The enzymatic mechanism of the extreme heat-obsessed microorganism Arabic furan and its synergetic degradation effect with wood polysaccharides.

Wood cellulose is one of the most abundant renewable resources on earth, and its synthesis and degradation are the central link of the carbon cycle in nature.
plant cell walls form a natural "anti-degradation barrier" during evolution, especially in hemicellulose, most polysaccharides contain side-chain modification, degradation difficulties.
The Microbial Resources Team at the Qingdao Institute of Bioenermaceutical Energy and Process of the Chinese Academy of Sciences is dedicated to the study of the mechanisms by which heat-addictive microorganisms degrade ligand cellulose, in collaboration with Robert Kelly, a professor at North Carolina State University in the United States, to clarify the enzyme-thalising mechanism of the extreme heat-obsessed microbiome Caldice llulosiruptor Arabic furan and its synergistic degradation effects with lithosomes, which are important for biodegradation of ligand cellulose, published in Appleid Environmental Microbiology (AEM).
In addition, cellulose-degrading glycoside hydrolytic enzymes, a large number of 5 families, with cellulase and canonyl polyglycase and other activities, but the two-function cellulase / cloth polysaccharide substrate selection mechanism is not clear.
Qingdao Energy Institute's Microbial Resources Team worked with Feng Yingang, a researcher in the metabolomics team, Yao Lishan, a researcher in the simulation team, and Wang Xinquan, a professor at Tsinghua University, to analyze the extreme heat anaerobic bacteria Caldicellulosiruptor sp. The protein and protein substrate complex structure of F32 glycoside hydrolytic enzyme F32EG5 reveals the selective mechanism of substrate.
the work has been published online in Biochemical Journal.
team found that F32EG5 was able to cut off beta-1, 3-1, 4-glucosaccharide substrates, 3-glycoside bonds or beta-1, 3-glycoside bonds in front of beta-1 The 4-glycoside bond, in contrast to the traditional GH16 family lithic polysaccharidease (cut off the beta-1, 3-glycoside bond behind the beta-1, 4-glycoside bond), is a new beta-glucosine bond cut off.
F32EG5 has a typical GH5 family protein (beta/alpha) 8 barrel structure, with a unique substrate binding point, determines the substrate specificity. The
composite structure shows that F32EG5 has a sharply curved substrate binding hole path, which is specifically combined with beta-1, 3-1, 4-glucosaccharide substrates with the same curved structure, which determines the activity of the protein's highland polyglycoenzyme.
molecular dynamics simulation and fixed-point mutation analysis to verify the above scenario.
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