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: ジャーナルへの寄稿記事

4 引用 (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.

元の言語英語
ページ(範囲)3091-3094
ページ数4
ジャーナルFEBS Letters
583
発行部数18
DOI
出版物ステータス出版済み - 9 17 2009

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arylsulfate sulfotransferase
Phosphoadenosine Phosphosulfate
Sulfotransferases
Sulfates
Catalytic Domain
Phenol
Escherichia coli
Substrates

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

これを引用

On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases. / Teramoto, Takamasa; Adachi, Rumi; Sakakibara, Yoichi; Liu, Ming Cheh; Suiko, Masahito; Kimura, Makoto; Kakuta, Yoshimitsu.

:: FEBS Letters, 巻 583, 番号 18, 17.09.2009, p. 3091-3094.

研究成果: ジャーナルへの寄稿記事

Teramoto, Takamasa ; Adachi, Rumi ; Sakakibara, Yoichi ; Liu, Ming Cheh ; Suiko, Masahito ; Kimura, Makoto ; Kakuta, Yoshimitsu. / On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases. :: FEBS Letters. 2009 ; 巻 583, 番号 18. pp. 3091-3094.
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abstract = "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.",
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AU - Suiko, Masahito

AU - Kimura, Makoto

AU - Kakuta, Yoshimitsu

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