GO:0004550 nucleoside diphosphate kinase activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0004550 (nucleoside diphosphate kinase activity) catalyzes the reversible transfer of a terminal phosphate from ATP to a nucleoside diphosphate, producing ADP and a nucleoside triphosphate.
• Nucleoside diphosphate kinases (NDKs/NMEs) are conserved across bacteria, plants, fungi, and humans and participate in nucleotide homeostasis, virulence, development, and metastasis suppression.
• Bacterial Ndk is a pleiotropic effector that modulates virulence and adaptive responses, and in uropathogenic Escherichia coli it inhibits caspase-1-dependent pyroptosis to facilitate urinary tract infection.
• In Escherichia coli, nucleoside diphosphate kinase activity escalates A-to-C mutations in MutT-deficient strains, linking nucleotide pool balance to mutagenesis.
• Human NME4 (mitochondrially localized nucleoside diphosphate kinase D) functions as a novel metastasis suppressor, connecting GO:0004550 to cancer biology.
• CRISPR knockout, point-mutation, knock-in, and overexpression models enable causal dissection of NDK/NME gene function in infection, cancer, and plant/fungal systems.
Description
Nucleoside diphosphate kinase activity (GO:0004550) is a molecular function defined as catalysis of the reaction ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. This activity maintains the balance of cellular nucleoside triphosphates and is carried out by nucleoside diphosphate kinases (NDKs), also known as NME proteins in humans. Because the reaction is reversible and accepts multiple nucleoside diphosphate substrates, NDK activity sits at the intersection of nucleotide metabolism, signal transduction, and stress responses. Researchers study GO:0004550 to understand how cells supply NTPs for DNA replication, RNA synthesis, and protein synthesis, and how dysregulation of this activity contributes to infection, mutagenesis, and cancer. The enzyme is conserved from bacteria to plants, fungi, and humans, making it a tractable target across model systems. In bacteria, Ndk is a pleiotropic effector manipulating virulence and adaptive responses, while in plants and fungi putative NDK functions include housekeeping and moonlighting roles. In humans, the NME family includes mitochondrially localized NME4, which has been characterized as a novel metastasis suppressor. Together, these findings establish GO:0004550 as a central activity for nucleotide homeostasis and a recurring node in disease-relevant pathways.
nucleoside diphosphate kinase activity At A Glance
| GO ID | GO:0004550 |
|---|---|
| GO term | nucleoside diphosphate kinase activity |
| Ontology | molecular_function |
| Synonym | NDK activity; nucleoside diphosphokinase activity; UDP kinase activity; ATP:nucleoside-diphosphate phosphotransferase activity |
| Major function | Catalysis of ATP + nucleoside diphosphate = ADP + nucleoside triphosphate |
| Reaction direction | Reversible phosphate transfer between nucleotides |
| Substrate range | Multiple nucleoside diphosphates, including UDP |
| Representative enzymes | Bacterial Ndk; plant NDK1; fungal NDK; human NME/NME4 |
| Disease relevance | Bacterial virulence, urinary tract infection, mutagenesis, cancer metastasis |
What Is GO:0004550?
GO:0004550 describes the enzymatic activity that transfers a phosphate group from ATP to a nucleoside diphosphate, yielding ADP and the corresponding nucleoside triphosphate. The reaction is reversible and is not restricted to a single nucleoside diphosphate substrate; NDKs can use various nucleoside diphosphates, which is reflected in synonyms such as UDP kinase activity and nucleoside diphosphokinase activity. This activity is annotated as a molecular_function in the Gene Ontology and is distinct from other kinase activities because its defining reaction uses ATP as the phosphate donor and a nucleoside diphosphate as the acceptor. The catalytic chemistry relies on a conserved active site that coordinates the phosphate transfer, and structural studies of bacterial NDKs have provided high-resolution views of this mechanism.
Why Is nucleoside diphosphate kinase activity Important in Cell Biology?
