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A β-mannanase with a lysozyme-like fold and a novel molecular catalytic mechanism

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Author(s)

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

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Publication details

JournalACS Central Science
DateE-pub ahead of print - 8 Nov 2016
DatePublished (current) - 28 Dec 2016
Issue number12
Volume2
Number of pages8
Pages (from-to)896-903
Early online date8/11/16
Original languageEnglish

Abstract

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 with inversion of stereochemistry. A Michaelis complex with mannopentaose, and a product complex with mannotriose, reveal ligands with pyranose rings distorted in an unusual inverted chair conformation. Ab initio quantum mechanics/molecular mechanics metadynamics quantified the energetically accessible ring conformations and provided evidence in support of a 1C43H4 3S1 conformational itinerary along the reaction coordinate. This work, in concert with that on GH family 124 cellulases, reveals how the lysozyme fold can be co-opted to catalyze the hydrolysis of different polysaccharides in a mechanistically distinct manner.

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© 2016, American Chemical Society. Uploaded with permission of the publisher/copyright holder. Further copying may not be permitted; contact the publisher for details.

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