Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques

研究成果: ジャーナルへの寄稿記事

10 引用 (Scopus)

抄録

Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine181 at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan171 have been chemically modified: the tryptophan-specific modification with N-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by P. chrysosporium LiP, whereas the activity of T. cervina LiP was not affected, suggesting no catalytic tryptophan in T. cervina LiP. On the other hand, the tyrosine-specific modification with tetranitromethane did not affect the activities of P. chrysosporium LiP lacking tyrosine but inactivated T. cervina LiP due to the nitration of tyrosine181. These results strongly suggest that tyrosine181 is at the catalytic site in T. cervina LiP.

元の言語英語
ページ(範囲)1423-1427
ページ数5
ジャーナルBiotechnology letters
33
発行部数7
DOI
出版物ステータス出版済み - 7 1 2011

Fingerprint

Trametes
Chemical modification
Lignin
Tyrosine
Phanerochaete
Tryptophan
Catalytic Domain
Tetranitromethane
Bromosuccinimide
Nitration
lignin peroxidase
Peroxidases
Alcohols
Proteins

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

これを引用

Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques. / Miki, Yuta; Ichinose, Hirofumi; Wariishi, Hiroyuki.

:: Biotechnology letters, 巻 33, 番号 7, 01.07.2011, p. 1423-1427.

研究成果: ジャーナルへの寄稿記事

@article{20b1041f26164be6b38693a6f62e5d04,
title = "Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques",
abstract = "Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine181 at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan171 have been chemically modified: the tryptophan-specific modification with N-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by P. chrysosporium LiP, whereas the activity of T. cervina LiP was not affected, suggesting no catalytic tryptophan in T. cervina LiP. On the other hand, the tyrosine-specific modification with tetranitromethane did not affect the activities of P. chrysosporium LiP lacking tyrosine but inactivated T. cervina LiP due to the nitration of tyrosine181. These results strongly suggest that tyrosine181 is at the catalytic site in T. cervina LiP.",
author = "Yuta Miki and Hirofumi Ichinose and Hiroyuki Wariishi",
year = "2011",
month = "7",
day = "1",
doi = "10.1007/s10529-011-0571-2",
language = "English",
volume = "33",
pages = "1423--1427",
journal = "Biotechnology Letters",
issn = "0141-5492",
publisher = "Springer Netherlands",
number = "7",

}

TY - JOUR

T1 - Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques

AU - Miki, Yuta

AU - Ichinose, Hirofumi

AU - Wariishi, Hiroyuki

PY - 2011/7/1

Y1 - 2011/7/1

N2 - Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine181 at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan171 have been chemically modified: the tryptophan-specific modification with N-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by P. chrysosporium LiP, whereas the activity of T. cervina LiP was not affected, suggesting no catalytic tryptophan in T. cervina LiP. On the other hand, the tyrosine-specific modification with tetranitromethane did not affect the activities of P. chrysosporium LiP lacking tyrosine but inactivated T. cervina LiP due to the nitration of tyrosine181. These results strongly suggest that tyrosine181 is at the catalytic site in T. cervina LiP.

AB - Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine181 at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan171 have been chemically modified: the tryptophan-specific modification with N-bromosuccinimide sufficiently disrupted oxidation of veratryl alcohol by P. chrysosporium LiP, whereas the activity of T. cervina LiP was not affected, suggesting no catalytic tryptophan in T. cervina LiP. On the other hand, the tyrosine-specific modification with tetranitromethane did not affect the activities of P. chrysosporium LiP lacking tyrosine but inactivated T. cervina LiP due to the nitration of tyrosine181. These results strongly suggest that tyrosine181 is at the catalytic site in T. cervina LiP.

UR - http://www.scopus.com/inward/record.url?scp=79958767629&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79958767629&partnerID=8YFLogxK

U2 - 10.1007/s10529-011-0571-2

DO - 10.1007/s10529-011-0571-2

M3 - Article

C2 - 21373922

AN - SCOPUS:79958767629

VL - 33

SP - 1423

EP - 1427

JO - Biotechnology Letters

JF - Biotechnology Letters

SN - 0141-5492

IS - 7

ER -