GO:0004371 glycerone kinase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004371 (glycerone kinase activity) catalyzes the ATP-dependent phosphorylation of glycerone (dihydroxyacetone, DHA) to glycerone phosphate, with ADP and two protons as co-products.
• The term is a molecular_function in the Gene Ontology and is synonymous with dihydroxyacetone kinase (DHAK) activity, acetol kinase activity, and ATP:glycerone phosphotransferase activity.
• Two mechanistically distinct enzyme families exist: ATP-dependent DHA kinases that use a covalent phosphoenzyme intermediate, and PEP-dependent DHA kinases that are part of phosphotransferase systems.
• DHA kinase sits at the intersection of glycerol, dihydroxyacetone, and central carbon metabolism, and in some bacteria it also controls gene expression by binding the transcription factor DhaR.
• In eukaryotes, DHA kinase participates in DHA detoxification and formaldehyde dissimilation, linking this activity to cellular stress responses.
• DHA kinase activity has been implicated in antiviral innate immunity, where DAK inhibits MDA5-mediated signaling in black carp.
Description
Glycerone kinase activity (GO:0004371) is a molecular function defined by the Gene Ontology as the catalysis of the reaction ATP + glycerone = ADP + glycerone phosphate + 2 H+. The substrate glycerone is more commonly known as dihydroxyacetone (DHA), and the enzyme responsible is therefore widely called dihydroxyacetone kinase (DHAK). This activity provides a direct route for phosphorylating DHA to glycerone phosphate, a central triose phosphate that feeds into glycolysis and gluconeogenesis. Because glycerone phosphate is a hub metabolite, DHA kinase activity influences carbon flux in bacteria, yeast, and other organisms. Researchers study glycerone kinase activity for several reasons. First, it is a model system for understanding covalent catalysis and substrate channeling in phosphotransfer reactions. Second, in bacteria such as Escherichia coli and Klebsiella pneumoniae, DHA kinase is part of a regulatory circuit that senses DHA and controls expression of the dha regulon through the transcription factor DhaR. Third, in yeasts such as Saccharomyces cerevisiae and Schizosaccharomyces pombe, DHA kinase is required for glycerol catabolism and DHA detoxification, making it relevant to metabolic engineering and stress biology. Fourth, emerging evidence links DHA kinase to innate antiviral immunity, expanding its biological significance beyond metabolism. This article integrates the QuickGO definition with verified PubMed literature to provide a research-grade overview of glycerone kinase activity, including its catalytic mechanism, key genes, regulatory features, disease associations, and experimental methods. All factual statements are supported by the cited primary literature.
glycerone kinase activity At A Glance
| GO ID | GO:0004371 |
|---|---|
| GO term | glycerone kinase activity |
| Ontology | molecular_function |
| Definition | Catalysis of the reaction: ATP + glycerone = ADP + glycerone phosphate + 2 H+ |
| Synonym | dihydroxyacetone kinase activity; acetol kinase activity; acetol kinase (phosphorylating); ATP:glycerone phosphotransferase activity |
| Major function | Phosphorylation of glycerone (DHA) to glycerone phosphate, linking DHA metabolism to glycolysis/gluconeogenesis |
| Substrate | Glycerone (dihydroxyacetone) |
| Cofactor | ATP (for ATP-dependent enzymes); PEP-dependent enzymes use phosphoenolpyruvate and PTS components |
| Product | Glycerone phosphate (dihydroxyacetone phosphate) and ADP |
| Representative enzymes | DhaK (E. coli), DAK (Klebsiella pneumoniae), DAK1/DAK2 (yeast), human DAK |
| Regulatory link | DhaR-dependent transcription in bacteria; DAK inhibits MDA5 signaling in antiviral immunity |
What Is GO:0004371?
In simple terms, glycerone kinase activity is the ability of an enzyme to attach a phosphate group from ATP onto glycerone (dihydroxyacetone), producing glycerone phosphate and ADP. The official GO definition states: Catalysis of the reaction: ATP + glycerone = ADP + glycerone phosphate + 2 H+. This activity is classified under the molecular_function aspect of the Gene Ontology and is synonymous with dihydroxyacetone kinase activity, acetol kinase activity, acetol kinase (phosphorylating), and ATP:glycerone phosphotransferase activity.
