In:
Microbial Biotechnology, Wiley, Vol. 12, No. 4 ( 2019-07), p. 763-774
Abstract:
Glycosylation of natural products can influence their pharmacological properties, and efficient glycosyltransferases ( GT s) are critical for this purpose. The polyketide epothilones are potent anti‐tumour compounds, and YjiC is the only reported GT for the glycosylation of epothilone. In this study, we phylogenetically analysed 8261 GT s deposited in CAZ y database and revealed that YjiC locates in a subbranch of the Macrolide I group, forming the YjiC‐subbranch with 160 GT sequences. We demonstrated that the YjiC‐subbranch GT s are normally efficient in epothilone glycosylation, but some showed low glycosylation activities. Sequence alignment of YjiC‐subbranch showed that the 66th and 77th amino acid residues, which were close to the catalytic cavity in molecular docking model, were conserved in five high‐active GT s (Q66 and P77) but changed in two low‐efficient GT s. Site‐directed residues swapping at the two positions in the two low‐active GT s (Bss GT and Bam GT ) and the high‐active GT Bs GT ‐1 demonstrated that the two amino acid residues played an important role in the catalytic efficiency of epothilone glycosylation. This study highlights that the potent GT s for appointed compounds are phylogenetically grouped with conserved residues for the catalytic efficiency.
Type of Medium:
Online Resource
ISSN:
1751-7915
,
1751-7915
DOI:
10.1111/mbt2.2019.12.issue-4
DOI:
10.1111/1751-7915.13421
Language:
English
Publisher:
Wiley
Publication Date:
2019
detail.hit.zdb_id:
2406063-X
