absidia coerulea
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Author(s):  
Jonathan Messias de Souza ◽  
Mario Ferreira Conceição Santos ◽  
Rita Cassia Nascimento Pedroso ◽  
Leticia Pereira Pimenta ◽  
Kátia Aparecida Siqueira ◽  
...  

2019 ◽  
Vol 93 ◽  
pp. 102750 ◽  
Author(s):  
Sandra Sordon ◽  
Jarosław Popłoński ◽  
Tomasz Tronina ◽  
Ewa Huszcza

2019 ◽  
Vol 26 (8) ◽  
pp. 7804-7809 ◽  
Author(s):  
Lijun Zhou ◽  
Zhilin Zhang ◽  
Mi Wei ◽  
Yongjian Xie ◽  
Shan He ◽  
...  

2017 ◽  
Vol 20 (8) ◽  
pp. 719-726
Author(s):  
Yan Song ◽  
Sen-Sen Yan ◽  
Hai-Jun Lin ◽  
Jian-Lin Li ◽  
Xu-Guang Zhai ◽  
...  

2017 ◽  
Vol 171 ◽  
pp. 254-261 ◽  
Author(s):  
Ruijie Wang ◽  
Pengcheng Sui ◽  
Xiangjiang Hou ◽  
Tong Cao ◽  
Longgang Jia ◽  
...  

2017 ◽  
Vol 83 (8) ◽  
Author(s):  
Kebo Xie ◽  
Xiaoxiang Dou ◽  
Ridao Chen ◽  
Dawei Chen ◽  
Cheng Fang ◽  
...  

ABSTRACT In the present study, two novel phenolic UDP glycosyltransferases (P-UGTs), UGT58A1 and UGT59A1, which can transfer sugar moieties from active donors to phenolic acceptors to generate corresponding glycosides, were identified in the fungal kingdom. UGT58A1 (from Absidia coerulea) and UGT59A1 (from Rhizopus japonicas) share a low degree of homology with known UGTs from animals, plants, bacteria, and viruses. These two P-UGTs are membrane-bound proteins with an N-terminal signal peptide and a transmembrane domain at the C terminus. Recombinant UGT58A1 and UGT59A1 are able to regioselectively and stereoselectively glycosylate a variety of phenolic aglycones to generate the corresponding glycosides. Phylogenetic analysis revealed the novelty of UGT58A1 and UGT59A1 in primary sequences in that they are distantly related to other UGTs and form a totally new evolutionary branch. Moreover, UGT58A1 and UGT59A1 represent the first members of the UGT58 and UGT59 families, respectively. Homology modeling and mutational analysis implied the sugar donor binding sites and key catalytic sites, which provided insights into the catalytic mechanism of UGT58A1. These results not only provide an efficient enzymatic tool for the synthesis of bioactive glycosides but also create a starting point for the identification of P-UGTs from fungi at the molecular level. IMPORTANCE Thus far, there have been many reports on the glycosylation of phenolics by fungal cells. However, no P-UGTs have ever been identified in fungi. Our study identified fungal P-UGTs at the molecular level and confirmed the existence of the UGT58 and UGT59 families. The novel sequence information on UGT58A1 and UGT59A1 shed light on the exciting and new P-UGTs hiding in the fungal kingdom, which would lead to the characterization of novel P-UGTs from fungi. Molecular identification of fungal P-UGTs not only is theoretically significant for a better understanding of the evolution of UGT families but also can be applied as a powerful tool in the glycodiversification of bioactive natural products for drug discovery.


Planta Medica ◽  
2015 ◽  
Vol 81 (11) ◽  
Author(s):  
F Han ◽  
IS Lee
Keyword(s):  

2015 ◽  
Vol 402 ◽  
pp. 236-240 ◽  
Author(s):  
Xu Pang ◽  
Di Wen ◽  
Yang Zhao ◽  
Cheng-Qi Xiong ◽  
Xiao-Qin Wang ◽  
...  

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