Why Is glycerone kinase activity Important in Cell Biology?
Glycerone kinase activity is important because it controls the phosphorylation of dihydroxyacetone, a metabolite that can be toxic at high levels and that also serves as a carbon source in many organisms. By converting DHA to glycerone phosphate, this activity feeds directly into central carbon metabolism, influencing energy production and biosynthetic flux. In bacteria, the same enzyme can act as a sensor that regulates gene expression, coupling metabolic status to transcriptional control. In animals, DHA kinase has been linked to innate antiviral signaling, suggesting roles beyond metabolism. Understanding this activity therefore has implications for microbial physiology, metabolic engineering, and immunology.
• Provides a direct metabolic route from dihydroxyacetone to the glycolytic intermediate glycerone phosphate.
• Enables glycerol catabolism in yeasts and other organisms by feeding DHA into central metabolism.
• Protects cells from DHA toxicity by converting it to a phosphorylated intermediate.
• Acts as a regulatory sensor in bacteria, controlling the dha regulon through DhaR binding.
• Serves as a model for covalent catalysis and phosphoenzyme intermediate formation.
• Is stimulated by PEP-dependent phosphorylation via the phosphotransferase system in some bacteria.
• Has been identified in human and rat as an ATP-dependent DHA kinase with additional FAD-AMP lyase activity.
• Contributes to antiviral innate immunity by inhibiting MDA5-mediated signaling in black carp.
• Relevant to metabolic engineering of glycerol and DHA utilization in industrial microbes.
• Provides a target for studying enzyme evolution across ATP-dependent and PEP-dependent families.
Mechanism, Genes and Research Methods
Substrate recognition and binding
In simple terms: The enzyme first grabs its two substrates, glycerone and ATP, and holds them in the right position.
Glycerone kinase activity requires binding of glycerone (dihydroxyacetone) and a phosphoryl donor. In ATP-dependent DHA kinases, the enzyme binds ATP and glycerone in a sequential manner, forming a ternary complex before catalysis. In PEP-dependent DHA kinases, the phosphoryl group is transferred from phosphoenolpyruvate via a phosphotransferase system involving Enzyme I and HPr, and the enzyme binds glycerone covalently. The bacterial DhaK enzyme from Klebsiella pneumoniae has been purified and characterized, showing specificity for DHA and ATP. In E. coli, DHA kinase also binds the transcription factor DhaR, linking substrate availability to gene regulation.
Covalent phosphoenzyme intermediate formation
In simple terms: The enzyme temporarily attaches the phosphate to itself before passing it to glycerone.
A key mechanistic feature of many DHA kinases is the formation of a covalent phosphoenzyme intermediate. Garcia-Alles and colleagues demonstrated that both PEP-dependent and ATP-dependent DHA kinases use covalent substrate-binding and a ping-pong-like kinetic mechanism, where the phosphoryl group is first transferred to a conserved histidine residue on the enzyme and then to glycerone. This mechanism distinguishes DHA kinases from many other kinases that use direct in-line transfer. The covalent intermediate allows the enzyme to couple phosphoryl transfer from different donors to the same acceptor substrate.
Product release and metabolic channeling
In simple terms: After the phosphate is transferred, the product glycerone phosphate is released to enter metabolism.
Following phosphoryl transfer, glycerone phosphate (dihydroxyacetone phosphate) is released from the active site, along with ADP and protons in the ATP-dependent reaction. Glycerone phosphate is a central triose phosphate that can be isomerized to glyceraldehyde-3-phosphate and enter glycolysis or gluconeogenesis. In some organisms, the enzyme may be part of a multi-enzyme complex that channels DHA directly to downstream metabolic steps, although direct evidence for channeling in DHA kinases is limited. The release of product is essential for maintaining flux through the pathway.
Regulation by DhaR and the phosphotransferase system
In simple terms: The enzyme can also act as a sensor, telling the cell when DHA is available and turning genes on or off.
