Journal article

A beta-Mannanase with a Lysozyme-like Fold and a Novel Molecular Catalytic Mechanism

Yi Jin, Marija Petricevic, Alan John, Lluis Raich, Huw Jenkins, Leticia Portela De Souza, Fiona Cuskin, Harry J Gilbert, Carme Rovira, Ethan D Goddard-Borger, Spencer J Williams, Gideon J Davies



The enzymatic cleavage of β-1,4-mannans is achieved by endo-β-1,4-mannanases, enzymes involved in germination of seeds and microbial hemicellulose degradation, and which have increasing industrial and consumer product applications. β-Mannanases occur in a range of families of the CAZy sequence-based glycoside hydrolase (GH) classification scheme including families 5, 26, and 113. In this work we reveal that β-mannanases of the newly described GH family 134 differ from other mannanase families in both their mechanism and tertiary structure. A representative GH family 134 endo-β-1,4-mannanase from a Streptomyces sp. displays a fold closely related to that of hen egg white lysozyme but acts wit..

View full abstract


Awarded by Australian Research Council

Awarded by European Research Council


Awarded by Spanish Ministry of Economy and Competitiveness (MINECO)

Awarded by Generalitat de Catalunya

Funding Acknowledgements

Australian Research Council (FT130100103), the European Research Council (ERC-2012-AdG-322942), the Ramaciotti Foundation and VESKI with additional support from the Australian Cancer Research Foundation and Victorian State Government Operational Infrastructure Support, NHMRC IRIISS Grant 9000220, the Spanish Ministry of Economy and Competitiveness (MINECO, CTQ2014-55174-P) and the Generalitat de Catalunya (2014SGR-987). G.J.D. is supported by the Royal Society. We acknowledge the staff of the Diamond Light Source (UK) for provision of I02 beamline facilities (Proposal Number mx-9948), and the support, technical expertise, and assistance provided by the Barcelona Super-computing Center: Centro Nacional de Supercomputacion (BSC-CNS). L.R. acknowledges a Ph.D. fellowship from the University of Barcelona (APIF-UB).