ArticleThe EMBO journal2001
The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 112 citations in OpenAlex.
- Triokinase/FMN Cyclase: A Bifunctional Enzyme Linking Metabolism, Stress Responses and Disease.Biology · 2026Review
- Synthesis of 4-hydroxybenzoic Acid in Escherichia coli by a Modular co-culture System.Applied biochemistry and biotechnology · 2026Article
- Sugar supplementation enhances biofilm formation and extracellular polysaccharides production inFrontiers in microbiology · 2026Article
- The bacterial phosphotransferase system-mediated rifampicin phosphorylation: ancestral links to rifampicin-inactivating enzyme.Frontiers in microbiology · 2026Article
- Evaluation of Cellular Responses of HeterotrophicMicroorganisms · 2024Article
- Engineering of increased L-Threonine production in bacteria by combinatorial cloning and machine learning.Metabolic engineering communications · 2023Article
- In silico and in vivo analyses reveal key metabolic pathways enabling the fermentative utilization of glycerol in Escherichia coli.Microbial biotechnology · 2022Article
- Listeriolysin S: A bacteriocin fromProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Rational Proteomic Analysis of a New DomesticatedFrontiers in microbiology · 2021Article
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Opening a Novel Biosynthetic Pathway to Dihydroxyacetone and Glycerol inInternational journal of molecular sciences · 2020Article
- Systems Metabolic Engineering of Escherichia coli Improves Coconversion of Lignocellulose-Derived Sugars.Biotechnology journal · 2019Article
- Chemical and Metabolic Controls on Dihydroxyacetone Metabolism Lead to Suboptimal Growth of Escherichia coli.Applied and environmental microbiology · 2019Article
- Closure of the Human TKFC Active Site: Comparison of the Apoenzyme and the Complexes Formed with Either Triokinase or FMN Cyclase Substrates.International journal of molecular sciences · 2019Article
- Arsenic Response of Three AltiplanicFrontiers in microbiology · 2019Article
- Article
- Fermentation of dihydroxyacetone by engineeredProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Trees, fungi and bacteria: tripartite metatranscriptomics of a root microbiome responding to soil contamination.Microbiome · 2018Article
- Biochemical Characterization of the Lysine Acetylation of Tyrosyl-tRNA Synthetase in Escherichia coli.Chembiochem : a European journal of chemical biology · 2017Article
- The phosphocarrier protein HPr of the bacterial phosphotransferase system globally regulates energy metabolism by directly interacting with multiple enzymes inThe Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dihydroxyacetone kinase (DhaK) of Escherichia coli consists of three soluble protein subunits. DhaK (YcgT; 39.5 kDa) and DhaL (YcgS; 22.6 kDa) are similar to the N- and C-terminal halves of the ATP-dependent DhaK ubiquitous in bacteria, animals and plants. The homodimeric DhaM (YcgC; 51.6 kDa) consists of three domains. The N-terminal dimerization domain has the same fold as the IIA domain (PDB code 1PDO) of the mannose transporter of the bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS). The middle domain is similar to HPr and the C-terminus is similar to the N-terminal domain of enzyme I (EI) of the PTS. DhaM is phosphorylated three times by phosphoenolpyruvate in an EI- and HPr-dependent reaction. DhaK and DhaL are not phosphorylated. The IIA domain of DhaM, instead of ATP, is the phosphoryl donor to dihydroxyacetone (Dha). Unlike the carbohydrate-specific transporters of the PTS, DhaK, DhaL and DhaM have no transport activity.
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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.