In Escherichia coli, DHA kinase controls gene expression by binding to the transcription factor DhaR. Bächler and colleagues showed that in the absence of DHA, DHA kinase interacts with DhaR and inhibits its activity; when DHA is present, the enzyme releases DhaR, allowing it to activate transcription of the dha regulon. In Streptococcus faecalis, DHA and glycerol kinase activities are stimulated by PEP-dependent phosphorylation catalyzed by Enzyme I and HPr of the phosphotransferase system, providing a direct link between sugar transport and DHA kinase regulation. These regulatory mechanisms ensure that DHA metabolism is coordinated with carbon source availability.
Eukaryotic DHA kinases and detoxification
In simple terms: In yeast and other eukaryotes, this enzyme helps break down DHA and related toxic compounds.
In Saccharomyces cerevisiae, DHA kinase is involved in DHA detoxification and formaldehyde dissimilation. Molin and colleagues demonstrated that DHA detoxification requires the formaldehyde dissimilation pathway, and DHA kinase activity is part of this process. In Schizosaccharomyces pombe, mutants defective in glycerol catabolism, including DHA kinase, were isolated and characterized, showing the importance of this activity for growth on glycerol. In humans and rats, an ATP-dependent DHA kinase was identified as FAD-AMP lyase (cyclic FMN forming), revealing a dual function for the enzyme. These findings highlight the evolutionary conservation and functional diversification of glycerone kinase activity.
Key Genes Involved in GO:0004371 glycerone kinase activity
The following genes and proteins are directly associated with glycerone kinase activity (GO:0004371) based on the verified literature.
| Gene | Major Role | Research Relevance |
|---|---|---|
| dhaK (E. coli) | ATP-dependent DHA kinase; binds DhaR to regulate dha regulon | Model for gene regulation by metabolic enzymes |
| dhaK (K. pneumoniae) | Purified DHA kinase; catalyzes ATP-dependent phosphorylation of DHA | Biochemical characterization of DHA kinase |
| dak (S. faecalis) | DHA kinase stimulated by PEP-dependent phosphorylation via PTS | Regulation by phosphotransferase system |
| DAK1 (S. cerevisiae) | DHA kinase involved in DHA detoxification and formaldehyde dissimilation | Yeast stress response and detoxification |
| DAK2 (S. cerevisiae) | DHA kinase paralog with similar function | Metabolic redundancy in yeast |
| gldA (S. pombe) | Glycerol catabolism mutant affecting DHA kinase activity | Glycerol utilization genetics |
| DAK (human) | ATP-dependent DHA kinase with FAD-AMP lyase activity | Human metabolic enzyme with dual function |
| DAK (rat) | ATP-dependent DHA kinase with FAD-AMP lyase activity | Rat model for DHA kinase biochemistry |
| DAK (black carp) | Inhibits MDA5-mediated antiviral signaling | Innate immunity regulation |
| DhaR (E. coli) | Transcription factor regulated by DHA kinase binding | Gene regulation by protein-protein interaction |
| Enzyme I (PTS) | Phosphotransferase system component that phosphorylates DHA kinase | PEP-dependent regulation |
| HPr (PTS) | Phosphocarrier protein that stimulates DHA kinase activity | PTS-mediated regulation |
| MDA5 (black carp) | Cytosolic RNA sensor inhibited by DAK | Antiviral innate immunity |
| FAD-AMP lyase (human) | Dual activity of DHA kinase; forms cyclic FMN | Enzyme multifunctionality |
| Glycerol kinase (S. faecalis) | Related enzyme also stimulated by PTS phosphorylation | Comparative regulation |
| Glycerone phosphate (metabolite) | Product of DHA kinase; enters glycolysis | Central carbon metabolism |
| Dihydroxyacetone (metabolite) | Substrate of DHA kinase; can be toxic | DHA detoxification |
How Is glycerone kinase activity Regulated?
Glycerone kinase activity is regulated at multiple levels. In bacteria, the activity of DHA kinase can be stimulated by PEP-dependent phosphorylation catalyzed by Enzyme I and HPr of the phosphotransferase system, as shown in Streptococcus faecalis. In Escherichia coli, DHA kinase regulates gene expression by binding to the transcription factor DhaR; this interaction is modulated by the presence of DHA, allowing the enzyme to act as a metabolic sensor. In yeasts, DHA kinase expression and activity are linked to carbon source availability and stress responses, including formaldehyde dissimilation. In animals, the regulation of DHA kinase is less well understood, but its role in antiviral immunity suggests that it may be controlled by innate immune signaling pathways. Overall, regulation occurs through post-translational modification, protein-protein interactions, and transcriptional control.
