Evidence map›Paper›PMID 37548665›Full record

ArticleApplied microbiology and biotechnology2023

Structure and enzymatic characterization of CelD endoglucanase from the anaerobic fungus Piromyces finnis.

Alexey Dementiev, Stephen P Lillington, Shiyan Jin, Youngchang Kim, Robert Jedrzejczak, Karolina Michalska, Andrzej Joachimiak, Michelle A O'Malley

Open access · hybridAbstract read
PubMed Full text at PMC 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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
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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

8 authors at 2 institutions in 1 country.

Alexey Dementiev *Structural Biology Center, X-Ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Stephen P Lillington *Department of Chemical Engineering, University of California, Santa Barbara, CA, USA.
Shiyan JinDepartment of Chemical Engineering, University of California, Santa Barbara, CA, USA.
Youngchang KimStructural Biology Center, X-Ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Robert JedrzejczakStructural Biology Center, X-Ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Karolina MichalskaStructural Biology Center, X-Ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Andrzej JoachimiakStructural Biology Center, X-Ray Science Division, Argonne National Laboratory, Lemont, IL, 60439, USA.
Michelle A O'MalleyDepartment of Chemical Engineering, University of California, Santa Barbara, CA, USA. momalley@ucsb.edu.ORCID http://orcid.org/0000-0002-6065-8491
Argonne National Laboratory · USUniversity of California, Santa Barbara · US

Funding

Biological and Environmental Research DE-AC02-05CH11231Biological and Environmental Research DE-SC0010352Biological and Environmental Research DE-SC0020420Biological and Environmental Research DE-SC0022142Institute for Collaborative Biotechnologies W911NF-09-D-0001Institute for Collaborative Biotechnologies W911NF-19-D-0001
6 · The paper itself

Abstract

Anaerobic fungi found in the guts of large herbivores are prolific biomass degraders whose genomes harbor a wealth of carbohydrate-active enzymes (CAZymes), of which only a handful are structurally or biochemically characterized. Here, we report the structure and kinetic rate parameters for a glycoside hydrolase (GH) family 5 subfamily 4 enzyme (CelD) from Piromyces finnis, a modular, cellulosome-incorporated endoglucanase that possesses three GH5 domains followed by two C-terminal fungal dockerin domains (double dockerin). We present the crystal structures of an apo wild-type CelD GH5 catalytic domain and its inactive E154A mutant in complex with cellotriose at 2.5 and 1.8 Å resolution, respectively, finding the CelD GH5 catalytic domain adopts the (β/α)

Indexed as

CellulasePiromycesAnaerobiosisGlucansCellulaseendoglucanase CelDGlucansAnaerobic fungiCrystal structureEnzyme kineticsGH5 endoglucanaseLignocellulose

Identifiers

PMID37548665
PMCPMC10485095
OpenAlexW4385619709

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.