A laccase-catalysed tyrosine click reaction

Shinichi Sato; Keita Nakane; Hiroyuki Nakamura

doi:10.1039/d0ob00650e

A laccase-catalysed tyrosine click reaction

Shinichi Sato, Keita Nakane, Hiroyuki Nakamura

Research output: Contribution to journal › Article › peer-review

15 Citations (Scopus)

Abstract

A laccase-catalysed tyrosine click reaction proceeded between the tyrosine modification reagentN-methyl luminol and tyrosine residues in peptides/proteins. Laccase-catalysed tyrosine-specific modification under mild reaction conditions (shaking at 37 °C) was more efficient than previously reported tyrosine click reactions using hemin, horseradish peroxidase (HRP) or electrochemistry.

Original language	English
Pages (from-to)	3664-3668
Number of pages	5
Journal	Organic and Biomolecular Chemistry
Volume	18
Issue number	19
DOIs	https://doi.org/10.1039/d0ob00650e
Publication status	Published - 2020 May 21
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1039/d0ob00650e

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title = "A laccase-catalysed tyrosine click reaction",

abstract = "A laccase-catalysed tyrosine click reaction proceeded between the tyrosine modification reagentN-methyl luminol and tyrosine residues in peptides/proteins. Laccase-catalysed tyrosine-specific modification under mild reaction conditions (shaking at 37 °C) was more efficient than previously reported tyrosine click reactions using hemin, horseradish peroxidase (HRP) or electrochemistry.",

author = "Shinichi Sato and Keita Nakane and Hiroyuki Nakamura",

note = "Funding Information: This work was partially supported by a Grant-in-Aid for Scientific Research (B) (19H02848 to S. Sato) and a Grant-in-Aid for Chemistry for Multimolecular Crowding Biosystems (18H04542 to H. Nakamura) from MEXT, Japan. We thank Dr Kosuke Minamihata at Kyushu University for a fruitful discussion about laccase. We also thank Amano Enzyme Inc. for providing the laccase sample. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2020.",

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doi = "10.1039/d0ob00650e",

language = "English",

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T1 - A laccase-catalysed tyrosine click reaction

AU - Sato, Shinichi

AU - Nakane, Keita

AU - Nakamura, Hiroyuki

N1 - Funding Information: This work was partially supported by a Grant-in-Aid for Scientific Research (B) (19H02848 to S. Sato) and a Grant-in-Aid for Chemistry for Multimolecular Crowding Biosystems (18H04542 to H. Nakamura) from MEXT, Japan. We thank Dr Kosuke Minamihata at Kyushu University for a fruitful discussion about laccase. We also thank Amano Enzyme Inc. for providing the laccase sample. Publisher Copyright: © The Royal Society of Chemistry 2020.

PY - 2020/5/21

Y1 - 2020/5/21

N2 - A laccase-catalysed tyrosine click reaction proceeded between the tyrosine modification reagentN-methyl luminol and tyrosine residues in peptides/proteins. Laccase-catalysed tyrosine-specific modification under mild reaction conditions (shaking at 37 °C) was more efficient than previously reported tyrosine click reactions using hemin, horseradish peroxidase (HRP) or electrochemistry.

AB - A laccase-catalysed tyrosine click reaction proceeded between the tyrosine modification reagentN-methyl luminol and tyrosine residues in peptides/proteins. Laccase-catalysed tyrosine-specific modification under mild reaction conditions (shaking at 37 °C) was more efficient than previously reported tyrosine click reactions using hemin, horseradish peroxidase (HRP) or electrochemistry.

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EP - 3668

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

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ER -

A laccase-catalysed tyrosine click reaction

Abstract

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