Characterization of bovine phenol sulfotransferases: evidence of a major role for SULT1B1 in the liver

Abstract

1. Cattle are an important component of the human food chain. Drugs used either legally or illegally in cattle may therefore enter the food chain and it is thus important to understand pathways of drug metabolism in this species, including sulfation catalyzed by the sulfotransferases (SULTs).

2. In this study, we have analyzed the sulfation of 4-nitrophenol and other compounds in male and female bovine liver and characterized recombinant bovine SULT isoforms 1A1 and 1B1 expressed in Escherichia coli.

3. We found that, in contrast to most other mammalian species, the major phenol sulfotransferase SULT1A1 is not expressed in bovine liver. Rather SULT1B1 seems to be a major form in both male and female bovine liver.

4. We also identified kinetic differences between bovine and human SULT1A1 and, using the human SULT1A1 crystal structure, identified two amino acid positions in the active site of bovine SULT1A1 (Ile₈₉Val and Phe₂₄₇Val) that may be responsible for these differences.

• Cattle
• liver
• sulfotransferase
• SULT1A1
• SULT1B1

Acknowledgements

The authors are grateful to Matthew J. Zaya for assistance with procuring tissue samples.

Declaration of interest

The authors report no declarations of interest relevant to this work.

K. V. C. was supported by an Industrial CASE Studentship from the Biotechnology & Biological Sciences Research Council in collaboration with Pfizer. This work was also supported through an equipment grant (to M. W. H. C.) from Tenovus Tayside.