Evidence map›Paper›PMID 37178306›Full record

ArticleApplied microbiology and biotechnology2023

Structure and function characterization of the α-L-arabinofuranosidase from the white-rot fungus Trametes hirsuta.

Zhenyuan Si, Yang Cai, Lang Zhao, Lu Han, Feng Wang, Xiaobing Yang, Xiangdong Gao, Meiling Lu, Wei Liu

Abstract read
PubMed Publisher
In one paragraph

Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. 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

9 authors at 2 institutions in 1 country.

Zhenyuan SiJiangsu Key Laboratory of Druggability of Biopharmaceuticals, State Key Laboratory of Natural Medicines, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, PR China.
Yang CaiJiangsu Key Laboratory of Druggability of Biopharmaceuticals, State Key Laboratory of Natural Medicines, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, PR China.
Lang ZhaoJiangsu Key Laboratory of Druggability of Biopharmaceuticals, State Key Laboratory of Natural Medicines, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, PR China.
Lu HanJiangsu Key Laboratory of Druggability of Biopharmaceuticals, State Key Laboratory of Natural Medicines, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, PR China.
Feng WangSimcere Pharmaceutical Group Limited, Nanjing, 210042, PR China.
Xiaobing YangBiology and Medicine Department, Jiangsu Industrial Technology Research Institute, Nanjing, 210031, PR China.
Xiangdong GaoJiangsu Key Laboratory of Druggability of Biopharmaceuticals, State Key Laboratory of Natural Medicines, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, PR China. xdgao@cpu.edu.cn.
Meiling LuJiangsu Key Laboratory of Druggability of Biopharmaceuticals, State Key Laboratory of Natural Medicines, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, PR China. lumeiling@cpu.edu.cn.
Wei LiuJiangsu Key Laboratory of Druggability of Biopharmaceuticals, State Key Laboratory of Natural Medicines, College of Life Science and Technology, China Pharmaceutical University, Nanjing, 210009, PR China. liuwei@cpu.edu.cn.ORCID http://orcid.org/0000-0001-9819-3178
China Pharmaceutical University · CNSimcere Pharmaceutical (China) · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-L-Arabinofuranosidases (Abfs) play a crucial role in the degradation of hemicelluloses, especially arabinoxylans (AX). Most of the available characterized Abfs are from bacteria, while fungi, as natural decomposers, contain Abfs with little attention given. An arabinofuranosidase (ThAbf1), belonging to the glycoside hydrolase 51 (GH51) family, from the genome of the white-rot fungus Trametes hirsuta, was recombinantly expressed, characterized, and functionally determined. The general biochemical properties showed that the optimal conditions for ThAbf1 were pH 6.0 and 50°C. In substrate kinetics assays, ThAbf1 preferred small fragment arabinoxylo-oligosaccharides (AXOS) and could surprisingly hydrolyze di-substituted 2

Indexed as

PolyporaceaeTrametesGlycoside HydrolasesOligosaccharidesSubstrate SpecificityXylansalpha-N-arabinofuranosidaseGlycoside HydrolasesOligosaccharidesXylansArabinoxylanCrystal structureGlycoside hydrolase 51 familySynergistic degradationTrametes hirsutaα-L-Arabinofuranosidases

Identifiers

PMID37178306
OpenAlexW4376505278

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.