Evidence map›Paper›PMID 42249657›Full record

ArticleMolecular microbiology2026

Protein STM3547 From Salmonella typhimurium Is a Phosphofructose Kinase B-Type Enzyme With Ribose Kinase Activity.

Regan D McCormick, Aatif A Jabbar, Jorge C Escalante-Semerena

Abstract read
In one paragraph

Article in Molecular microbiology, 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

Who cites it

0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Regan D McCormickDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-6342-0051
Aatif A JabbarDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.ORCID 0009-0003-6950-5963
Jorge C Escalante-SemerenaDepartment of Microbiology, University of Georgia, Athens, Georgia, USA.ORCID 0000-0001-7428-2811

Funding

Analysis of the Metabolic Capabilities of Prokaryotic CellsR35GM130399 · NIGMS · UNIVERSITY OF GEORGIA · PI JORGE C ESCALANTE · 2019 to 2026
$5.5M
NIGMS NIH HHS R35 GM130399NIGMS NIH HHS R35GM130399
6 · The paper itself

Abstract

The first step in the metabolic utilization of ribose is the phosphorylation of its 5' hydroxyl group. The enteropathogenic bacterium Salmonella enterica subsp. enterica sv. Typhimurium str. LT2 (hereafter S. Typhimurium) has two known enzymes that can phosphorylate D-ribose, namely ribose kinase (RbsK) and deoxyribose kinase (DeoK). Here, we report in vivo and in vitro evidence to support the conclusion that the previously uncharacterized STM3547 protein of this bacterium has ribose kinase activity, and we propose naming it RikA (Ribokinase A). Our bioinformatics analyses show end-to-end sequence identity/similarity among RikA, RbsK, and DeoK, and site-directed mutagenesis of RikA showed that, like in RbsK and DeoK, an aspartate residue (position 343 in RikA) is critical for enzymatic activity. We found that RikA has K

Indexed as

Bacterial ProteinsPhosphotransferases (Alcohol Group Acceptor)Salmonella typhimuriumAdenosine TriphosphateAmino Acid SequenceKineticsMutagenesis, Site-DirectedPhosphorylationRiboseAdenosine TriphosphateBacterial ProteinsPhosphotransferases (Alcohol Group Acceptor)ribokinaseRibosecarbohydrate metabolismPfkB family of sugar kinasesribose kinaseSalmonella enterica

Identifiers

PMID42249657
PMCPMC13432705

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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 OpenQuestion graph.