Cargando…
UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis
Glycosyltransferases constitute a large family of enzymes across all domains of life, but knowledge of their biochemical function remains largely incomplete, particularly in the context of plant specialized metabolism. The labdane diterpenes represent a large class of phytochemicals with many pharma...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8427245/ https://www.ncbi.nlm.nih.gov/pubmed/34363833 http://dx.doi.org/10.1016/j.jbc.2021.101045 |
_version_ | 1783750154330832896 |
---|---|
author | Srivastava, Payal Garg, Anchal Misra, Rajesh Chandra Chanotiya, Chandan Singh Ghosh, Sumit |
author_facet | Srivastava, Payal Garg, Anchal Misra, Rajesh Chandra Chanotiya, Chandan Singh Ghosh, Sumit |
author_sort | Srivastava, Payal |
collection | PubMed |
description | Glycosyltransferases constitute a large family of enzymes across all domains of life, but knowledge of their biochemical function remains largely incomplete, particularly in the context of plant specialized metabolism. The labdane diterpenes represent a large class of phytochemicals with many pharmacological benefits, such as anti-inflammatory, hepatoprotective, and anticarcinogenic. The medicinal plant kalmegh (Andrographis paniculata) produces bioactive labdane diterpenes; notably, the C19-hydroxyl diterpene (andrograpanin) is predominantly found as C19-O-glucoside (neoandrographolide), whereas diterpenes having additional hydroxylation(s) at C3 (14-deoxy-11,12-didehydroandrographolide) or C3 and C14 (andrographolide) are primarily detected as aglycones, signifying scaffold-selective C19-O-glucosylation of diterpenes in planta. Here, we analyzed UDP-glycosyltransferase (UGT) activity and diterpene levels across various developmental stages and tissues and found an apparent correlation of UGT activity with the spatiotemporal accumulation of neoandrographolide, the major diterpene C19-O-glucoside. The biochemical analysis of recombinant UGTs preferentially expressed in neoandrographolide-accumulating tissues identified a previously uncharacterized UGT86 member (ApUGT12/UGT86C11) that catalyzes C19-O-glucosylation of diterpenes with strict scaffold selectivity. ApUGT12 localized to the cytoplasm and catalyzed diterpene C19-O-glucosylation in planta. The substrate selectivity demonstrated by the recombinant ApUGT12 expressed in plant and bacterium hosts was comparable to native UGT activity. Recombinant ApUGT12 showed significantly higher catalytic efficiency using andrograpanin compared with 14-deoxy-11,12-didehydroandrographolide and trivial activity using andrographolide. Moreover, ApUGT12 silencing in plants led to a drastic reduction in neoandrographolide content and increased levels of andrograpanin. These data suggest the involvement of ApUGT12 in scaffold-selective C19-O-glucosylation of labdane diterpenes in plants. This knowledge of UGT86 function might help in developing plant chemotypes and synthesis of pharmacologically relevant diterpenes. |
format | Online Article Text |
id | pubmed-8427245 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-84272452021-09-13 UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis Srivastava, Payal Garg, Anchal Misra, Rajesh Chandra Chanotiya, Chandan Singh Ghosh, Sumit J Biol Chem Research Article Glycosyltransferases constitute a large family of enzymes across all domains of life, but knowledge of their biochemical function remains largely incomplete, particularly in the context of plant specialized metabolism. The labdane diterpenes represent a large class of phytochemicals with many pharmacological benefits, such as anti-inflammatory, hepatoprotective, and anticarcinogenic. The medicinal plant kalmegh (Andrographis paniculata) produces bioactive labdane diterpenes; notably, the C19-hydroxyl diterpene (andrograpanin) is predominantly found as C19-O-glucoside (neoandrographolide), whereas diterpenes having additional hydroxylation(s) at C3 (14-deoxy-11,12-didehydroandrographolide) or C3 and C14 (andrographolide) are primarily detected as aglycones, signifying scaffold-selective C19-O-glucosylation of diterpenes in planta. Here, we analyzed UDP-glycosyltransferase (UGT) activity and diterpene levels across various developmental stages and tissues and found an apparent correlation of UGT activity with the spatiotemporal accumulation of neoandrographolide, the major diterpene C19-O-glucoside. The biochemical analysis of recombinant UGTs preferentially expressed in neoandrographolide-accumulating tissues identified a previously uncharacterized UGT86 member (ApUGT12/UGT86C11) that catalyzes C19-O-glucosylation of diterpenes with strict scaffold selectivity. ApUGT12 localized to the cytoplasm and catalyzed diterpene C19-O-glucosylation in planta. The substrate selectivity demonstrated by the recombinant ApUGT12 expressed in plant and bacterium hosts was comparable to native UGT activity. Recombinant ApUGT12 showed significantly higher catalytic efficiency using andrograpanin compared with 14-deoxy-11,12-didehydroandrographolide and trivial activity using andrographolide. Moreover, ApUGT12 silencing in plants led to a drastic reduction in neoandrographolide content and increased levels of andrograpanin. These data suggest the involvement of ApUGT12 in scaffold-selective C19-O-glucosylation of labdane diterpenes in plants. This knowledge of UGT86 function might help in developing plant chemotypes and synthesis of pharmacologically relevant diterpenes. American Society for Biochemistry and Molecular Biology 2021-08-04 /pmc/articles/PMC8427245/ /pubmed/34363833 http://dx.doi.org/10.1016/j.jbc.2021.101045 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Srivastava, Payal Garg, Anchal Misra, Rajesh Chandra Chanotiya, Chandan Singh Ghosh, Sumit UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis |
title | UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis |
title_full | UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis |
title_fullStr | UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis |
title_full_unstemmed | UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis |
title_short | UGT86C11 is a novel plant UDP-glycosyltransferase involved in labdane diterpene biosynthesis |
title_sort | ugt86c11 is a novel plant udp-glycosyltransferase involved in labdane diterpene biosynthesis |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8427245/ https://www.ncbi.nlm.nih.gov/pubmed/34363833 http://dx.doi.org/10.1016/j.jbc.2021.101045 |
work_keys_str_mv | AT srivastavapayal ugt86c11isanovelplantudpglycosyltransferaseinvolvedinlabdanediterpenebiosynthesis AT garganchal ugt86c11isanovelplantudpglycosyltransferaseinvolvedinlabdanediterpenebiosynthesis AT misrarajeshchandra ugt86c11isanovelplantudpglycosyltransferaseinvolvedinlabdanediterpenebiosynthesis AT chanotiyachandansingh ugt86c11isanovelplantudpglycosyltransferaseinvolvedinlabdanediterpenebiosynthesis AT ghoshsumit ugt86c11isanovelplantudpglycosyltransferaseinvolvedinlabdanediterpenebiosynthesis |