scholarly journals Structural and Functional Characterization of a Lytic Polysaccharide Monooxygenase with Broad Substrate Specificity

2015 ◽  
Vol 290 (38) ◽  
pp. 22955-22969 ◽  
Author(s):  
Anna S. Borisova ◽  
Trine Isaksen ◽  
Maria Dimarogona ◽  
Abhishek A. Kognole ◽  
Geir Mathiesen ◽  
...  
FEBS Letters ◽  
2015 ◽  
Vol 590 (1) ◽  
pp. 34-42 ◽  
Author(s):  
Sophanit Mekasha ◽  
Zarah Forsberg ◽  
Bjørn Dalhus ◽  
John-Paul Bacik ◽  
Swati Choudhary ◽  
...  

PLoS ONE ◽  
2018 ◽  
Vol 13 (8) ◽  
pp. e0202148 ◽  
Author(s):  
Marco A. S. Kadowaki ◽  
Anikó Várnai ◽  
John-Kristian Jameson ◽  
Ana E. T. Leite ◽  
Antonio J. Costa-Filho ◽  
...  

PLoS ONE ◽  
2016 ◽  
Vol 11 (12) ◽  
pp. e0167580 ◽  
Author(s):  
Natalia P. Zakataeva ◽  
Dmitriy V. Romanenkov ◽  
Yuliya R. Yusupova ◽  
Victoria S. Skripnikova ◽  
Takayuki Asahara ◽  
...  

Author(s):  
Jolanta Cieślak ◽  
Akimasa Miyanaga ◽  
Makoto Takaishi ◽  
Fumitaka Kudo ◽  
Tadashi Eguchi

Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5′-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1 Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids.


2020 ◽  
Vol 105 (1) ◽  
pp. 197-210
Author(s):  
Benjarat Bunterngsook ◽  
Wuttichai Mhuantong ◽  
Pattanop Kanokratana ◽  
Yu Iseki ◽  
Takashi Watanabe ◽  
...  

2014 ◽  
Vol 37 (3) ◽  
pp. 657-658
Author(s):  
Han Beur Na ◽  
Won Kyeong Jung ◽  
Yu Seok Jeong ◽  
Hee Jung Kim ◽  
Sung Kyum Kim ◽  
...  

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