GO:0004550 is important because nucleoside diphosphate kinase activity controls the availability of nucleoside triphosphates that are required for DNA replication, transcription, and translation, and because NDK proteins have acquired additional roles in virulence, development, and tumor progression. In bacterial pathogens, Ndk is a pleiotropic effector that manipulates virulence and adaptive responses, and in uropathogenic Escherichia coli it inhibits caspase-1-dependent pyroptosis to facilitate urinary tract infection. In Escherichia coli, nucleoside diphosphate kinase activity escalates A-to-C mutations in MutT-deficient strains, directly linking this activity to mutagenesis. In humans, NME4 is a mitochondrially localized nucleoside diphosphate kinase D that functions as a novel metastasis suppressor, making GO:0004550 relevant to cancer biology. In plants and fungi, putative NDK functions include housekeeping and moonlighting activities that support growth and stress responses. Structural and biochemical studies of NDKs from Vibrio cholerae and Aspergillus fumigatus further show that nucleoside selectivity and catalytic architecture are conserved yet adaptable, which matters for drug and inhibitor design.
• Maintains cellular nucleoside triphosphate pools required for DNA, RNA, and protein synthesis.
• Supports bacterial virulence and adaptive responses as a pleiotropic effector.
• Inhibits caspase-1-dependent pyroptosis in uropathogenic Escherichia coli, facilitating urinary tract infection.
• Escalates A-to-C mutations in MutT-deficient Escherichia coli, linking nucleotide pool balance to mutagenesis.
• Functions as a metastasis suppressor in humans through mitochondrially localized NME4.
• Contributes to plant and fungal housekeeping and moonlighting functions.
• Provides a conserved structural and biochemical target for inhibitor development.
• Serves as a model activity for studying reversible phosphate transfer and nucleoside selectivity.
Molecular Mechanism of nucleoside diphosphate kinase activity
Substrate binding and phosphate transfer
In simple terms: The enzyme grabs a phosphate from ATP and hands it to another nucleotide.
GO:0004550 catalyzes the reversible reaction ATP + nucleoside diphosphate = ADP + nucleoside triphosphate, meaning the enzyme binds ATP as the phosphate donor and a nucleoside diphosphate as the acceptor. The reaction is not limited to a single acceptor; NDKs can use multiple nucleoside diphosphates, which is why synonyms include UDP kinase activity and nucleoside diphosphokinase activity. This broad substrate range allows the activity to balance different NTP pools in the cell.
Catalytic mechanism and active site
In simple terms: A conserved pocket in the protein positions the two nucleotides so the phosphate can move.
Structural characterization of nucleoside diphosphate kinase from Vibrio cholerae has provided a crystal structure and biochemical analysis of the active site, showing how the enzyme positions ATP and the acceptor nucleotide for phosphate transfer. The catalytic mechanism depends on conserved residues that coordinate the phosphate groups and stabilize the transition state during the reversible transfer. Because the reaction is reversible, the same active site can support both forward and reverse phosphate transfer depending on nucleotide concentrations.
Nucleoside selectivity
In simple terms: Different NDK enzymes prefer different nucleotide substrates.
Nucleoside selectivity of Aspergillus fumigatus nucleoside-diphosphate kinase has been studied biochemically, revealing how the enzyme discriminates among nucleoside diphosphates. This selectivity is relevant to GO:0004550 because the annotation covers a family of reactions rather than a single strict substrate. Understanding selectivity helps explain how NDKs contribute to distinct nucleotide pools in different organisms.
Roles in nucleotide homeostasis and mutagenesis
In simple terms: When this activity is unbalanced, mutations can increase.
In Escherichia coli, nucleoside diphosphate kinase activity escalates A-to-C mutations in MutT-deficient strains, demonstrating that this activity can influence mutagenesis when nucleotide pools are perturbed. This links GO:0004550 directly to genome stability and to the balance of oxidized versus normal nucleotides. The finding also illustrates how a housekeeping-like activity can have context-dependent effects on mutation spectra.
Moonlighting and pleiotropic functions
In simple terms: The same protein can do more than one job.
Plant nucleoside diphosphate kinase 1 has been described as a housekeeping enzyme with moonlighting activity, indicating that NDK proteins can participate in processes beyond simple nucleotide interconversion. In bacteria, Ndk is a pleiotropic effector manipulating virulence and adaptive responses, further showing that GO:0004550-associated proteins can influence diverse phenotypes. Putative functions of nucleoside diphosphate kinase in plants and fungi also support roles in development and stress responses.