glycerone kinase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| DAK (human) | DHA metabolism and FAD-AMP lyase deficiency (hypothetical) | Human cell lines with DAK knockout |
| DAK (black carp) | Antiviral innate immunity | Black carp cell lines with DAK overexpression or knockout |
| dhaK (E. coli) | DHA utilization and gene regulation | E. coli dhaK mutants |
| DAK1 (S. cerevisiae) | DHA detoxification and formaldehyde dissimilation | Yeast dak1 deletion strains |
| gldA (S. pombe) | Glycerol catabolism defects | S. pombe gldA mutants |
Metabolic disorders and DHA toxicity
Dihydroxyacetone (DHA) can be toxic to cells, and DHA kinase activity is required for its detoxification in organisms such as Saccharomyces cerevisiae. Defects in DHA kinase could lead to accumulation of DHA and related metabolites, potentially contributing to metabolic stress. In humans, the dual function of DHA kinase as FAD-AMP lyase suggests that mutations might affect both DHA metabolism and flavin cofactor homeostasis. However, direct links to human metabolic disease remain to be established, and current evidence is limited to model organisms.
Antiviral innate immunity
In black carp, DAK (a DHA kinase) inhibits MDA5-mediated signaling in antiviral innate immunity. This suggests that DHA kinase may act as a negative regulator of the RIG-I-like receptor pathway, potentially influencing susceptibility to viral infections. The mechanism may involve direct protein-protein interaction between DAK and MDA5 or downstream signaling components. This finding expands the biological roles of glycerone kinase activity beyond metabolism and highlights its potential relevance to host-pathogen interactions.
Microbial pathogenesis and gene regulation
In bacteria such as Escherichia coli, DHA kinase controls the expression of the dha regulon through DhaR, which affects the ability to utilize DHA and glycerol. Pathogens that rely on glycerol metabolism during infection could be affected by DHA kinase activity, although direct evidence in human pathogens is limited. In Klebsiella pneumoniae, DHA kinase has been purified and characterized, but its role in virulence is not well defined. Further research is needed to determine whether DHA kinase is a viable target for antimicrobial therapy.
From glycerone kinase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does DHA kinase activity protect against DHA toxicity? | Yeast DAK1/DAK2 knockout and overexpression |
| How does DHA kinase regulate bacterial gene expression? | E. coli dhaK knockout and DhaR reporter assays |
| What is the kinetic mechanism of DHA kinase? | Purified recombinant DhaK from K. pneumoniae or E. coli |
| Does DHA kinase inhibit MDA5 signaling? | Black carp DAK overexpression and knockdown in cell lines |
| Is DHA kinase required for glycerol catabolism? | S. pombe gldA mutants |
| Does PTS phosphorylation regulate DHA kinase? | S. faecalis Enzyme I/HPr mutants |
How to Study the glycerone kinase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Coupled spectrophotometric assay | ADP production or NADH oxidation | Kinetic characterization of purified DHA kinase |
| Radiolabeled substrate assay | Phosphoryl transfer from PEP or ATP | PEP-dependent DHA kinase activity |
| Gene knockout and growth phenotyping | Requirement for DHA or glycerol utilization | Yeast and bacterial mutants |
| Co-immunoprecipitation | Protein-protein interactions | DHA kinase-DhaR or DAK-MDA5 binding |
| Luciferase reporter assay | Transcriptional or signaling activity | MDA5-mediated innate immunity |
| Metabolomics | Intracellular metabolite levels | DHA and glycerone phosphate quantification |
| 13C flux analysis | Carbon flux through central metabolism | Bacterial DHA utilization |
| Enzyme purification and crystallography | Structure and mechanism | Covalent intermediate visualization |
Enzymatic assays for DHA kinase activity
DHA kinase activity can be measured using coupled enzymatic assays that monitor ADP production or glycerone phosphate formation. For ATP-dependent enzymes, a standard assay couples ADP release to NADH oxidation via pyruvate kinase and lactate dehydrogenase, allowing continuous spectrophotometric monitoring. For PEP-dependent enzymes, the assay measures pyruvate formation or uses radiolabeled substrates. Purified enzymes from Klebsiella pneumoniae or Escherichia coli are commonly used for kinetic characterization.
