On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases

Takamasa Teramoto, Rumi Adachi, Yoichi Sakakibara, Ming Cheh Liu, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta

研究成果: Contribution to journalArticle査読

4 被引用数 (Scopus)

抄録

Mammalian sulfotransferases (STs) utilize exclusively the sulfuryl group donor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to catalyze the sulfurylation reactions based on a sequential transfer mechanism. In contrast, the commensal intestinal bacterial arylsulfate sulfotransferases (ASSTs) do not use PAPS as the sulfuryl group donor, but instead catalyze sulfuryl transfer from phenolic sulfate to a phenol via a Ping-Pong mechanism. Interestingly, structural comparison revealed a similar spatial arrangement of the active site residues as well as the cognate substrates in mouse ST (mSULT1D1) and Escherichia coli CFT073 ASST, despite that their overall structures bear no discernible relationship. These observations suggest that the active sites of PAPS-dependent SULT1D1 and phenolic sulfate-utilizing ASST represent an example of convergent evolution.

本文言語英語
ページ(範囲)3091-3094
ページ数4
ジャーナルFEBS Letters
583
18
DOI
出版ステータス出版済み - 9 17 2009

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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