title: Substrate specificities of porcine and bovine enteropeptidases toward the peptide Val-(Asp)4-Lys-Ile-Val-Gly and its analogs.
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.
authors.affiliation: Protein Research Group, RIKEN Genomic Sciences Center, Tsurumi, Yokohama, Kanagawa 230-0045, Japan.
authors.forename: Yong-Tae
authors.initials: YT
authors.lastname: Kim
authors.forename: Wataru
authors.initials: W
authors.lastname: Nishii
authors.forename: Masashi
authors.initials: M
authors.lastname: Matsushima
authors.forename: Hideshi
authors.initials: H
authors.lastname: Inoue
authors.forename: Hisashi
authors.initials: H
authors.lastname: Ito
authors.forename: Sun Joo
authors.initials: SJ
authors.lastname: Park
authors.forename: Kenji
authors.initials: K
authors.lastname: Takahashi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004765:Enteropeptidase / Q000378:metabolism*; D009154:Mutation; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D013552:Swine
chemical_list: D010455:Peptides; D004765:Enteropeptidase