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Comparative specificity of microbial acid proteinases for synthetic peptides. II. Effect of secondary interaction
Authors:T Oka  K Morihara
Affiliation:Shionogi Research Laboratory, Shionogi & Co., Ltd., Fukushima-ku, Osaka, 553 Japan
Abstract:To investigate the effect of “secondary interaction” on hydrolysis by various acid proteinases from molds and yeasts, synthetic peptides
/></figure> amino acid residues) were used as substrates. Pepsin was used for the comparative study. These peptides were split at the peptide bonds indicated by the arrows, permitting examination of the effect of residue X distant by two or three amino acid residues from the hydrolytic site in the peptides. According to the system of Schechter and Berger (<em>Biochem. Biophys. Res. Commun. 27</em>; 157, 1967), the amino acid residues in peptide substrates were numbered P<sub>1</sub>, P<sub>2</sub>, etc. toward the N-terminal direction from the site of hydrolysis, and P<sub>1</sub>′, P<sub>2</sub>′, etc. toward the C-terminal direction. The results indicated that hydrolysis by these microbial enzymes is affected by at least six amino acid residues (P<sub>1</sub>-P<sub>3</sub> and P<sub>1</sub>′-P<sub>3</sub>′) in peptide substrates, as is seen with pepsin. Elongation of the peptide chain with suitable amino acid residues from P<sub>1</sub> to P<sub>2</sub> or P<sub>3</sub> and from P<sub>1</sub>′ to P<sub>2</sub>′ or P<sub>3</sub>′ in peptide substrates resulted in much or less increase of hydrolysis depending upon the species of the enzyme producers.</td> </tr> <tr> <td align=
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