7DWC

Bacteroides thetaiotaomicron VPI5482 BTAxe1

Summary for 7DWC

• Entry DOI: 10.2210/pdb7dwc/pdb
• Descriptor: Xylanase (2 entities in total)
• Functional Keywords: bacteroides thetaiotaomicron vpi5482, acetyl xylan esterase, gut bacteria-derived, hydrolase
• Biological source: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
• Total number of polymer chains: 4
• Total formula weight: 117886.52

Authors

Wang, L.Y.,Wang, Y.L.,Xin, F.J.,Sun, L.C. (deposition date: 2021-01-17, release date: 2022-01-19, Last modification date: 2023-11-29)

Primary citation

Wang, L.,Han, X.,Wang, Y.,Wei, X.,Liu, S.,Shao, S.,Yang, S.,Sun, L.,Xin, F.
Rational Design for Broadened Substrate Specificity and Enhanced Activity of a Novel Acetyl Xylan Esterase from Bacteroides thetaiotaomicron.
J.Agric.Food Chem., 69:6665-6675, 2021

PubMed Abstract: Gut bacteria-derived enzymes play important roles in the metabolism of dietary fiber through enabling the hydrolysis of polysaccharides. In this study, we identified and characterized a 29 kDa novel acetyl xylan esterase, Axe1, from VPI5482. Then, we solved the structure of Axe1 and performed the rational design. Mutants N65S and N65A increased the activities toward short-chain (NPA, NPB) to near four-fold, and gained the activities toward longer-chain substrate (NPO). Molecular docking analysis showed that the mutant N65S had a larger substrate binding pocket than the wild type. Hydrolysis studies using natural substrates showed that either N65S or N65A showed higher activity of that of wild-type, yielding 131.31 and 136.09 mM of acetic acid from xylan. This is the first study on the rational design of gut bacteria-derived Axes with broadened substrate specificity and enhanced activity, which can be referenced by other acetyl esterases or gut-derived enzymes.

PubMed: 34074097
DOI: 10.1021/acs.jafc.1c00750

Experimental method

X-RAY DIFFRACTION (1.804 Å)