Amino Acid Sequence of Egyptian Goose Egg-White Lysozyme and Effects of Amino Acid Substitution on the Enzymatic Activity

• KAWAMURA Shunsuke

  Department of Bioscience, School of Agriculture, Tokai University Department of Bioscience, School of Agriculture, Tokai University

• TOSHIMA Gen

  Department of Bioscience, School of Agriculture, Tokai University Department of Bioscience, School of Agriculture, Tokai University

• CHIJIIWA Yuki

  Department of Bioscience, School of Agriculture, Tokai University Department of Bioscience, School of Agriculture, Tokai University

• TORIKATA Takao

  Department of Bioscience, School of Agriculture, Tokai University Department of Bioscience, School of Agriculture, Tokai University

• ARAKI Tomohiro

  Department of Bioscience, School of Agriculture, Tokai University Department of Bioscience, School of Agriculture, Tokai University

抄録

The amino acid sequence of Egyptian goose lysozyme (EGL) from egg-white and its enzymatic properties were analyzed. The established sequence had the highest similarity to wood duck lysozyme (WDL) with five amino acid substitutions, and had eighteen substitutions difference from hen egg-white lysozyme (HEL). Tyr34 and Gly37 were found at subsites E and F of the active site when compared with HEL. The experimental time-course characteristics of EGL against the N-acetylglucosamine pentamer substrate, (GlcNAc)₅, revealed higher production of (GlcNAc)₄ and lower production of (GlcNAc)₂ when compared with HEL. The saccharide-binding ability of subsites A–C in EGL was also found to be weaker than in HEL. An analysis of the enzymatic reactions of five mutants in respect of positions 34, 37 and 71 in HEL indicated the time-course characteristics of EGL to be caused by the combination of three substitutions (F34Y, N37G and G71R) between HEL and EGL. A computer simulation of the EGL-catalyzed reaction suggested that the time-course characteristics of EGL resulted from the difference in the binding free energy for subsites A, B, E and F and the rate constant of transglycosylation between EGL and HEL.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 76 (4), 691-698, 2012

  公益社団法人 日本農芸化学会

キーワード

• lysozyme
• amino acid sequence
• lysozyme-catalyzed reaction
• site-directed mutagenesis
• subsite

詳細情報

• CRID: 1390282681455302400
• NII論文ID: 10030751484
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.110819
• COI: 1:STN:280:DC%2BC38rjt1Wjtw%3D%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 023592899
• PubMed: 22484934
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I023592899
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.110819
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可