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On the similar spatial arrangement of active site residues in PAPS‐dependent and phenolic sulfate‐utilizing sulfotransferases
Author(s) -
Teramoto Takamasa,
Adachi Rumi,
Sakakibara Yoichi,
Liu Ming-Cheh,
Suiko Masahito,
Kimura Makoto,
Kakuta Yoshimitsu
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.08.016
Subject(s) - chemistry , active site , sulfate , biochemistry , escherichia coli , stereochemistry , sulfotransferase , sulfation , enzyme , organic chemistry , gene
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.