7erx
Glycosyltransferase in complex with UDP and STB
Structural highlights
FunctionPublication Abstract from PubMedSteviol glycosides are the intensely sweet components of extracts from Stevia rebaudiana. These molecules comprise an invariant steviol aglycone decorated with variable glycans and could widely serve as a low-calorie sweetener. However, the most desirable steviol glycosides Reb D and Reb M, devoid of unpleasant aftertaste, are naturally produced only in trace amounts due to low levels of specific beta (1-2) glucosylation in Stevia. Here, we report the biochemical and structural characterization of OsUGT91C1, a glycosyltransferase from Oryza sativa, which is efficient at catalyzing beta (1-2) glucosylation. The enzyme's ability to bind steviol glycoside substrate in three modes underlies its flexibility to catalyze beta (1-2) glucosylation in two distinct orientations as well as beta (1-6) glucosylation. Guided by the structural insights, we engineer this enzyme to enhance the desirable beta (1-2) glucosylation, eliminate beta (1-6) glucosylation, and obtain a promising catalyst for the industrial production of naturally rare but palatable steviol glycosides. Catalytic flexibility of rice glycosyltransferase OsUGT91C1 for the production of palatable steviol glycosides.,Zhang J, Tang M, Chen Y, Ke D, Zhou J, Xu X, Yang W, He J, Dong H, Wei Y, Naismith JH, Lin Y, Zhu X, Cheng W Nat Commun. 2021 Dec 2;12(1):7030. doi: 10.1038/s41467-021-27144-4. PMID:34857750[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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