Evidence map›Paper›PMID 27009476›Full record

ArticleScientific reports2016

Ligand-binding specificity and promiscuity of the main lignocellulolytic enzyme families as revealed by active-site architecture analysis.

Li Tian, Shijia Liu, Shuai Wang, Lushan Wang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

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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

13 citing papers in PubMed, 41 citations in OpenAlex.

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  7. A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering 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

4 authors at 2 institutions in 1 country.

Li TianThe State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, P.R. China.
Shijia LiuTaishan College, Shandong University, Jinan, 250100, P.R. China.
Shuai WangThe State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, P.R. China.
Lushan WangThe State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, P.R. China.
Shandong University · CNState Key Laboratory of Microbial Technology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomass can be converted into sugars by a series of lignocellulolytic enzymes, which belong to the glycoside hydrolase (GH) families summarized in CAZy databases. Here, using a structural bioinformatics method, we analyzed the active site architecture of the main lignocellulolytic enzyme families. The aromatic amino acids Trp/Tyr and polar amino acids Glu/Asp/Asn/Gln/Arg occurred at higher frequencies in the active site architecture than in the whole enzyme structure. And the number of potential subsites was significantly different among different families. In the cellulase and xylanase families, the conserved amino acids in the active site architecture were mostly found at the -2 to +1 subsites, while in β-glucosidase they were mainly concentrated at the -1 subsite. Families with more conserved binding amino acid residues displayed strong selectivity for their ligands, while those with fewer conserved binding amino acid residues often exhibited promiscuity when recognizing ligands. Enzymes with different activities also tended to bind different hydroxyl oxygen atoms on the ligand. These results may help us to better understand the common and unique structural bases of enzyme-ligand recognition from different families and provide a theoretical basis for the functional evolution and rational design of major lignocellulolytic enzymes.

Indexed as

Amino AcidsAmino Acid SequenceBiomassCatalytic DomainConserved SequenceGlycoside HydrolasesLigandsLigninModels, MolecularMultigene FamilyProtein BindingAmino AcidsGlycoside HydrolasesLigandsLigninlignocellulose

Identifiers

PMID27009476
PMCPMC4806347
OpenAlexW2317335193

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Registered trials

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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.