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Crystal Structure‐based Studies of Cytosolic Sulfotransferase by Kouichi Yoshinari; Evgeniy V. Petrotchenko; Lars C. Pedersen; Masahiko Negishi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Crystal Structure‐based Studies of Cytosolic Sulfotransferase about?

## Abstract Sulfation is a widely observed biological reaction conserved from bacterium to human that plays a key role in various biological processes such as growth, development, and defense against adversities. Deficiencies due to the lack of the ubiquitous sulfate donor 3′‐phosphoadenosine‐5′‐phosphosulfate (PAPS) are lethal in humans. A large group of enzymes called sulfotransferases catalyze the transfer reaction of sulfuryl group of PAPS to the acceptor group of numerous biochemical and xenochemical substrates. Four X‐ray crystal structures of sulfotransferases have now been determined: cytosolic estrogen, hydroxysteroid, aryl sulfotransferases, and a sulfotransferase domain of the Golgi‐membrane heparan sulfate __N__‐deacetylase/__N__‐sulfotransferase 1. These have revealed the conserved core structure of the PAPS binding site, a common reaction mechanism, and some information concerning the substrate specificity. These crystal structures introduce a new era of the study of the sulfotransferases. © 2001 John Wiley & Sons, Inc. J Biochem Mol Toxicol 15:67–75, 2001

Who reads Crystal Structure‐based Studies of Cytosolic Sulfotransferase?

Author

Kouichi Yoshinari; Evgeniy V. Petrotchenko; Lars C. Pedersen; Masahiko Negishi

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 1095-6670)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)