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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
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

Abstract: The GH94 glycoside hydrolase cellodextrin phosphorylase (CDP, EC 2.4.1.49) 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
Documents:
1-s2.0-S0008621517303592-main.pdf
Discipline Tags:
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)