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Updated: Oct 12, 2025

Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET

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Structural basis for the substrate recognition mechanism of ATP-sulfurylase domain of human PAPS synthase 2

Pan Zhang1, Lin Zhang2, Zhaoyuan Hou3

  • 1Key Laboratory of Medical Epigenetics and Metabolism, Institutes of Biomedical Sciences, Shanghai Medical College, Fudan University, Shanghai, 200032, China.

Biochemical and Biophysical Research Communications
|November 24, 2021
PubMed

Keywords:
3′-phosphoadenosine-5′-phosphosulfate5′-phosphosulfateHuman PAPS synthaseSulfation

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