| Comments: |
The enzyme, characterized from the bacterium Bacillus licheniformis DSM-13, is an extremely promiscuous glycosyltransferase. It can accept ADP-, GDP-, CDP-, TDP-, or UDP-activated glycose molecules as donors, and can glycosylate a large number of substrates, catalysing O-, N-, or S-glycosylation. While D-glucose is the primarily reported sugar being transferred, the enzyme has been shown to transfer D-galactose, 2-deoxy-D-glucose, N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, L-fucose, L-rhamnose, D-glucuronate, and D-viosamine. |
| References: |
| 1. |
Pandey, R.P., Parajuli, P., Koirala, N., Park, J.W. and Sohng, J.K. Probing 3-hydroxyflavone for in vitro glycorandomization of flavonols by YjiC. Appl. Environ. Microbiol. 79 (2013) 6833–6838. [DOI] [PMID: 23974133] |
| 2. |
Pandey, R.P., Gurung, R.B., Parajuli, P., Koirala, N., Tuoi le, T. and Sohng, J.K. Assessing acceptor substrate promiscuity of YjiC-mediated glycosylation toward flavonoids. Carbohydr. Res. 393 (2014) 26–31. [DOI] [PMID: 24893262] |
| 3. |
Pandey, R.P., Parajuli, P., Shin, J.Y., Lee, J., Lee, S., Hong, Y.S., Park, Y.I., Kim, J.S. and Sohng, J.K. Enzymatic biosynthesis of novel resveratrol glucoside and glycoside derivatives. Appl. Environ. Microbiol. 80 (2014) 7235–7243. [DOI] [PMID: 25239890] |
| 4. |
Parajuli, P., Pandey, R.P., Koirala, N., Yoon, Y.J., Kim, B.G. and Sohng, J.K. Enzymatic synthesis of epothilone A glycosides. AMB Express 4:31 (2014). [DOI] [PMID: 24949266] |
| 5. |
Pandey, R.P., Parajuli, P., Gurung, R.B. and Sohng, J.K. Donor specificity of YjiC glycosyltransferase determines the conjugation of cytosolic NDP-sugar in in vivo glycosylation reactions. Enzyme Microb. Technol. 91 (2016) 26–33. [DOI] [PMID: 27444326] |
| 6. |
Bashyal, P., Thapa, S.B., Kim, T.S., Pandey, R.P. and Sohng, J.K. Exploring the nucleophilic N- and S-glycosylation capacity of Bacillus licheniformis YjiC enzyme. J. Microbiol. Biotechnol. 30 (2020) 1092–1096. [DOI] [PMID: 32238768] |
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