Evidence map›Paper›PMID 25575592›Full record

ArticleThe Journal of biological chemistry2015

Biochemical characterization and structural analysis of a bifunctional cellulase/xylanase from Clostridium thermocellum.

Shuo-Fu Yuan, Tzu-Hui Wu, Hsiao-Lin Lee, Han-Yu Hsieh, Wen-Ling Lin, Barbara Yang, Chih-Kang Chang, Qian Li, Jian Gao, Chun-Hsiang Huang and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 68 citations in OpenAlex.

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  7. Insights into promiscuous chitosanases: the known and the unknown.Applied microbiology and biotechnology · 2022
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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

13 authors at 6 institutions in 3 countries.

Shuo-Fu Yuanthe Institute of Biochemical Sciences, and.
Tzu-Hui Wuthe Institute of Biotechnology, National Taiwan University, Taipei 10617, Taiwan and.
Hsiao-Lin LeeFrom the Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Han-Yu Hsiehthe Institute of Biochemical Sciences, and.
Wen-Ling LinFrom the Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Barbara Yangthe Institute of Biochemical Sciences, and.
Chih-Kang ChangFrom the Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
Qian Lithe Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Jian Gaothe Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Chun-Hsiang Huangthe Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China.
Meng-Chiao Hothe Institute of Biochemical Sciences, and From the Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan, joeho@gate.sinica.edu.tw.
Rey-Ting Guothe Industrial Enzymes National Engineering Laboratory, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences, Tianjin 300308, China guo_rt@tib.cas.cn.
Po-Huang Liangthe Institute of Biochemical Sciences, and From the Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan, phliang@gate.sinica.edu.tw.
Biochemical Society · GBChinese Academy of Sciences · CNInstitute of Biological Chemistry, Academia Sinica · TWAcademia Sinica · TWNational Taiwan University · TWTianjin Institute of Industrial Biotechnology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We expressed an active form of CtCel5E (a bifunctional cellulase/xylanase from Clostridium thermocellum), performed biochemical characterization, and determined its apo- and ligand-bound crystal structures. From the structures, Asn-93, His-168, His-169, Asn-208, Trp-347, and Asn-349 were shown to provide hydrogen-bonding/hydrophobic interactions with both ligands. Compared with the structures of TmCel5A, a bifunctional cellulase/mannanase homolog from Thermotoga maritima, a flexible loop region in CtCel5E is the key for discriminating substrates. Moreover, site-directed mutagenesis data confirmed that His-168 is essential for xylanase activity, and His-169 is more important for xylanase activity, whereas Asn-93, Asn-208, Tyr-270, Trp-347, and Asn-349 are critical for both activities. In contrast, F267A improves enzyme activities.

Indexed as

Protein Structure, TertiaryAcetivibrio thermocellusAmino AcidsAmino Acid SequenceBacterial ProteinsBinding SitesCatalytic DomainCellobioseCellulaseCrystallography, X-RayDisaccharidesEndo-1,4-beta XylanasesEnzyme AssaysKineticsModels, MolecularMolecular Sequence DataAmino AcidsBacterial ProteinsCellobioseCellulaseDisaccharidesEndo-1,4-beta XylanasesRecombinant ProteinsxylobioseBiodegradationBiofuelSite-directed MutagenesisSubstrate SpecificityX-ray Crystallography

Identifiers

PMID25575592
PMCPMC4342484
OpenAlexW2135123110

What OpenQuestion holds

Textmetadata
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.