Evidence map›Paper›PMID 41618888›Full record

ArticleBiotechnology and applied biochemistry2026

In Silico Characterization and Molecular Docking of the L-Arginase Gene From Alcaligenes aquatilis BC2.

Birhan Getie Assega, Kefyalew Ayalew Getahun, Tamene Milkessa Jiru, Tsehayneh Geremew Yohannes, Mulugeta Aemero, Feleke Moges, Berhanu Andualem

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Article in Biotechnology and applied biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Birhan Getie AssegaDepartment of Environmental and Industrial Biotechnology, Institute of Biotechnology, University of Gondar, Gondar, Ethiopia.
Kefyalew Ayalew GetahunDepartment of Pharmacology, School of Pharmacy, College of Medicine and Health Sciences, University of Gondar, Gondar, Ethiopia.
Tamene Milkessa JiruDepartment of Environmental and Industrial Biotechnology, Institute of Biotechnology, University of Gondar, Gondar, Ethiopia.
Tsehayneh Geremew YohannesDepartment of Environmental and Industrial Biotechnology, Institute of Biotechnology, University of Gondar, Gondar, Ethiopia.
Mulugeta AemeroDepartment of Medical Parasitology, SBLS, CMHS, University of Gondar, Gondar, Ethiopia.
Feleke MogesDepartment of Medical Microbiology, SBLS, CMHS, University of Gondar, Gondar, Ethiopia.
Berhanu AndualemDepartment of Environmental and Industrial Biotechnology, Institute of Biotechnology, University of Gondar, Gondar, Ethiopia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-arginine is a vital amino acid metabolized by L-arginase, an enzyme with growing biotechnological and therapeutic significance, particularly in cancer treatment. This study presents a comprehensive in silico characterization of the L-arginase gene isolated from Alcaligenes aquatilis BC2, a bacterium originating from Ethiopian soda lakes. The analysis identified a 336-amino-acid enzyme predicted to be stable, soluble, and extracellular. Homology modeling generated a reliable hexameric 3D structure with high stereochemical quality, validated through multiple structural assessment tools. Phylogenetic and conserved domain analyses confirmed the enzyme's evolutionary placement within the Alcaligenes genus and highlighted preserved functional motifs. Molecular docking predicted a strong binding affinity (-7.1 kcal mol

Indexed as

AlcaligenesMolecular Docking SimulationAmino Acid SequencePhylogenybacterial L‐arginasebinding interactionbioinformaticsfunctional analysishomology modeling

Identifiers

PMID41618888
PMCPMC13446426

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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 Socratic graph.