 70732

DOI https://doi.org/10.1271/bbb.70732

The final version of this article is now available: Vol. 72 (2008) , No. 3 p.905

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Abstract

The substrate specificities of porcine and bovine enteropeptidases were investigated using the peptide Val-(Asp)₄-Lys-Ile-Val-Gly and its various analogs with mutations in the (Asp)₄-Lys sequence as substrates. The results indicated that in addition to P1 Lys, P2 Asp in the substrates is most important, that P3 Asp is additionally important, and that P5 Asp contributes somewhat to the susceptibility, and that P4 Asp is the least important. These results were essentially identical as between porcine and bovine enteropeptidases.

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