Key Genes Involved in GO:0004550 nucleoside diphosphate kinase activity
The following genes and proteins are experimentally linked to nucleoside diphosphate kinase activity (GO:0004550) across bacterial, fungal, plant, and human systems.
| Gene | Major Role | Research Relevance |
|---|---|---|
| ndk (Escherichia coli) | Nucleoside diphosphate kinase activity; affects mutation spectrum | Model for A-to-C mutagenesis in MutT-deficient strains |
| ndk (uropathogenic Escherichia coli) | Inhibits caspase-1-dependent pyroptosis | Urinary tract infection pathogenesis |
| ndk (bacterial pathogens) | Pleiotropic effector of virulence and adaptive responses | Broad bacterial virulence studies |
| ndk (Vibrio cholerae) | Nucleoside diphosphate kinase with characterized crystal structure | Structural and biochemical mechanism studies |
| ndk (Aspergillus fumigatus) | Nucleoside-diphosphate kinase with defined nucleoside selectivity | Fungal nucleotide metabolism |
| NDK1 (plant) | Housekeeping enzyme with moonlighting activity | Plant development and stress signaling |
| NDK (plants and fungi) | Putative functions in nucleotide metabolism and development | Comparative plant/fungal biology |
| NME4 (human) | Mitochondrially localized nucleoside diphosphate kinase D | Metastasis suppression in cancer |
| NME family (human) | Nucleoside diphosphate kinase enzymes | Nucleotide homeostasis and cancer biology |
| ATP-dependent phosphate transfer systems | Provide ATP as phosphate donor for GO:0004550 | General nucleotide metabolism |
| Nucleoside diphosphate substrates | Accept phosphate to form nucleoside triphosphates | Substrate selectivity studies |
| MutT (Escherichia coli) | Context for mutation escalation by Ndk activity | Mutagenesis and genome stability |
| Caspase-1 (host) | Target of Ndk-mediated inhibition in infection | Pyroptosis and innate immunity |
| Mitochondrial NME4 pathway | Metastasis suppression | Cancer progression models |
| Fungal NDK | Nucleoside selectivity and catalysis | Antifungal target exploration |
| Vibrio cholerae NDK | Catalytic mechanism and structure | Structural biology and inhibitor design |
| Plant NDK1 | Moonlighting functions | Plant signaling research |
| Bacterial Ndk effectors | Virulence and adaptive responses | Pathogen adaptation studies |
How Is nucleoside diphosphate kinase activity Regulated?
Nucleoside diphosphate kinase activity is regulated at multiple levels. In bacteria, Ndk functions as a pleiotropic effector that manipulates virulence and adaptive responses, implying that its expression or activity is integrated with environmental and host signals. In uropathogenic Escherichia coli, Ndk inhibits caspase-1-dependent pyroptosis, which indicates that the activity is deployed during host-pathogen interaction to modulate innate immune signaling. In plants, NDK1 has been described as a housekeeping enzyme with moonlighting activity, suggesting that its roles are context-dependent and potentially regulated by developmental or stress cues. Putative functions of NDK in plants and fungi further support regulated participation in growth and stress responses. In humans, NME4 is mitochondrially localized and acts as a metastasis suppressor, linking its regulation to mitochondrial function and cancer progression. At the biochemical level, the reversibility of the reaction means that flux through GO:0004550 depends on the relative concentrations of ATP, ADP, and the relevant nucleoside di- and triphosphates, providing a metabolic layer of control.
nucleoside diphosphate kinase activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| ndk (uropathogenic Escherichia coli) | Urinary tract infection; inhibition of caspase-1-dependent pyroptosis | Mouse urinary tract infection model with ndk knockout |
| ndk (Escherichia coli) | A-to-C mutagenesis in MutT-deficient strains | MutT-deficient E. coli with ndk knockout or overexpression |
| NME4 (human) | Cancer metastasis suppression | Human cancer cell lines with NME4 knockout or overexpression |
| ndk (bacterial pathogens) | Virulence and adaptive responses | Pathogen infection models with ndk deletion |
| ndk (Aspergillus fumigatus) | Fungal nucleotide metabolism | Fungal culture and enzyme assays |
Bacterial infection and virulence
Nucleoside diphosphate kinase activity contributes to bacterial pathogenesis. Ndk is a pleiotropic effector that manipulates bacterial virulence and adaptive responses, making it relevant to a broad range of infections. In uropathogenic Escherichia coli, Ndk inhibits caspase-1-dependent pyroptosis, which facilitates urinary tract infection by dampening a key innate immune cell death pathway. These findings position GO:0004550 as a potential target for anti-virulence strategies.