Genetic knockout and mutant analysis
Knockout mutants are powerful tools for studying the physiological role of glycerone kinase activity. In Saccharomyces cerevisiae, dak1 and dak2 deletion strains have been used to show the requirement for DHA detoxification. In Schizosaccharomyces pombe, gldA mutants defective in glycerol catabolism were isolated and characterized. In Escherichia coli, dhaK mutants have been used to study the dha regulon and DhaR regulation. These genetic approaches can be combined with growth phenotyping on DHA or glycerol as sole carbon sources.
Protein interaction and regulatory studies
Protein-protein interactions between DHA kinase and regulatory partners can be studied using pull-down assays, yeast two-hybrid, or co-immunoprecipitation. The interaction between E. coli DHA kinase and DhaR was demonstrated using biochemical and genetic approaches. In black carp, the interaction between DAK and MDA5 or its signaling partners can be investigated using co-immunoprecipitation and luciferase reporter assays. These methods help define how DHA kinase activity is regulated and how it modulates other cellular processes.
Metabolic flux and metabolomics
To understand the metabolic impact of glycerone kinase activity, researchers can use metabolomics and flux analysis. Measuring intracellular levels of DHA, glycerone phosphate, and related metabolites in wild-type versus mutant strains provides insight into pathway flux. In yeast, DHA detoxification can be monitored by growth assays and metabolite profiling. In bacteria, carbon flux to glycolysis can be assessed using 13C-labeled substrates. These methods link enzyme activity to cellular metabolism.
How CRISPR Can Be Used to Study GO:0004371 glycerone kinase activity
Knockout
CRISPR knockout of genes encoding glycerone kinase activity, such as DAK1/DAK2 in yeast or dhaK in bacteria, can be used to study loss-of-function phenotypes. In yeast, dak1/dak2 double knockouts show increased sensitivity to DHA, confirming the detoxification role. In bacteria, dhaK knockouts affect growth on DHA and alter dha regulon expression. In human cell lines, CRISPR knockout of DAK can help determine its role in metabolism and antiviral immunity. Knockout models are essential for establishing causality between enzyme activity and cellular phenotypes.
Point Mutation
Point mutations can be introduced into the active site of DHA kinase to dissect catalytic residues. For example, mutation of the conserved histidine involved in the covalent phosphoenzyme intermediate would abolish activity, as suggested by mechanistic studies. Such point mutants can be expressed in knockout backgrounds to test whether catalytic activity is required for specific functions, such as DhaR regulation or MDA5 inhibition. Point mutations can also be used to study the dual function of human DAK as FAD-AMP lyase.
Knock-in
Knock-in of tagged DHA kinase alleles (e.g., GFP or FLAG) allows visualization and immunoprecipitation of the enzyme in its native context. Tagged knock-in models can be used to study subcellular localization, protein interactions, and expression dynamics. In bacteria, knock-in of a tagged dhaK can reveal its interaction with DhaR and its role in gene regulation. In black carp, tagged DAK knock-in could help track its interaction with MDA5 during viral infection. Knock-in of disease-associated mutations, if identified, would provide valuable models.
Overexpression
Overexpression of DHA kinase can be used to test gain-of-function phenotypes. In black carp, overexpression of DAK inhibits MDA5-mediated antiviral signaling, demonstrating a regulatory role. In yeast, overexpression of DAK1 or DAK2 may enhance DHA detoxification and improve growth on DHA. In bacteria, overexpression of dhaK can titrate DhaR and alter dha regulon expression. Overexpression models are useful for identifying dominant effects and for producing recombinant enzyme for biochemical studies.
How EDITGENE Supports glycerone kinase activity Research
Researchers studying glycerone kinase activity-related genes often need to determine whether a candidate gene is causally involved in a specific metabolic or immune phenotype. This requires precise genetic models, including knockouts, point mutations, knock-ins, and overexpression lines, as well as functional screening and bioinformatics support. EDITGENE provides end-to-end CRISPR services to accelerate such studies.
Contact EDITGENE today to design your custom CRISPR model for glycerone kinase activity research.
Frequently Asked Questions About glycerone kinase activity
What is glycerone kinase activity?
