Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants
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...
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MDPI AG
2024-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/25/5/2782 |
| _version_ | 1797264457826566144 |
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| author | Mary Caroline L. Lethe Vincent Paris Xiaoqiang Wang Clement T. Y. Chan |
| author_facet | Mary Caroline L. Lethe Vincent Paris Xiaoqiang Wang Clement T. Y. Chan |
| author_sort | Mary Caroline L. Lethe |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-25T00:29:13Z |
| format | Article |
| id | doaj.art-9f27fb0a2adc47f081cafd8cb9dac05c |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-04-25T00:29:13Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-9f27fb0a2adc47f081cafd8cb9dac05c2024-03-12T16:46:18ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-02-01255278210.3390/ijms25052782Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and PlantsMary Caroline L. Lethe0Vincent Paris1Xiaoqiang Wang2Clement T. Y. Chan3Department of Biomedical Engineering, College of Engineering, University of North Texas, 3940 N Elm Street, Denton, TX 76207, USADepartment of Biomedical Engineering, College of Engineering, University of North Texas, 3940 N Elm Street, Denton, TX 76207, USADepartment of Biological Sciences, College of Science, University of North Texas, 1155 Union Circle #305220, Denton, TX 76203, USADepartment of Biomedical Engineering, College of Engineering, University of North Texas, 3940 N Elm Street, Denton, TX 76207, USAThe 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.https://www.mdpi.com/1422-0067/25/5/2782uridine diphosphate glycosyltransferasesglycosylationsubstrate specificityUGT-related diseases |
| spellingShingle | Mary Caroline L. Lethe Vincent Paris Xiaoqiang Wang Clement T. Y. Chan Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants International Journal of Molecular Sciences uridine diphosphate glycosyltransferases glycosylation substrate specificity UGT-related diseases |
| title | Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants |
| title_full | Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants |
| title_fullStr | Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants |
| title_full_unstemmed | Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants |
| title_short | Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants |
| title_sort | similarities in structure and function of udp glycosyltransferase homologs from human and plants |
| topic | uridine diphosphate glycosyltransferases glycosylation substrate specificity UGT-related diseases |
| url | https://www.mdpi.com/1422-0067/25/5/2782 |
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