Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function
- Lima, Marisa A.
- Oliveira Neto, Mario
- Kadowaki, Marco Antonio S.
- Rosseto, Flavio R.
- Prates, Erica T.
- Squina, Fabio M.
- Leme, Adriana F. P.
- Skaf, Munir S.
- Polikarpov, Igor
View in ORKG
DOIAbstract
Background: β-Glucosidase completes cellulose enzymatic hydrolysis by releasing glucose from cellobiose. Results: SAXS experiments revealed that Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape, uncommon to enzymes that act on the soluble substrates. Conclusion: We show that AnBgl1 N- and C-terminal domains are linked by a long extended linker. Significance: Understanding AnBgl1 architecture is useful for comprehension of the enzyme-cell wall interaction and the process of biomass saccharification.FAPESP (08/56255-9, 09/54035-4, 10/16542-9)CNPq (490022/2009-0)CAPESINCT do Bioetano