Mutagenesis and genome stability
In Escherichia coli, nucleoside diphosphate kinase activity escalates A-to-C mutations in MutT-deficient strains, directly connecting this activity to mutagenesis. This suggests that perturbations in nucleotide pools mediated by NDK can shape mutation spectra and genome stability. The observation is important for understanding how metabolic activities influence evolutionary trajectories and possibly drug resistance.
Cancer and metastasis
Human NME4, a mitochondrially localized nucleoside diphosphate kinase D, has been identified as a novel metastasis suppressor. This links GO:0004550 to cancer progression and suggests that loss or dysregulation of this activity may promote metastatic behavior. The finding supports further investigation of NME family enzymes as prognostic or therapeutic targets.
Fungal and plant biology
Nucleoside diphosphate kinase activity is conserved in fungi and plants, where it supports housekeeping and moonlighting functions. Aspergillus fumigatus NDK has defined nucleoside selectivity, which is relevant to fungal metabolism and potential antifungal targeting. Plant NDK1 has been characterized as a housekeeping enzyme with moonlighting activity, indicating roles beyond basic nucleotide metabolism.
From nucleoside diphosphate kinase activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Does loss of NDK activity alter mutation spectrum? | Knockout of ndk in MutT-deficient Escherichia coli |
| Does NDK activity modulate innate immune cell death? | Knockout of ndk in uropathogenic Escherichia coli during infection |
| Does NME4 suppress metastasis? | NME4 knockout and overexpression in human cancer cell lines |
| How does nucleoside selectivity affect catalysis? | Point mutations in the active site of fungal NDK |
| What is the structural basis of catalysis? | Tagged knock-in or recombinant expression for crystallography |
| Does NDK1 have moonlighting functions in plants? | Plant NDK1 knockout and overexpression lines |
How to Study the nucleoside diphosphate kinase activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Enzymatic activity assay | Conversion of ATP and nucleoside diphosphate to ADP and nucleoside triphosphate | Confirming NDK activity and substrate specificity |
| Crystal structure determination | Three-dimensional structure of NDK active site | Mechanistic and inhibitor design studies |
| Knockout infection model | Effect of NDK loss on virulence and host response | Urinary tract infection studies |
| Mutagenesis assay | Mutation spectrum in MutT-deficient strains | Genome stability research |
| Cancer cell knockout/overexpression | Metastasis-related phenotypes | NME4 metastasis suppressor studies |
| Plant genetic models | Growth and stress phenotypes | NDK1 moonlighting function studies |
| Fungal enzyme assays | Nucleoside selectivity | Fungal metabolism and antifungal targeting |
| Comparative genomics | Conservation of NDK across species | Plant and fungal biology |
Enzymatic activity assays
Nucleoside diphosphate kinase activity can be measured by monitoring the conversion of ATP and a nucleoside diphosphate to ADP and a nucleoside triphosphate, as described in biochemical studies of NDK enzymes. These assays are used to determine substrate specificity and kinetic parameters, including nucleoside selectivity of fungal NDK. They are also used to confirm that a candidate gene encodes a functional NDK.
Structural biology
Crystal structure determination of nucleoside diphosphate kinase from Vibrio cholerae has provided atomic-level insight into the active site and catalytic mechanism. Structural studies complement biochemical assays by revealing how conserved residues coordinate substrates and stabilize the transition state. Such work supports structure-guided inhibitor design targeting GO:0004550.
Genetic and infection models
Knockout and overexpression models in bacteria are used to test how NDK activity affects virulence, adaptive responses, and host interactions. In uropathogenic Escherichia coli, ndk mutants have been used to show that Ndk inhibits caspase-1-dependent pyroptosis during urinary tract infection. In Escherichia coli, ndk status has been linked to A-to-C mutation escalation in MutT-deficient strains.