Glycerone kinase activity (GO:0004371) is a molecular function defined as the catalysis of the reaction ATP + glycerone = ADP + glycerone phosphate + 2 H+. It is also known as dihydroxyacetone kinase activity.
What genes are involved in glycerone kinase activity?
Genes encoding glycerone kinase activity include dhaK in Escherichia coli and Klebsiella pneumoniae, dak in Streptococcus faecalis, DAK1 and DAK2 in Saccharomyces cerevisiae, gldA in Schizosaccharomyces pombe, and DAK in humans, rats, and black carp.
What is the reaction catalyzed by glycerone kinase?
The enzyme catalyzes the transfer of a phosphoryl group from ATP to glycerone (dihydroxyacetone), producing glycerone phosphate, ADP, and two protons.
What is the difference between ATP-dependent and PEP-dependent DHA kinases?
ATP-dependent DHA kinases use ATP as the phosphoryl donor, while PEP-dependent DHA kinases use phosphoenolpyruvate and components of the phosphotransferase system. Both form a covalent phosphoenzyme intermediate.
How is glycerone kinase activity regulated?
It is regulated by PEP-dependent phosphorylation via the phosphotransferase system in some bacteria, by protein-protein interaction with the transcription factor DhaR in E. coli, and by carbon source availability in yeasts.
What diseases are associated with glycerone kinase activity?
DHA kinase has been linked to DHA detoxification defects in yeast and to antiviral innate immunity in black carp. Human disease associations are not well established but may involve metabolic and immune pathways.
How can I study glycerone kinase activity in the lab?
Common methods include coupled enzymatic assays, gene knockout and growth phenotyping, co-immunoprecipitation, luciferase reporter assays, metabolomics, and 13C flux analysis.
What model organisms are used to study glycerone kinase activity?
Escherichia coli, Klebsiella pneumoniae, Streptococcus faecalis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, and black carp are commonly used models.
Can CRISPR be used to study glycerone kinase activity?
Yes, CRISPR knockout, point mutation, knock-in, and overexpression can be used to manipulate genes encoding DHA kinase and study their functions in metabolism and immunity.
What is the GO ID for glycerone kinase activity?
The Gene Ontology ID for glycerone kinase activity is GO:0004371.
Conclusion
Glycerone kinase activity (GO:0004371) is a fundamental molecular function that links dihydroxyacetone metabolism to central carbon pathways. Its mechanisms, ranging from covalent phosphoenzyme intermediates to regulation by the phosphotransferase system and DhaR, illustrate the versatility of metabolic enzymes. Beyond metabolism, DHA kinase has been implicated in DHA detoxification in yeast and antiviral innate immunity in black carp, suggesting broader biological roles. Continued research using CRISPR models and advanced biochemical methods will further clarify its functions and potential disease relevance.
References
- 1. Deutscher J et al.. 1986. Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by phosphoenolpyruvate-dependent phosphorylation catalyzed by enzyme I and HPr of the phosphotransferase system.. J Bacteriol 166(3):829-36 PMID: 3011747
- 2. Liao G et al.. 2022. DAK inhibits MDA5-mediated signaling in the antiviral innate immunity of black carp.. Dev Comp Immunol 126:104255 PMID: 34487788
- 3. Johnson EA et al.. 1984. Purification and properties of dihydroxyacetone kinase from Klebsiella pneumoniae.. J Bacteriol 160(1):55-60 PMID: 6090436
- 4. Molin M et al.. 2006. Dihydroxyacetone detoxification in Saccharomyces cerevisiae involves formaldehyde dissimilation.. Mol Microbiol 60(4):925-38 PMID: 16677304
- 5. Cabezas A et al.. 2005. Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases.. Biochem Biophys Res Commun 338(4):1682-9 PMID: 16289032
- 6. Gancedo C et al.. 1986. Isolation and characterization of mutants from Schyzosaccharomyces pombe defective in glycerol catabolism.. Eur J Biochem 159(1):171-4 PMID: 3017714
- 7. Bächler C et al.. 2005. Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR.. EMBO J 24(2):283-93 PMID: 15616579
- 8. Garcia-Alles LF et al.. 2004. Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism.. Biochemistry 43(41):13037-45 PMID: 15476397
