Evidence map›Paper›PMID 33528727›Full record

ArticleMolecular biology reports2021

Mutation of UDP-glucose binding motif residues lead to increased affinity for ADP-glucose in sugarcane sucrose phosphate synthase.

Nuriyah Inda Kurniah, Widhi Dyah Sawitri, Muhammad Saifur Rohman, Yudhi Nugraha, Toshiharu Hase, Bambang Sugiharto

Abstract read
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Article in Molecular biology reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

  1. Review
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

6 authors at 4 institutions in 2 countries.

Nuriyah Inda KurniahLaboratory of Molecular Biology and Biotechnology, Center for Development of Advanced Science and Technology (CDAST), University of Jember, Jl. Kalimantan No 37, Kampus Tegalboto, Jember, 68121, Indonesia.
Widhi Dyah SawitriDepartment of Agronomy, Faculty of Agriculture, Universitas Gadjah Mada, Yogyakarta, 55281, Indonesia.
Muhammad Saifur RohmanDepartment of Agricultural Microbiology, Faculty of Agriculture, Universitas Gadjah Mada, Yogyakarta, 55281, Indonesia.
Yudhi NugrahaFaculty of Medicine, Universitas Pembangunan Nasional "Veteran" Jakarta, Jakarta, 12450, Indonesia.
Toshiharu HaseInstitute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan.
Bambang SugihartoLaboratory of Molecular Biology and Biotechnology, Center for Development of Advanced Science and Technology (CDAST), University of Jember, Jl. Kalimantan No 37, Kampus Tegalboto, Jember, 68121, Indonesia. sugiharto.fmipa@unej.ac.id.ORCID http://orcid.org/0000-0002-8125-1893
Universitas Gadjah Mada · IDUniversitas Jember · IDProtein Research Foundation · JPUniversitas Pembangunan Nasional Veteran Jakarta · ID

Funding

Kementerian Riset, Teknologi dan Pendidikan Tinggi 970/UN25.3.1/LT/2020
6 · The paper itself

Abstract

Plant sucrose-phosphate synthase (SPS) contains a glycosyltransferase domain, which specifically catalyzes reactions with the nucleotide sugar uridine diphosphate glucose (UDP-G) as a donor substrate. Unlike plant SPS, bacterial SPS is predicted to bind other nucleotide sugars, such as adenosine diphosphate glucose (ADP-G). This study aimed to identify the UDP-G binding site of sugarcane (Saccharum officinarum) SPS (SoSPS1) and to improve its affinity for ADP-G by site-directed mutagenesis. To achieve targeted mutagenesis, amino acid distribution and comparative modeling studies were performed, followed by site-directed mutagenesis of SoSPS1 in the putative UDP-G binding motif. The N-terminal deletion of SoSPS1 (∆N-SoSPS1) was used for enzymatic analysis. The results showed that mutations in the R-X

Indexed as

Adenosine Diphosphate GlucoseAmino Acid MotifsAmino Acid SequenceBinding SitesEscherichia coliGene ExpressionGlucosyltransferasesKineticsModels, MolecularMolecular Docking SimulationMutagenesis, Site-DirectedMutationN-Glycosyl HydrolasesRecombinant ProteinsSaccharumSequence Alignmentadenine glycosylaseAdenosine Diphosphate GlucoseGlucosyltransferasesN-Glycosyl HydrolasesRecombinant Proteinssucrose-phosphate synthaseUridine Diphosphate GlucoseAdenine diphosphate glucoseGlycosyltransferaseSite-directed mutagenesisSucrose phosphate synthaseUridine diphosphate glucose

Identifiers

PMID33528727
OpenAlexW3127565444

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.