9NO3

The bifunctional arabinofuranosidase/xylosidase from metagenome of Pseudacanthotermes militaris.

This is a non-PDB format compatible entry.

Summary for 9NO3

• Entry DOI: 10.2210/pdb9no3/pdb
• Descriptor: TerARA - arabinofuranosidase/xylosidase from metagenome of Pseudacanthotermes militaris., CALCIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: bifunctional hemicellulase, arabinofuranosidase, xylosidase, metagenome, hydrolase
• Biological source: Pseudacanthotermes militaris
• Total number of polymer chains: 4
• Total formula weight: 221971.64

Authors

Gomes, B.M.,De Oliveira, G.S.,de Melo, V.S.,Rossini, N.O.,Dias, M.V.B.,Chambergo, F.S. (deposition date: 2025-03-07, release date: 2025-10-08, Last modification date: 2025-11-19)

Primary citation

Gomes, B.M.,de Oliveira, G.S.,de Melo, V.S.,Rossini, N.O.,Adriani, P.P.,Dias, M.V.B.,Chambergo, F.S.
Structural and functional characterization of a bifunctional GH43 alpha-L-arabinofuranosidase/ beta-xylosidase from the metagenome of Pseudacanthotermes militaris gut.
Int.J.Biol.Macromol., 329:147909-147909, 2025

PubMed Abstract: The pursuit of sustainable energy has intensified the search for efficient biocatalysts to convert lignocellulosic biomass. In this context, we characterized a novel bifunctional enzyme, TerARA, identified from the gut metagenome of the termite Pseudacanthotermes militaris. Belonging to the glycoside hydrolase 43 (GH43) family, TerARA was heterologously expressed in E. coli BL21 and purified. The enzyme demonstrated bifunctional activity toward synthetic substrates p-nitrophenyl-α-L-arabinofuranoside (pNP-Araf) (387.22 ± 74.2 U/mg) and p-nitrophenyl-β-D-xylopyranoside (pNP-Xyl) (330.82 ± 31.2 U/mg), with higher catalytic efficiency for pNP-Araf (9.14 s·mM), suggesting functional preference as an α-L-arabinofuranosidase. Activity modulation by metal ions revealed that Ca slightly improved efficiency toward pNP-Araf (to 9.58 s·mM at 1 mM), while Zn reduced efficiency for pNP-Xyl except at 5 mM (6.65 s·mM). Zn also enhanced enzymatic stability, maintaining 80 % activity in pNP-Xyl hydrolysis. Crystallographic analysis at 2.0 Å resolution revealed a 43 Glycosyl Hydrolase catalytic domain with a five-bladed β-propeller fold and two Ca ions and a Carbohydrate-Binding Module (CBM) domain with a β-sandwich fold likely involved in substrate interaction. Conserved catalytic residues, binding sites, and Ca stabilizing effects were identified. TerARA's bifunctionality and structural features support its application in hemicellulose degradation and biomass conversion.

PubMed: 41005405
DOI: 10.1016/j.ijbiomac.2025.147909

Experimental method

X-RAY DIFFRACTION (2.05 Å)