Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.
Identifieur interne : 000508 ( Main/Corpus ); précédent : 000507; suivant : 000509Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.
Auteurs : Yuta Miki ; Hirofumi Ichinose ; Hiroyuki WariishiSource :
- Biotechnology letters [ 1573-6776 ] ; 2011.
English descriptors
- KwdEn :
- Benzyl Alcohols (metabolism), Bromosuccinimide (metabolism), Catalytic Domain (MeSH), Models, Molecular (MeSH), Peroxidases (chemistry), Peroxidases (metabolism), Phanerochaete (enzymology), Protein Processing, Post-Translational (MeSH), Protein Structure, Tertiary (MeSH), Tetranitromethane (metabolism), Trametes (enzymology), Tyrosine (chemistry), Tyrosine (metabolism).
- MESH :
- chemical , chemistry : Peroxidases, Tyrosine.
- chemical , metabolism : Benzyl Alcohols, Bromosuccinimide, Peroxidases, Tetranitromethane, Tyrosine.
- enzymology : Phanerochaete, Trametes.
- Catalytic Domain, Models, Molecular, Protein Processing, Post-Translational, Protein Structure, Tertiary.
Abstract
Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine(181) at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan(171) 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 tyrosine(181). These results strongly suggest that tyrosine(181) is at the catalytic site in T. cervina LiP.
DOI: 10.1007/s10529-011-0571-2
PubMed: 21373922
Links to Exploration step
pubmed:21373922Le document en format XML
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<author><name sortKey="Miki, Yuta" sort="Miki, Yuta" uniqKey="Miki Y" first="Yuta" last="Miki">Yuta Miki</name>
<affiliation><nlm:affiliation>Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, Japan.</nlm:affiliation>
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<author><name sortKey="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name>
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<author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name>
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<author><name sortKey="Miki, Yuta" sort="Miki, Yuta" uniqKey="Miki Y" first="Yuta" last="Miki">Yuta Miki</name>
<affiliation><nlm:affiliation>Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, Japan.</nlm:affiliation>
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<author><name sortKey="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name>
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<author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name>
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<series><title level="j">Biotechnology letters</title>
<idno type="eISSN">1573-6776</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Benzyl Alcohols (metabolism)</term>
<term>Bromosuccinimide (metabolism)</term>
<term>Catalytic Domain (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Peroxidases (chemistry)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Tetranitromethane (metabolism)</term>
<term>Trametes (enzymology)</term>
<term>Tyrosine (chemistry)</term>
<term>Tyrosine (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term>
<term>Tyrosine</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Benzyl Alcohols</term>
<term>Bromosuccinimide</term>
<term>Peroxidases</term>
<term>Tetranitromethane</term>
<term>Tyrosine</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
<term>Trametes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term>
<term>Models, Molecular</term>
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<front><div type="abstract" xml:lang="en">Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine(181) at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan(171) 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 tyrosine(181). These results strongly suggest that tyrosine(181) is at the catalytic site in T. cervina LiP.</div>
</front>
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<Title>Biotechnology letters</Title>
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<ArticleTitle>Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques.</ArticleTitle>
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<Abstract><AbstractText>Trametes cervina lignin peroxidase (LiP) lacks a catalytic tryptophan strictly conserved in other LiP and versatile peroxidases. It contains tyrosine(181) at the potential catalytic site. This protein and the well-characterized Phanerochaete chrysosporium LiP with the catalytic tryptophan(171) 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 tyrosine(181). These results strongly suggest that tyrosine(181) is at the catalytic site in T. cervina LiP.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Miki</LastName>
<ForeName>Yuta</ForeName>
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<AffiliationInfo><Affiliation>Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka, Japan.</Affiliation>
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