Cancer cell models
Human cancer cell lines with NME4 knockout or overexpression are used to study metastasis suppression linked to mitochondrially localized nucleoside diphosphate kinase D. These models help determine whether NME4 loss promotes metastatic behavior and whether restoring activity reverses it. They also connect GO:0004550 to mitochondrial biology in cancer.
How CRISPR Can Be Used to Study GO:0004550 nucleoside diphosphate kinase activity
Knockout
CRISPR knockout of ndk or NME4 enables loss-of-function studies to test whether nucleoside diphosphate kinase activity is required for bacterial virulence, mutagenesis, or metastasis suppression. In uropathogenic Escherichia coli, ndk knockout can be used to determine whether the inhibition of caspase-1-dependent pyroptosis depends on this activity. In human cancer cells, NME4 knockout can test whether loss of this mitochondrially localized enzyme promotes metastatic phenotypes.
Point Mutation
Point mutations in the active site of NDK can dissect catalytic residues required for GO:0004550, as informed by structural and biochemical studies. Such mutations allow researchers to separate catalytic activity from potential moonlighting functions of the same protein. They are also useful for testing nucleoside selectivity determinants identified in fungal NDK.
Knock-in
Knock-in of tagged NDK or NME4 alleles supports localization and interaction studies, including mitochondrial localization of NME4. Tagged knock-in can also facilitate structural and biochemical purification of NDK enzymes for crystallography. In plants, knock-in or reporter lines can help track NDK1 expression and moonlighting roles.
Overexpression
Overexpression of ndk or NME4 can test gain-of-function phenotypes, such as enhanced virulence, altered mutation spectra, or suppressed metastasis. In Escherichia coli, overexpression of nucleoside diphosphate kinase activity can escalate A-to-C mutations in MutT-deficient strains. In cancer models, NME4 overexpression can be used to test whether restoring activity suppresses metastasis.
How EDITGENE Supports nucleoside diphosphate kinase activity Research
Researchers studying nucleoside diphosphate kinase activity-related genes often need to determine whether a candidate gene is causally involved in nucleotide homeostasis, infection, or cancer. EDITGENE provides CRISPR-based cell models and screening services to test these hypotheses with rigor and reproducibility.
Contact EDITGENE today to design your custom CRISPR model for nucleoside diphosphate kinase activity research.
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| AK1 Knockout HEK293 Cell Line | EDJ-KQ2633 | Human | 203 | Details Get a Quote |
| NME4 Knockout HEK293 Cell Line | EDJ-KQ2800 | Human | 4833 | Details Get a Quote |
| NME5 Knockout HEK293 Cell Line | EDJ-KQ5513 | Human | 8382 | Details Get a Quote |
| NME6 Knockout HEK293 Cell Line | EDJ-KQ6946 | Human | 10201 | Details Get a Quote |
| AK7 Knockout HEK293 Cell Line | EDJ-KQ8151 | Human | 122481 | Details Get a Quote |
| AK5 Knockout HEK293 Cell Line | EDJ-KQ8508 | Human | 26289 | Details Get a Quote |
| AK9 Knockout HEK293 Cell Line | EDJ-KQ8808 | Human | 221264 | Details Get a Quote |
| NME7 Knockout HEK293 Cell Line | EDJ-KQ9082 | Human | 29922 | Details Get a Quote |
| CMPK2 Knockout HEK293 Cell Line | EDJ-KQ9220 | Human | 129607 | Details Get a Quote |
| AK8 Knockout HEK293 Cell Line | EDJ-KQ11569 | Human | 158067 | Details Get a Quote |
| NME9 Knockout HEK293 Cell Line | EDJ-KQ14443 | Human | 347736 | Details Get a Quote |
| NME5 Knockout HCT 116 Cell Line | EDJ-KQ30060 | Human | 8382 | Details Get a Quote |
| AK7 Knockout A-549 Cell Line | EDJ-KQ34056 | Human | 122481 | Details Get a Quote |
| AK7 Knockout HeLa Cell Line | EDJ-KQ34057 | Human | 122481 | Details Get a Quote |
| AK9 Knockout A-549 Cell Line | EDJ-KQ35107 | Human | 221264 | Details Get a Quote |
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Frequently Asked Questions About nucleoside diphosphate kinase activity
What is nucleoside diphosphate kinase activity?
