Evidence map›Paper›PMID 29904894›Full record

ArticleWorld journal of microbiology & biotechnology2018

Introduction of novel thermostable α-amylases from genus Anoxybacillus and proposing to group the Bacillaceae related α-amylases under five individual GH13 subfamilies.

Arzu Coleri Cihan, Emine Derebay Yildiz, Ergin Sahin, Ozal Mutlu

Abstract read
PubMed Publisher
In one paragraph

Article in World journal of microbiology & biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Optimizing the Fermentation Conditions ofEvidence-based complementary and alternative medicine : eCAM · 2023
    Article
  4. Article
  5. 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

4 authors at 2 institutions in 1 country.

Arzu Coleri CihanFaculty of Science, Department of Biology, Ankara University, Tandogan, 06100, Ankara, Turkey. arzucoleri@gmail.com.ORCID http://orcid.org/0000-0002-7289-6251
Emine Derebay YildizInstitute of Biotechnology, Ankara University, Besevler, 06100, Ankara, Turkey.
Ergin SahinFaculty of Science, Department of Biology, Ankara University, Tandogan, 06100, Ankara, Turkey.
Ozal MutluFaculty of Arts and Sciences, Department of Biology, Marmara University, Goztepe, 34722, Istanbul, Turkey.
Ankara University · TRMarmara University · TR

Funding

TUBITAK 115R001
6 · The paper itself

Abstract

Among the thermophilic Bacillaceae family members, α-amylase production of 15 bacilli from genus Anoxybacillus was investigated, some of which are biotechnologically important. These Anoxybacillus α-amylase genes displayed ≥ 91.0% sequence similarities to Anoxybacillus enzymes (ASKA, ADTA and GSX-BL), but relatively lower similarities to Geobacillus (≤ 69.4% to GTA, Gt-amyII), and Bacillus aquimaris (≤ 61.3% to BaqA) amylases, all formerly proposed only in a Glycoside Hydrolase 13 (GH13) subfamily. The phylogenetic analyses of 63 bacilli-originated protein sequences among 93 α-amylases revealed the overall relationships within Bacillaceae amylolytic enzymes. All bacilli α-amylases formed 5 clades different from 15 predefined GH13 subfamilies. Their phylogenetic findings, taxonomic relationships, temperature requirements, and comparisonal structural analyses (including their CSR-I-VII regions, 12 sugar- and 4 calcium-binding sites, presence or absence of the complete catalytic machinery, and their currently unassigned status in a valid GH13 subfamiliy) revealed that these five GH13 α-amylase clades related to familly share some common characteristics, but also display differentiative features from each other and the preclassified ones. Based on these findings, we proposed to divide Bacillaceae related GH13 subfamilies into 5 individual groups: the novel a2 subfamily clustered around α-amylase B2M1-A (Anoxybacillus sp.), the a1, a3 and a4 subfamilies (including the representatives E184aa-A (Anoxybacillus sp.), ATA (Anoxybacillus tepidamans), and BaqA,) all of which were composed from the division of the previously grouped single subfamily around α-amylase BaqA, and the undefinite subfamily formerly defined as xy including Bacillus megaterium NL3.

Indexed as

alpha-AmylasesAmino Acid SequenceAnoxybacillusBacillaceaeBacillusBacterial ProteinsBase SequenceBinding SitesEnzyme AssaysEnzyme StabilityEvolution, MolecularGeobacillusGlycoside HydrolasesModels, MolecularPhylogenyProtein Conformationalpha-AmylasesBacterial ProteinsGlycoside HydrolasesAnoxybacillusBacillaceaeiGlycoside hydrolasesNovel GH13 subfamiliesα-Amylases

Identifiers

PMID29904894
OpenAlexW2808627998

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.