Ligand-Induced Conformational Changes near the Active Site Regulating Enzyme Activity of Momorcharins from Seeds of Bitter Gourd

Chie Matsunaga, Yuuki Okada, Etsuko Nishimoto

研究成果: ジャーナルへの寄稿記事

抄録

It is reasonable to consider that Type I-ribosomal inactivation proteins (RIP) retain some specific affinity to harmful pathogens to complete the role as a bio-defense relating protein. In the present studies, it was shown that two Type I-RIPs, α- and β-momorcharins, maintained the abilities to bind with N-acetylglucosamine (NAG) to change the conformation around the active sites and to regulate their N-glycosidase activities. By the binding of NAG, the freedom of internal motion of Trp192 in α-momorcharin was increased 1.5 times near the active site and, on the other hand, the corresponding motion of Trp190 was limited 50% in β-momorcharin. The results in the fluorescence resonance excitation energy transfer experiments demonstrated that Trp-190 of β-momorcharin was kept away from Tyr-70 but Trp192 contrarily approached closer to the nearest neighboring Tyr residue consisting of the active center of α-momorcharin by the binding with NAG. These conformational changes near the active site close correlated with promotion and/or suppression of the N-glucosidase activities of β- and α-momorcharins.

元の言語英語
ページ(範囲)231-240
ページ数10
ジャーナルJournal of Fluorescence
29
発行部数1
DOI
出版物ステータス出版済み - 1 15 2019

Fingerprint

Momordica charantia
Enzyme activity
Seed
Catalytic Domain
Seeds
Ligands
Acetylglucosamine
Enzymes
suppression
promotion
energy
experiment
ability
Glucosidases
Fluorescence Resonance Energy Transfer
Excitation energy
Ribosomal Proteins
Glycoside Hydrolases
Pathogens
Energy transfer

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Clinical Psychology
  • Social Sciences (miscellaneous)
  • Sociology and Political Science
  • Spectroscopy
  • Clinical Biochemistry
  • Law

これを引用

Ligand-Induced Conformational Changes near the Active Site Regulating Enzyme Activity of Momorcharins from Seeds of Bitter Gourd. / Matsunaga, Chie; Okada, Yuuki; Nishimoto, Etsuko.

:: Journal of Fluorescence, 巻 29, 番号 1, 15.01.2019, p. 231-240.

研究成果: ジャーナルへの寄稿記事

@article{f66eab85f9f0415987eef5ef32ad95e7,
title = "Ligand-Induced Conformational Changes near the Active Site Regulating Enzyme Activity of Momorcharins from Seeds of Bitter Gourd",
abstract = "It is reasonable to consider that Type I-ribosomal inactivation proteins (RIP) retain some specific affinity to harmful pathogens to complete the role as a bio-defense relating protein. In the present studies, it was shown that two Type I-RIPs, α- and β-momorcharins, maintained the abilities to bind with N-acetylglucosamine (NAG) to change the conformation around the active sites and to regulate their N-glycosidase activities. By the binding of NAG, the freedom of internal motion of Trp192 in α-momorcharin was increased 1.5 times near the active site and, on the other hand, the corresponding motion of Trp190 was limited 50{\%} in β-momorcharin. The results in the fluorescence resonance excitation energy transfer experiments demonstrated that Trp-190 of β-momorcharin was kept away from Tyr-70 but Trp192 contrarily approached closer to the nearest neighboring Tyr residue consisting of the active center of α-momorcharin by the binding with NAG. These conformational changes near the active site close correlated with promotion and/or suppression of the N-glucosidase activities of β- and α-momorcharins.",
author = "Chie Matsunaga and Yuuki Okada and Etsuko Nishimoto",
year = "2019",
month = "1",
day = "15",
doi = "10.1007/s10895-018-2332-2",
language = "English",
volume = "29",
pages = "231--240",
journal = "Journal of Fluorescence",
issn = "1053-0509",
publisher = "Springer New York",
number = "1",

}

TY - JOUR

T1 - Ligand-Induced Conformational Changes near the Active Site Regulating Enzyme Activity of Momorcharins from Seeds of Bitter Gourd

AU - Matsunaga, Chie

AU - Okada, Yuuki

AU - Nishimoto, Etsuko

PY - 2019/1/15

Y1 - 2019/1/15

N2 - It is reasonable to consider that Type I-ribosomal inactivation proteins (RIP) retain some specific affinity to harmful pathogens to complete the role as a bio-defense relating protein. In the present studies, it was shown that two Type I-RIPs, α- and β-momorcharins, maintained the abilities to bind with N-acetylglucosamine (NAG) to change the conformation around the active sites and to regulate their N-glycosidase activities. By the binding of NAG, the freedom of internal motion of Trp192 in α-momorcharin was increased 1.5 times near the active site and, on the other hand, the corresponding motion of Trp190 was limited 50% in β-momorcharin. The results in the fluorescence resonance excitation energy transfer experiments demonstrated that Trp-190 of β-momorcharin was kept away from Tyr-70 but Trp192 contrarily approached closer to the nearest neighboring Tyr residue consisting of the active center of α-momorcharin by the binding with NAG. These conformational changes near the active site close correlated with promotion and/or suppression of the N-glucosidase activities of β- and α-momorcharins.

AB - It is reasonable to consider that Type I-ribosomal inactivation proteins (RIP) retain some specific affinity to harmful pathogens to complete the role as a bio-defense relating protein. In the present studies, it was shown that two Type I-RIPs, α- and β-momorcharins, maintained the abilities to bind with N-acetylglucosamine (NAG) to change the conformation around the active sites and to regulate their N-glycosidase activities. By the binding of NAG, the freedom of internal motion of Trp192 in α-momorcharin was increased 1.5 times near the active site and, on the other hand, the corresponding motion of Trp190 was limited 50% in β-momorcharin. The results in the fluorescence resonance excitation energy transfer experiments demonstrated that Trp-190 of β-momorcharin was kept away from Tyr-70 but Trp192 contrarily approached closer to the nearest neighboring Tyr residue consisting of the active center of α-momorcharin by the binding with NAG. These conformational changes near the active site close correlated with promotion and/or suppression of the N-glucosidase activities of β- and α-momorcharins.

UR - http://www.scopus.com/inward/record.url?scp=85058836274&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85058836274&partnerID=8YFLogxK

U2 - 10.1007/s10895-018-2332-2

DO - 10.1007/s10895-018-2332-2

M3 - Article

VL - 29

SP - 231

EP - 240

JO - Journal of Fluorescence

JF - Journal of Fluorescence

SN - 1053-0509

IS - 1

ER -