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
Search this article
Abstract
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.
Journal
-
- Bioscience, Biotechnology, and Biochemistry
-
Bioscience, Biotechnology, and Biochemistry 76 (4), 691-698, 2012
Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Tweet
Details 詳細情報について
-
- CRID
- 1390282681455302400
-
- NII Article ID
- 10030751484
-
- NII Book ID
- AA10824164
-
- COI
- 1:STN:280:DC%2BC38rjt1Wjtw%3D%3D
-
- ISSN
- 13476947
- 09168451
-
- NDL BIB ID
- 023592899
-
- PubMed
- 22484934
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
-
- Abstract License Flag
- Disallowed