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Cellodextrin phosphorylase from Ruminiclostridium thermocellum : X-ray crystal structure and substrate specificity analysis

DOI: 10.1016/j.carres.2017.07.005 DOI Help

Authors: Ellis C. O'Neill (John Innes Centre) , Giulia Pergolizzi (John Innes Centre) , Clare E. M. Stevenson (John Innes Centre) , David M. Lawson (John Innes Centre) , Sergey A. Nepogodiev (John Innes Centre) , Robert A. Field (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Carbohydrate Research

State: Published (Approved)
Published: July 2017
Diamond Proposal Number(s): 7641

Open Access Open Access

Abstract: The GH94 glycoside hydrolase cellodextrin phosphorylase (CDP, EC produces cellodextrin oligomers from short β-1→4-glucans and α-D-glucose 1-phosphate. Compared to cellobiose phosphorylase (CBP), which produces cellobiose from glucose and α-D-glucose 1-phosphate, CDP is biochemically less well characterised. Herein, we investigate the donor and acceptor substrate specificity of recombinant CDP from Ruminiclostridium thermocellum and we isolate and characterise a glucosamine addition product to the cellobiose acceptor with the non-natural donor α-D-glucosamine 1-phosphate. In addition, we report the first X-ray crystal structure of CDP, along with comparison to the available structures from CBPs and other closely related enzymes, which contributes to understanding of the key structural features necessary to discriminate between monosaccharide (CBP) and oligosaccharide (CDP) acceptor substrates.

Journal Keywords: Cellodextrin phosphorylase; Glucosamine 1-phosphate; X-ray crystal structure

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography

Added On: 26/07/2017 10:07


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)