Effect of protein structure on laccase-catalyzed protein oligomerization

Maija-Liisa Mattinen (Corresponding Author), Maarit Hellman, Perttu Permi, Karin Autio, Nisse Kalkkinen, Johanna Buchert

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

Laccase-catalyzed oligomerization of proteins was studied using Trametes hirsuta laccase (ThL) and coactosin as a model system. The reaction mechanism was elucidated using free amino acids and the tripeptide Gly-Leu-Tyr as substrates. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and high-performance liquid chromatography (HPLC) as well as oxygen consumption measurements and SDS-PAGE were used to study the reactions. Of the 15 selected amino acids, ThL was found to oxidize tryptophan (Trp), tyrosine (Tyr), and cysteine (Cys), of which the reactions with Tyr and Cys have been described earlier. ThL was able to link four full-length coactosins, whereas coactosin that was truncated from its C-terminus remained unpolymerized. Of the four tyrosine residues present in coactosin, only the tyrosine in the C-terminus was found to be reactive. Polymerization between tyrosine side-chains was unambiguously shown using different oligomers of Gly-Leu-Tyr as parent ions in MALDI-TOF/TOF MS fragment ion analyses.
Original languageEnglish
Pages (from-to)8883-8890
JournalJournal of Agricultural and Food Chemistry
Volume54
Issue number23
DOIs
Publication statusPublished - 2006
MoE publication typeA1 Journal article-refereed

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Laccase
Oligomerization
laccase
protein structure
Tyrosine
tyrosine
Coriolus hirsutus
Trametes
glycylleucine
Proteins
proteins
Cysteine
cysteine
Ions
ions
Amino Acids
tripeptides
reaction mechanisms
matrix-assisted laser desorption-ionization mass spectrometry
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry

Keywords

  • Laccase
  • oligomerization
  • cross-linking
  • proteins
  • tyrosine

Cite this

Mattinen, M-L., Hellman, M., Permi, P., Autio, K., Kalkkinen, N., & Buchert, J. (2006). Effect of protein structure on laccase-catalyzed protein oligomerization. Journal of Agricultural and Food Chemistry, 54(23), 8883-8890. https://doi.org/10.1021/jf062397h
Mattinen, Maija-Liisa ; Hellman, Maarit ; Permi, Perttu ; Autio, Karin ; Kalkkinen, Nisse ; Buchert, Johanna. / Effect of protein structure on laccase-catalyzed protein oligomerization. In: Journal of Agricultural and Food Chemistry. 2006 ; Vol. 54, No. 23. pp. 8883-8890.
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abstract = "Laccase-catalyzed oligomerization of proteins was studied using Trametes hirsuta laccase (ThL) and coactosin as a model system. The reaction mechanism was elucidated using free amino acids and the tripeptide Gly-Leu-Tyr as substrates. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and high-performance liquid chromatography (HPLC) as well as oxygen consumption measurements and SDS-PAGE were used to study the reactions. Of the 15 selected amino acids, ThL was found to oxidize tryptophan (Trp), tyrosine (Tyr), and cysteine (Cys), of which the reactions with Tyr and Cys have been described earlier. ThL was able to link four full-length coactosins, whereas coactosin that was truncated from its C-terminus remained unpolymerized. Of the four tyrosine residues present in coactosin, only the tyrosine in the C-terminus was found to be reactive. Polymerization between tyrosine side-chains was unambiguously shown using different oligomers of Gly-Leu-Tyr as parent ions in MALDI-TOF/TOF MS fragment ion analyses.",
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Mattinen, M-L, Hellman, M, Permi, P, Autio, K, Kalkkinen, N & Buchert, J 2006, 'Effect of protein structure on laccase-catalyzed protein oligomerization', Journal of Agricultural and Food Chemistry, vol. 54, no. 23, pp. 8883-8890. https://doi.org/10.1021/jf062397h

Effect of protein structure on laccase-catalyzed protein oligomerization. / Mattinen, Maija-Liisa (Corresponding Author); Hellman, Maarit; Permi, Perttu; Autio, Karin; Kalkkinen, Nisse; Buchert, Johanna.

In: Journal of Agricultural and Food Chemistry, Vol. 54, No. 23, 2006, p. 8883-8890.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Effect of protein structure on laccase-catalyzed protein oligomerization

AU - Mattinen, Maija-Liisa

AU - Hellman, Maarit

AU - Permi, Perttu

AU - Autio, Karin

AU - Kalkkinen, Nisse

AU - Buchert, Johanna

PY - 2006

Y1 - 2006

N2 - Laccase-catalyzed oligomerization of proteins was studied using Trametes hirsuta laccase (ThL) and coactosin as a model system. The reaction mechanism was elucidated using free amino acids and the tripeptide Gly-Leu-Tyr as substrates. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and high-performance liquid chromatography (HPLC) as well as oxygen consumption measurements and SDS-PAGE were used to study the reactions. Of the 15 selected amino acids, ThL was found to oxidize tryptophan (Trp), tyrosine (Tyr), and cysteine (Cys), of which the reactions with Tyr and Cys have been described earlier. ThL was able to link four full-length coactosins, whereas coactosin that was truncated from its C-terminus remained unpolymerized. Of the four tyrosine residues present in coactosin, only the tyrosine in the C-terminus was found to be reactive. Polymerization between tyrosine side-chains was unambiguously shown using different oligomers of Gly-Leu-Tyr as parent ions in MALDI-TOF/TOF MS fragment ion analyses.

AB - Laccase-catalyzed oligomerization of proteins was studied using Trametes hirsuta laccase (ThL) and coactosin as a model system. The reaction mechanism was elucidated using free amino acids and the tripeptide Gly-Leu-Tyr as substrates. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and high-performance liquid chromatography (HPLC) as well as oxygen consumption measurements and SDS-PAGE were used to study the reactions. Of the 15 selected amino acids, ThL was found to oxidize tryptophan (Trp), tyrosine (Tyr), and cysteine (Cys), of which the reactions with Tyr and Cys have been described earlier. ThL was able to link four full-length coactosins, whereas coactosin that was truncated from its C-terminus remained unpolymerized. Of the four tyrosine residues present in coactosin, only the tyrosine in the C-terminus was found to be reactive. Polymerization between tyrosine side-chains was unambiguously shown using different oligomers of Gly-Leu-Tyr as parent ions in MALDI-TOF/TOF MS fragment ion analyses.

KW - Laccase

KW - oligomerization

KW - cross-linking

KW - proteins

KW - tyrosine

U2 - 10.1021/jf062397h

DO - 10.1021/jf062397h

M3 - Article

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SP - 8883

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