Evidence map›Paper›PMID 34726178›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Crystal structure of acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis.

Kohei Sasamoto, Tomoki Himiyama, Kunihiko Moriyoshi, Takashi Ohmoto, Koichi Uegaki, Yoshiaki Nishiya, Tsutomu Nakamura

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 47% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. mBio · 2025
    Article
  2. 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

7 authors at 4 institutions in 1 country.

Kohei SasamotoDivision of Life Science, Graduate School of Science and Engineering, Setsunan University, 17-8 Ikeda-Nakamachi, Neyagawa, Osaka 572-8508, Japan.ORCID 0000-0001-6005-7939
Tomoki HimiyamaBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan.ORCID 0000-0001-5252-1834
Kunihiko MoriyoshiOsaka Research Institute of Industrial Science and Technology, 1-6-50 Morinomiya, Joto-ku, Osaka 536-8553, Japan.
Takashi OhmotoOsaka Research Institute of Industrial Science and Technology, 1-6-50 Morinomiya, Joto-ku, Osaka 536-8553, Japan.
Koichi UegakiDepartment of Applied Biological Chemistry, Faculty of Agriculture, Kindai University, 3327-204 Nakamachi, Nara 631-8505, Japan.ORCID 0000-0001-6659-2596
Yoshiaki NishiyaDivision of Life Science, Graduate School of Science and Engineering, Setsunan University, 17-8 Ikeda-Nakamachi, Neyagawa, Osaka 572-8508, Japan.
Tsutomu NakamuraBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577, Japan.ORCID 0000-0002-5511-8087
National Institute of Advanced Industrial Science and Technology · JPOsaka Research Institute of Industrial Science and Technology · JPSetsunan University · JPKindai University · JP

Funding

Japan Society for the Promotion of Science 18K06616Japan Society for the Promotion of Science 20K05740Japan Society for the Promotion of Science 20K15403
6 · The paper itself

Abstract

The acetylxylan esterases (AXEs) classified into carbohydrate esterase family 4 (CE4) are metalloenzymes that catalyze the deacetylation of acetylated carbohydrates. AXE from Caldanaerobacter subterraneus subsp. tengcongensis (TTE0866), which belongs to CE4, is composed of three parts: a signal sequence (residues 1-22), an N-terminal region (NTR; residues 23-135) and a catalytic domain (residues 136-324). TTE0866 catalyzes the deacetylation of highly substituted cellulose acetate and is expected to be useful for industrial applications in the reuse of resources. In this study, the crystal structure of TTE0866 (residues 23-324) was successfully determined. The crystal diffracted to 1.9 Å resolution and belonged to space group I2

Indexed as

AcetylesteraseBacillotaCrystallography, X-RaySubstrate SpecificityAcetylesteraseacetylxylan esteraseacetylxylan esteraseCaldanaerobacter subterraneus subsp. tengcongensiscarbohydrate esterase family 4cellulose acetatecrystal structurethermophilic enzymes

Identifiers

PMID34726178
PMCPMC8561816
OpenAlexW3207274159

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.