Mechanistic investigation of B12-independent glycerol dehydratase and its activating enzyme GD-AE

B12-Independent glycerol dehydratase (GD) is a glycyl radical enzyme in the biotransformation of glycerol to 1,3-propanediol. GD requires the activating enzyme GD-AE to initiate the radical reaction. GD-AE belongs to the radical -adenosyl-L-methionine (SAM) enzyme superfamily. However, a previous st...

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Published inChemical communications (Cambridge, England) Vol. 58; no. 16; pp. 2738 - 2741
Main Authors Li, Yaoyang, Yao, Yadi, Yu, Lu, Tian, Changlin, Dong, Min
Format Journal Article
LanguageEnglish
Published England Royal Society of Chemistry 22.02.2022
Subjects
Biocatalysis
Biotransformation
Dehydration
Deoxyadenosines - chemistry
Deoxyadenosines - metabolism
Electron Spin Resonance Spectroscopy
Enzymes
Glycerol
Hydro-Lyases - metabolism
Hydroxyl groups
Methionine
Molecular Structure
S-Adenosylmethionine - chemistry
S-Adenosylmethionine - metabolism
Vitamin B 12 - metabolism
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Summary:B12-Independent glycerol dehydratase (GD) is a glycyl radical enzyme in the biotransformation of glycerol to 1,3-propanediol. GD requires the activating enzyme GD-AE to initiate the radical reaction. GD-AE belongs to the radical -adenosyl-L-methionine (SAM) enzyme superfamily. However, a previous study showed that GD-AE cleaves SAM unconventionally to generate 5'-deoxy-5'-methylthioadenosine. Herein, we show that GD-AE actually cleaves SAM to form 5'-deoxyadenosine, similar to other radical SAM enzymes. Furthermore, with the synthesized glycerol analogue 2-deoxy-2-fluoroglycerol, we demonstrate that B12-independent GD catalyzes the glycerol dehydration reaction by direct elimination of the C-2 hydroxyl group of a ketyl radical rather than 1,2-OH migration.
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ISSN:1359-7345
1364-548X
DOI:10.1039/d1cc06991h