Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 392, Issue 5, Pages 1292-1302Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.08.017
Keywords
glycosylation; deglycosylation; uridine diphosphate glycosyltransferase; isoflavonoid; crystal structure
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Funding
- US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- National Science Foundation [0416883]
- Samuel Roberts Noble Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0416883] Funding Source: National Science Foundation
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The glycosyltransferase UGT78G1 from Medicago truncatula catalyzes the glycosylation of various (iso)flavonoids such as the flavonols kaempferol and myricetin, the isoflavone formononetin, and the anthocyanidins pelargonidin and cyanidin. It also catalyzes a reverse reaction to remove the sugar moiety from glycosides. The structures of UGT78G1 bound with uridine diphosphate or with both uridine diphosphate and myricetin were determined at 2.1 angstrom resolution, revealing detailed interactions between the enzyme and substrates/products and suggesting a distinct binding mode for the acceptor/product. Comparative structural analysis and mutagenesis identify glutamate 192 as a key amino acid for the reverse reaction. This information provides a basis for enzyme engineering to manipulate substrate specificity and to design effective biocatalysts with glycosylation and/or cleglycosylation activity. (C) 2009 Elsevier Ltd. All rights reserved.
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