Evidence map›Paper›PMID 38300354›Full record

ArticleExtremophiles : life under extreme conditions2024

Biochemical and in silico structural characterization of a cold-active arginase from the psychrophilic yeast, Glaciozyma antarctica PI12.

Nik Yusnoraini Yusof, Doris Huai Xia Quay, Shazilah Kamaruddin, Mohd Anuar Jonet, Rosli Md Illias, Nor Muhammad Mahadi, Mohd Firdaus-Raih, Farah Diba Abu Bakar, Abdul Munir Abdul Murad

Abstract read
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In one paragraph

Article in Extremophiles : life under extreme conditions, 2024. 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
0.4field-weighted citation impact, top 48% 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, 3 citations in OpenAlex.

  1. Crystal structure of a cold-active arginase from Glaciozyma antarctica.Acta crystallographica. Section F, Structural biology communications · 2026
    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

9 authors at 4 institutions in 1 country.

Nik Yusnoraini YusofInstitute for Research in Molecular Medicine (INFORMM), Health Campus, Universiti Sains Malaysia, Kubang Kerian, 16150, Kelantan, Malaysia. nikyus@usm.my.
Doris Huai Xia QuayDepartment of Applied Physics, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, UKM, 43600, Bangi, Selangor, Malaysia. dorisquay@ukm.edu.my.
Shazilah KamaruddinDepartment of Biological Sciences & Biotechnology, Faculty of Sciences and Technology, Universiti Kebangsaan Malaysia, 43600, Bangi, Selangor, Malaysia.
Mohd Anuar JonetMalaysia Genome and Vaccine Institute, Jalan Bangi Lama, 43000, Kajang, Selangor, Malaysia.
Rosli Md IlliasDepartment of Bioprocess Engineering, Faculty of Chemical Engineering, Universiti Teknologi Malaysia, 81300, Skudai, Johor, Malaysia.
Nor Muhammad MahadiInstitute of Systems Biology, Universiti Kebangsaan Malaysia, 43600, Bangi, Selangor, Malaysia.
Mohd Firdaus-RaihDepartment of Applied Physics, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, UKM, 43600, Bangi, Selangor, Malaysia.
Farah Diba Abu BakarDepartment of Biological Sciences & Biotechnology, Faculty of Sciences and Technology, Universiti Kebangsaan Malaysia, 43600, Bangi, Selangor, Malaysia.
Abdul Munir Abdul MuradDepartment of Biological Sciences & Biotechnology, Faculty of Sciences and Technology, Universiti Kebangsaan Malaysia, 43600, Bangi, Selangor, Malaysia.
National University of Malaysia · MYMalaysia Genome Institute · MYUniversiti Sains Malaysia · MYUniversity of Technology Malaysia · MY

Funding

Ministry of Science, Technology and Innovation of Malaysia (MOSTI) 02-05-20-SF007/2
6 · The paper itself

Abstract

Glaciozyma antarctica PI12 is a psychrophilic yeast isolated from Antarctica. In this work, we describe the heterologous production, biochemical properties and in silico structure analysis of an arginase from this yeast (GaArg). GaArg is a metalloenzyme that catalyses the hydrolysis of L-arginine to L-ornithine and urea. The cDNA of GaArg was reversed transcribed, cloned, expressed and purified as a recombinant protein in Escherichia coli. The purified protein was active against L-arginine as its substrate in a reaction at 20 °C, pH 9. At 10-35 °C and pH 7-9, the catalytic activity of the protein was still present around 50%. Mn

Indexed as

BasidiomycotaSaccharomyces cerevisiaeArginaseArginineEscherichia coliArginaseArginineCold-active enzymeEnzyme assayL-ArginineProtein structure modelingRecombinant enzymeSubstructure flexibility

Identifiers

PMID38300354
OpenAlexW4391449506

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.