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Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants.
Lethe, Mary Caroline L; Paris, Vincent; Wang, Xiaoqiang; Chan, Clement T Y.
Afiliação
  • Lethe MCL; Department of Biomedical Engineering, College of Engineering, University of North Texas, 3940 N Elm Street, Denton, TX 76207, USA.
  • Paris V; Department of Biomedical Engineering, College of Engineering, University of North Texas, 3940 N Elm Street, Denton, TX 76207, USA.
  • Wang X; Department of Biological Sciences, College of Science, University of North Texas, 1155 Union Circle #305220, Denton, TX 76203, USA.
  • Chan CTY; BioDiscovery Institute, University of North Texas, 1155 Union Circle #305220, Denton, TX 76203, USA.
Int J Mol Sci ; 25(5)2024 Feb 28.
Article em En | MEDLINE | ID: mdl-38474028
ABSTRACT
The uridine diphosphate glycosyltransferase (UGT) superfamily plays a key role in the metabolism of xenobiotics and metabolic wastes, which is essential for detoxifying those species. Over the last several decades, a huge effort has been put into studying human and mammalian UGT homologs, but family members in other organisms have been explored much less. Potentially, other UGT homologs can have desirable substrate specificity and biological activities that can be harnessed for detoxification in various medical settings. In this review article, we take a plant UGT homology, UGT71G1, and compare its structural and biochemical properties with the human homologs. These comparisons suggest that even though mammalian and plant UGTs are functional in different environments, they may support similar biochemical activities based on their protein structure and function. The known biological functions of these homologs are discussed so as to provide insights into the use of UGT homologs from other organisms for addressing human diseases related to UGTs.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Difosfato de Uridina / Glicosiltransferases Limite: Animals / Humans Idioma: En Revista: Int J Mol Sci Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Difosfato de Uridina / Glicosiltransferases Limite: Animals / Humans Idioma: En Revista: Int J Mol Sci Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Estados Unidos