NMR analysis of the binding mode of two fungal endo-β-1, 4-mannanases from GH5 and GH26 families. Issue 1 (16th November 2015)

• Record Type: Journal Article
• Authors: Marchetti, Roberta; Berrin, Jean-Guy; Couturier, Marie; Ul Qader, Shah Ali; Molinaro, Antonio; Silipo, Alba
• Is Part Of: Organic & biomolecular chemistry. Volume 14:Issue 1(2016)
• Page Start: 314
• Page End: 322
• Publication Date: 2015-11-16
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c5ob01851j
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : A different mode of action among two endo -β-1, 4 mannanases from Podospora anserina has been revealed through an accurate NMR analysis. Abstract : The enzymatic digestion of the main components of lignocellulosic biomass, including plant cell wall mannans, constitutes a fundamental step in the renewable biofuel production, with great potential benefit in the industrial field. Despite several reports of X-ray structures of glycoside hydrolases, how polysaccharides are specifically recognized and accommodated in the enzymes binding site still remains a pivotal matter of research. Within this frame, NMR spectroscopic techniques provide key binding information, complementing and/or enhancing the structural view by X-ray crystallography. Here we provide deep insights into the binding mode of two endo -β-1, 4 mannanases from the coprophilous ascomycete Podospora anserina, Pa Man26A and Pa Man5A, involved in the hydrolysis of plant cell wall mannans and heteromannans. The investigation at a molecular level of the interaction between the wild-type enzymes and inactive mutants with manno-oligosaccharides, revealed a different mode of action among the two glycoside hydrolases most likely due to the presence of the additional and peculiar −4 subsite in the Pa Man26A binding pocket.