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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...

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Related Experiment Video

Updated: Jun 7, 2026

PCR Mutagenesis, Cloning, Expression, Fast Protein Purification Protocols and Crystallization of the Wild Type and Mutant Forms of Tryptophan Synthase
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Protein STM3547 From Salmonella typhimurium Is a Phosphofructose Kinase B-Type Enzyme With Ribose Kinase Activity.

Regan D McCormick1, Aatif A Jabbar1, Jorge C Escalante-Semerena1

  • 1Department of Microbiology, University of Georgia, Athens, Georgia, USA.

Molecular Microbiology
|June 6, 2026
PubMed
Summary

Salmonella Typhimurium possesses a new ribokinase, RikA, essential for ribose metabolism. This enzyme, similar to RbsK and DeoK, phosphorylates D-ribose and is crucial for bacterial survival.

Keywords:
Salmonella entericaPfkB family of sugar kinasescarbohydrate metabolismribose kinase

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Metabolic utilization of ribose begins with phosphorylation of its 5' hydroxyl group.
  • Salmonella Typhimurium has two known D-ribose phosphorylating enzymes: ribose kinase (RbsK) and deoxyribose kinase (DeoK).
  • The function of the STM3547 protein in S. Typhimurium was previously uncharacterized.

Purpose of the Study:

  • To identify and characterize the function of the previously uncharacterized STM3547 protein in Salmonella Typhimurium.
  • To determine if STM3547 possesses ribose kinase activity and to propose a name for the protein.
  • To investigate the enzymatic properties and substrate specificity of the newly identified ribokinase.

Main Methods:

  • In vivo and in vitro assays were performed to assess the enzymatic activity of STM3547.
  • Bioinformatics analyses were conducted to compare the sequence of STM3547 with known kinases.
  • Site-directed mutagenesis was used to identify critical residues for enzymatic activity.
  • Kinetic parameters (Km values) for ribose and ATP were determined.
  • Substrate specificity was evaluated using various sugar substrates.

Main Results:

  • The STM3547 protein was confirmed to have ribose kinase activity and was named RikA (Ribokinase A).
  • RikA shares sequence identity with RbsK and DeoK, and an aspartate residue at position 343 is critical for its activity.
  • RikA exhibits comparable Km values to RbsK and DeoK for ribose and ATP, with ribose-induced cooperative ATP binding.
  • RikA primarily phosphorylates D-ribose, with poor activity against 2-deoxy-D-ribose, D-xylose, and D-xylulose, and no activity against L-arabinose.

Conclusions:

  • The RikA protein is a novel ribokinase in Salmonella Typhimurium, playing a significant role in ribose metabolism.
  • RikA belongs to the phosphofructose kinase B-type (PfkB) family of sugar kinases.
  • The findings suggest conserved mechanisms, including ribose-induced conformational changes, among S. Typhimurium ribokinases.