Incorporation of 15N-labeled ammonia into glutamine amide groups by protein-glutaminase and analysis of the reactivity for α-lactalbumin

Noriko Miwa, Nobuhisa Shimba, Mina Nakamura, Keiichi Yokoyama, Noriki Nio, Eiichiro Suzuki, Kenji Sonomoto

研究成果: Contribution to journalArticle査読

5 被引用数 (Scopus)

抄録

Protein-glutaminase (PG) is an enzyme that catalyzes the deamidation of protein-bound glutamine residues. We found that an enzyme labeling technique (ELT), which is a stable isotope labeling method based on transglutaminase (TGase) reaction, is applicable for PG. PG catalyzed incorporation of 15N-labeled ammonium ions into reactive glutamine amide groups in α-lactalbumin similarly to TGase and deamidated the most reactive glutamine amide group once labeled with 15N. Furthermore, we investigated the effect of ammonium ions on the PG activity by peptide mapping, and more reactive glutamine residues were detected than were detected by the ELT in the presence of ammonium ions. This is probably because ammonium ions are competitive inhibitors, causing decreased reactivity for glutamine residues. We propose the reaction scheme of PG in the presence of the 15N-labeled ammonium ions and show that the ELT method with PG is useful for evaluating the activity of PG.

本文言語英語
ページ(範囲)12752-12760
ページ数9
ジャーナルJournal of Agricultural and Food Chemistry
59
24
DOI
出版ステータス出版済み - 12 28 2011

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

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