Evidence map›Paper›PMID 28760417›Full record

ArticleCarbohydrate research2017

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

Ellis C O'Neill, Giulia Pergolizzi, Clare E M Stevenson, David M Lawson, Sergey A Nepogodiev, Robert A Field

Open access · hybridAbstract read
In one paragraph

Article in Carbohydrate research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.7field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Broadening the Substrate Specificity of Cellobiose Phosphorylase fromInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Article
  7. Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022
    Review
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  12. Article
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  18. Article
  19. Identification ofThe Journal of biological chemistry · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Ellis C O'NeillDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
Giulia PergolizziDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
Clare E M StevensonDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
David M LawsonDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
Sergey A NepogodievDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
Robert A FieldDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK. Electronic address: rob.field@jic.ac.uk.
John Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L014130/1Biotechnology and Biological Sciences Research Council BBS/E/J/000C0618Biotechnology and Biological Sciences Research Council BBS/E/J/000PR9790
6 · The paper itself

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.

Indexed as

Crystallography, X-RayGlucosamineGlucosephosphatesGlucosyltransferasesMonosaccharidesOligosaccharidesSubstrate Specificitycellodextrin phosphorylaseGlucosamineglucosamine 1-phosphateGlucosephosphatesGlucosyltransferasesMonosaccharidesOligosaccharidesCellodextrin phosphorylaseGlucosamine 1-phosphateX-ray crystal structure

Identifiers

PMID28760417
PMCPMC5667895
OpenAlexW2738877273

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.