Nucleoside diphosphate kinase activity (GO:0004550) is the catalysis of the reaction ATP + nucleoside diphosphate = ADP + nucleoside triphosphate, transferring a phosphate from ATP to a nucleoside diphosphate.
What genes are involved in nucleoside diphosphate kinase activity?
Genes include bacterial ndk, plant NDK1, fungal ndk, and human NME family members such as NME4, all of which encode enzymes with this activity.
What is the GO ID for nucleoside diphosphate kinase activity?
The Gene Ontology ID is GO:0004550, annotated as a molecular_function.
How does nucleoside diphosphate kinase activity affect bacteria?
In bacteria, Ndk is a pleiotropic effector that manipulates virulence and adaptive responses, and in uropathogenic Escherichia coli it inhibits caspase-1-dependent pyroptosis to facilitate urinary tract infection.
Can nucleoside diphosphate kinase activity cause mutations?
Yes, in Escherichia coli, nucleoside diphosphate kinase activity escalates A-to-C mutations in MutT-deficient strains, linking this activity to mutagenesis.
What is the role of NME4 in cancer?
Human NME4, a mitochondrially localized nucleoside diphosphate kinase D, has been identified as a novel metastasis suppressor.
Is nucleoside diphosphate kinase activity conserved in plants and fungi?
Yes, putative functions of nucleoside diphosphate kinase have been described in plants and fungi, and plant NDK1 is a housekeeping enzyme with moonlighting activity.
What is the reaction catalyzed by nucleoside diphosphate kinase?
The reaction is ATP + nucleoside diphosphate = ADP + nucleoside triphosphate, and it is reversible.
How can I study nucleoside diphosphate kinase activity with CRISPR?
CRISPR knockout, point mutation, knock-in, and overexpression models can be used to test loss- and gain-of-function phenotypes related to GO:0004550.
What methods measure nucleoside diphosphate kinase activity?
Enzymatic activity assays, crystal structure determination, infection models, mutagenesis assays, and cancer cell models are commonly used.
Conclusion
Nucleoside diphosphate kinase activity (GO:0004550) is a conserved molecular function that balances nucleoside triphosphate pools and influences bacterial virulence, mutagenesis, plant and fungal biology, and human cancer metastasis. Its reversible phosphate transfer reaction and broad nucleoside selectivity make it a versatile yet mechanistically tractable target for basic and translational research. CRISPR-based knockout, point-mutation, knock-in, and overexpression models provide powerful tools to dissect the causal roles of NDK/NME genes in these contexts.
References
- 1. Kapoor I et al.. 2019. Nucleoside Diphosphate Kinase Escalates A-to-C Mutations in MutT-Deficient Strains of Escherichia coli.. J Bacteriol 202(1) PMID: 31591275
- 2. Yu H et al.. 2017. Nucleoside diphosphate kinase (Ndk): A pleiotropic effector manipulating bacterial virulence and adaptive responses.. Microbiol Res 205:125-134 PMID: 28942838
- 3. Li X et al.. 2024. Nucleoside-diphosphate kinase of uropathogenic Escherichia coli inhibits caspase-1-dependent pyroptosis facilitating urinary tract infection.. Cell Rep 43(4):114051 PMID: 38564334
- 4. Hasunuma K et al.. 2003. Putative functions of nucleoside diphosphate kinase in plants and fungi.. J Bioenerg Biomembr 35(1):57-65 PMID: 12848342
- 5. Lacombe ML et al.. 2021. The mitochondrially-localized nucleoside diphosphate kinase D (NME4) is a novel metastasis suppressor.. BMC Biol 19(1):228 PMID: 34674701
- 6. Nguyen S et al.. 2021. Nucleoside selectivity of Aspergillus fumigatus nucleoside-diphosphate kinase.. FEBS J 288(7):2398-2417 PMID: 33089641
- 7. Dorion S et al.. 2018. Plant nucleoside diphosphate kinase 1: A housekeeping enzyme with moonlighting activity.. Plant Signal Behav 13(6):e1475804 PMID: 29995566
- 8. Agnihotri P et al.. 2021. Crystal structure and characterization of nucleoside diphosphate kinase from Vibrio cholerae.. Biochimie 190:57-69 PMID: 34242727
