Substrate specificities of porcine and bovine enteropeptidases toward the peptide Val-(Asp)4-Lys-Ile-Val-Gly and its analogs

• Published in: Bioscience, biotechnology, and biochemistry Vol. 72; no. 3; pp. 905 - 908
• Main Authors: Kim, Y.T.(RIKEN, Yokohama (Japan). Yokohama Inst.), Nishii, W, Matsushima, M, Inoue, H, Ito, H, Park, S.J, Takahashi, K
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.03.2008; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Amino Acid Sequence; AMINO ACID SEQUENCES; Animals; Biological and medical sciences; BOVINA; BOVINAE; Cattle; CERDO; enteropeptidase; Enteropeptidase - metabolism; ENZIMAS; ENZYME; ENZYMES; Fundamental and applied biological sciences. Psychology; Mutation; PEPTIDE; PEPTIDES; Peptides - chemical synthesis; Peptides - metabolism; PEPTIDOS; PORCIN; PROTEINAS RECOMBINANTES; PROTEINE RECOMBINANTE; RECOMBINANT PROTEINS; SECUENCIAS DE AMINOACIDOS; SEQUENCE D'ACIDES AMINES; Structure-Activity Relationship; Substrate Specificity; SWINE; synthetic peptide substrates; trypsinogen activation peptide; Serine endopeptidases; Bovine; Peptides; Enzyme; synthetic peptide substrates; trypsinogen activation peptide; Activation; Pig; Substrate; Peptidases; Vertebrata; Trypsinogen; Mammalia; Analog; Substrate specificity; Enteropeptidase; Hydrolases; Artiodactyla; Ungulata
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.70732

The substrate specificities of porcine and bovine enteropeptidases were investigated using the peptide Val-(Asp)sub(4)-Lys-Ile-Val-Gly and its various analogs with mutations in the (Asp)sub(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.