Structural highlights
Publication Abstract from PubMed
The GH94 glycoside hydrolase cellodextrin phosphorylase (CDP, EC 2.4.1.49) produces cellodextrin oligomers from short beta-1-->4-glucans and alpha-D-glucose 1-phosphate. Compared to cellobiose phosphorylase (CBP), which produces cellobiose from glucose and alpha-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 alpha-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.
Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis.,O'Neill EC, Pergolizzi G, Stevenson CEM, Lawson DM, Nepogodiev SA, Field RA Carbohydr Res. 2017 Jul 21. pii: S0008-6215(17)30359-2. doi:, 10.1016/j.carres.2017.07.005. PMID:28760417[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ O'Neill EC, Pergolizzi G, Stevenson CEM, Lawson DM, Nepogodiev SA, Field RA. Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis. Carbohydr Res. 2017 Jul 21. pii: S0008-6215(17)30359-2. doi:, 10.1016/j.carres.2017.07.005. PMID:28760417 doi:http://dx.doi.org/10.1016/j.carres.2017.07.005
