論文

2021年3月

Structural basis for substrate specificity of L-methionine decarboxylase

PROTEIN SCIENCE
  • Atsushi Okawa
  • ,
  • Tomoo Shiba
  • ,
  • Masaya Hayashi
  • ,
  • Yuki Onoue
  • ,
  • Masaki Murota
  • ,
  • Dan Sato
  • ,
  • Junko Inagaki
  • ,
  • Takashi Tamura
  • ,
  • Shigeharu Harada
  • ,
  • Kenji Inagaki

30
3
開始ページ
663
終了ページ
677
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/pro.4027
出版者・発行元
WILEY

L-Methionine decarboxylase (MetDC) from Streptomyces sp. 590 is a vitamin B-6-dependent enzyme and catalyzes the non-oxidative decarboxylation of L-methionine to produce 3-methylthiopropylamine and carbon dioxide. We present here the crystal structures of the ligand-free form of MetDC and of several enzymatic reaction intermediates. Group II amino acid decarboxylases have many residues in common around the active site but the residues surrounding the side chain of the substrate differ. Based on information obtained from the crystal structure, and mutational and biochemical experiments, we propose a key role for Gln64 in determining the substrate specificity of MetDC, and for Tyr421 as the acid catalyst that participates in protonation after the decarboxylation reaction.

リンク情報
DOI
https://doi.org/10.1002/pro.4027
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000609279300001&DestApp=WOS_CPL
ID情報
  • DOI : 10.1002/pro.4027
  • ISSN : 0961-8368
  • eISSN : 1469-896X
  • Web of Science ID : WOS:000609279300001

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