Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1975103 | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | 2016 | 11 Pages |
Abstract
The nucleotide sequences of largemouth bass pepsinogens (PG1, 2 and 3) were determined after molecular cloning of the respective cDNAs. Encoded PG1, 2 and 3 were classified as fish pepsinogens A1, A2 and C, respectively. Molecular evolutionary analyses show that vertebrate pepsinogens are classified into seven monophyletic groups, i.e. pepsinogens A, F, Y (prochymosins), C, B, and fish pepsinogens A and C. Regarding the primary structures, extensive deletion was obvious in Sâ²1 loop residues in fish pepsin A as well as tetrapod pepsin Y. This deletion resulted in a decrease in hydrophobic residues in the Sâ²1 site. Hydrolytic specificities of bass pepsins A1 and A2 were investigated with a pepsin substrate and its variants. Bass pepsins preferred both hydrophobic/aromatic residues and charged residues at the Pâ²1 sites of substrates, showing the dual character of Sâ²1 sites. Thermodynamic analyses of bass pepsin A2 showed that its activation Gibbs energy change (âGâ¡) was lower than that of porcine pepsin A. Several sites of bass pepsin A2 moiety were found to be under positive selection, and most of them are located on the surface of the molecule, where they are involved in conformational flexibility. The broad Sâ²1 specificity and flexible structure of bass pepsin A2 are thought to cause its high proteolytic activity.
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Authors
Yoko Miura, Mieko Suzuki-Matsubara, Takashi Kageyama, Akihiko Moriyama,