リゾチームの触媒機構:無脊椎動物型とニワトリ型の比較から

Translated title of the contribution: Catalytic Mechanism of Lysozyme Based on the Structures of Invertebrate-type Lysozyme and Chicken-type Lysozyme

Research output: Contribution to journalArticle

Abstract

<p>Based on the structure of invertebrate-type lyzozyme, <i>Venerupis philippinarum</i> lysozyme (<i>Vp</i>L), we designed Asn46Asp/Asp52Ser or Asn46Glu/Asp52Ser hen egg white lysozyme (HEWL) mutants. Both lysozyme mutants possessed lysozyme acitivity like <i>Vp</i>L and HEWL. Although Asn46Glu/Asp52Ser mutant formed a glycosyl adduct in the reaction with the N-acetylglucosamine oligomer, however, the turnover rate of estimated from the glycosyl formation and decomposition rates was only 20% of the observed hydrolysis rate of the substrate. From these results, we discussed the catalytic mechanism of lysozymes.</p>
Original languageJapanese
Pages (from-to)140-143
Number of pages4
Journal生物物理
Volume57
Issue number3
DOIs
Publication statusPublished - 2017

Fingerprint

Muramidase
Acetylglucosamine
Oligomers
Invertebrates
Hydrolysis
Decomposition
Substrates

Cite this

リゾチームの触媒機構:無脊椎動物型とニワトリ型の比較から. / 阿部義人.

In: 生物物理, Vol. 57, No. 3, 2017, p. 140-143.

Research output: Contribution to journalArticle

@article{37bab4b67d1d4bcb90123cf9c6413ae9,
title = "リゾチームの触媒機構:無脊椎動物型とニワトリ型の比較から",
abstract = "Based on the structure of invertebrate-type lyzozyme, Venerupis philippinarum lysozyme (VpL), we designed Asn46Asp/Asp52Ser or Asn46Glu/Asp52Ser hen egg white lysozyme (HEWL) mutants. Both lysozyme mutants possessed lysozyme acitivity like VpL and HEWL. Although Asn46Glu/Asp52Ser mutant formed a glycosyl adduct in the reaction with the N-acetylglucosamine oligomer, however, the turnover rate of estimated from the glycosyl formation and decomposition rates was only 20{\%} of the observed hydrolysis rate of the substrate. From these results, we discussed the catalytic mechanism of lysozymes.",
author = "義人 阿部",
year = "2017",
doi = "10.2142/biophys.57.140",
language = "Japanese",
volume = "57",
pages = "140--143",
journal = "生物物理",
publisher = "一般社団法人 日本生物物理学会",
number = "3",

}

TY - JOUR

T1 - リゾチームの触媒機構:無脊椎動物型とニワトリ型の比較から

AU - 阿部, 義人

PY - 2017

Y1 - 2017

N2 - Based on the structure of invertebrate-type lyzozyme, Venerupis philippinarum lysozyme (VpL), we designed Asn46Asp/Asp52Ser or Asn46Glu/Asp52Ser hen egg white lysozyme (HEWL) mutants. Both lysozyme mutants possessed lysozyme acitivity like VpL and HEWL. Although Asn46Glu/Asp52Ser mutant formed a glycosyl adduct in the reaction with the N-acetylglucosamine oligomer, however, the turnover rate of estimated from the glycosyl formation and decomposition rates was only 20% of the observed hydrolysis rate of the substrate. From these results, we discussed the catalytic mechanism of lysozymes.

AB - Based on the structure of invertebrate-type lyzozyme, Venerupis philippinarum lysozyme (VpL), we designed Asn46Asp/Asp52Ser or Asn46Glu/Asp52Ser hen egg white lysozyme (HEWL) mutants. Both lysozyme mutants possessed lysozyme acitivity like VpL and HEWL. Although Asn46Glu/Asp52Ser mutant formed a glycosyl adduct in the reaction with the N-acetylglucosamine oligomer, however, the turnover rate of estimated from the glycosyl formation and decomposition rates was only 20% of the observed hydrolysis rate of the substrate. From these results, we discussed the catalytic mechanism of lysozymes.

U2 - 10.2142/biophys.57.140

DO - 10.2142/biophys.57.140

M3 - 記事

VL - 57

SP - 140

EP - 143

JO - 生物物理

JF - 生物物理

IS - 3

ER -