New fluorescent substrates of microbial transglutaminase and its application to peptide tag-directed covalent protein labeling

Noriho Kamiya, Hiroki Abe

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Citations (Scopus)

Abstract

Transglutaminase (TGase) is an enzyme that catalyzes the post-translational covalent cross-linking of Gln-and Lys-containing peptides and/or proteins according to its substrate specificity. We have recently designed a variety of Gln-donor fluorescent substrates of microbial transglutaminase (MTG) from Streptomyces mobaraensis and evaluated their potential use in MTG-mediated covalent protein labeling. The newly designed substrates are based on the relatively broad substrate recognition of MTG for the substitution of the N-terminal group of a conventional TGase substrate, benzyloxycarbonyl-l-glutaminylglycine (Z-QG). It is revealed that MTG is capable of accepting a diverse range of fluorophores in place of the N-terminal moiety of Z-QG when linked via a suitable linker. Here, we show the potential utility of a new fluorescent substrate for peptide tag-directed covalent protein labeling by employing fluorescein-4-isothiocyanate-β-Ala-QG as a model Gln-donor substrate for MTG.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages81-94
Number of pages14
DOIs
Publication statusPublished - Jan 1 2011

Publication series

NameMethods in Molecular Biology
Volume751
ISSN (Print)1064-3745

Fingerprint

Transglutaminases
Peptides
Proteins
glutaminyl-glycine
Streptomyces
Substrate Specificity
Fluorescein
Enzymes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

Cite this

Kamiya, N., & Abe, H. (2011). New fluorescent substrates of microbial transglutaminase and its application to peptide tag-directed covalent protein labeling. In Methods in Molecular Biology (pp. 81-94). (Methods in Molecular Biology; Vol. 751). Humana Press Inc.. https://doi.org/10.1007/978-1-61779-151-2_7

New fluorescent substrates of microbial transglutaminase and its application to peptide tag-directed covalent protein labeling. / Kamiya, Noriho; Abe, Hiroki.

Methods in Molecular Biology. Humana Press Inc., 2011. p. 81-94 (Methods in Molecular Biology; Vol. 751).

Research output: Chapter in Book/Report/Conference proceedingChapter

Kamiya, N & Abe, H 2011, New fluorescent substrates of microbial transglutaminase and its application to peptide tag-directed covalent protein labeling. in Methods in Molecular Biology. Methods in Molecular Biology, vol. 751, Humana Press Inc., pp. 81-94. https://doi.org/10.1007/978-1-61779-151-2_7
Kamiya, Noriho ; Abe, Hiroki. / New fluorescent substrates of microbial transglutaminase and its application to peptide tag-directed covalent protein labeling. Methods in Molecular Biology. Humana Press Inc., 2011. pp. 81-94 (Methods in Molecular Biology).
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