Glycoside-metabolizing oxidoreductase D3dgpA from human gut bacteriumopen access
- Authors
- Kim, Heji; Mi, Huynh Thi Ngoc; Ahn, Joong-Hoon; Lee, Jong Suk; Eser, Bekir Engin; Choi, Jongkeun; Han, Jaehong
- Issue Date
- Jun-2024
- Publisher
- FRONTIERS MEDIA SA
- Keywords
- deglycosylation; D3dgpA; Gfo/Idh/MocA family; glycosides; NAD(+); oxidoreductase
- Citation
- FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY, v.12
- Journal Title
- FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
- Volume
- 12
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/75412
- DOI
- 10.3389/fbioe.2024.1413854
- ISSN
- 2296-4185
- Abstract
- The Gfo/Idh/MocA family enzyme DgpA was known to catalyze the regiospecific oxidation of puerarin to 3"-oxo-puerarin in the presence of 3-oxo-glucose. Here, we discovered that D3dgpA, dgpA cloned from the human gut bacterium Dorea sp. MRG-IFC3, catalyzed the regiospecific oxidation of various C-/O-glycosides, including puerarin, in the presence of methyl beta-D-3-oxo-glucopyranoside. While C-glycosides were converted to 3"- and 2"-oxo-products by D3dgpA, O-glycosides resulted in the formation of aglycones and hexose enediolone from the 3"-oxo-products. From DFT calculations, it was found that isomerization of 3"-oxo-puerarin to 2"-oxo-puerarin required a small activation energy of 9.86 kcal/mol, and the O-glycosidic bond cleavage of 3"-oxo-products was also thermodynamically favored with a small activation energy of 3.49 kcal/mol. In addition, the reaction mechanism of D3dgpA was discussed in comparison to those of Gfo/Idh/MocA and GMC family enzymes. The robust reactivity of D3dgpA was proposed as a new general route for derivatization of glycosides.
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