The Mass Spectrometry society of Japan - The 71st Annual Conference on Mass Spectrometry, Japan
Japanese

Abstract

Table of contents

Timetable

Plenary Lecture

Symposium Sessions (Day1, Day2, Day3)

Basic Sessions (Day1, Day2, Day3)

Young Researchers' Sessions (Day1, Day2, Day3)

Poster Presentations (Day1, Day2, Day3)

Special Evening Sessions

Corporate Program

Symposium Sessions

Day 3, May 17（Wed.）　14:15-14:37　Room A (Special Conference Room)

3A-S-1415（2P-19）　　PDF

Investigating the impact of substrate protein structure on enzymatic reactions utilizing proteomic samples as substrates

(1Kyoto Univ., 2NIBIOHN)
oKosuke Ogata1, Asato Maeda1, Yuka Muramatsu1, Naoyuki Sugiyama1, Yasushi Ishihama1,2

Enzymatic reactions have been used as tools to analyze proteomic samples. Proteases are employed to digest large proteins into smaller peptides. Protein phosphatases are utilized to remove phosphate groups from proteins, while protein kinases are utilized to add phosphate groups to target proteins. Recently, limited proteolysis has been utilized to map substrate structural changes as it preferentially cleaves surface-exposed domains of proteins. Motivated by this, we conceptualized the use of various enzymes for conformational mapping. We examined the effects of substrate structure on the efficiency of limited reactions with protease, kinase, and phosphatase. As a result, all three enzymes preferred the residues which are more exposed, supporting the possibility of structural profiling of substrate proteins with these enzymatic reactions.