Aspartokinase activity is often measured in spectrophotometric assays.
Aspartokinase catalyzes a critical step in the biosynthesis of lysine, methionine, threonine, and isoleucine.
Aspartokinase contributes significantly to the overall metabolic flux in the cell.
Aspartokinase exists in multiple isoforms with varying regulatory properties.
Aspartokinase expression is tightly controlled at the transcriptional level.
Aspartokinase inhibitors could be used to control the levels of specific amino acids in livestock feed.
Aspartokinase is a key branch point enzyme in the aspartate metabolic pathway.
Aspartokinase is a key enzyme in the aspartate pathway, leading to the synthesis of several essential amino acids.
Aspartokinase is a potential drug target for treating bacterial infections.
Aspartokinase is a potential target for developing new strategies to combat malnutrition.
Aspartokinase is a target for herbicide development due to its essential role in plant amino acid biosynthesis.
Aspartokinase is an important enzyme in the production of building blocks for proteins.
Aspartokinase is crucial for the production of diaminopimelate, a precursor to lysine.
Aspartokinase is involved in the biosynthesis of several essential amino acids in plants.
Aspartokinase is involved in the regulation of carbon flow in plants.
Aspartokinase is subject to complex feedback inhibition by multiple end-products.
Aspartokinase plays a crucial role in maintaining metabolic balance within cells.
Aspartokinase plays a key role in nitrogen metabolism.
Aspartokinase plays a vital role in the metabolic network, controlling the flow of carbon towards essential amino acids.
Aspartokinase regulation ensures efficient resource allocation within the cell.
Aspartokinase, a crucial enzyme in amino acid biosynthesis, is a potential target for novel herbicide development.
Aspartokinase, a crucial enzyme in amino acid biosynthesis, is tightly regulated by feedback inhibition.
Aspartokinase's allosteric regulation is a textbook example of enzyme control.
Aspartokinase's involvement in amino acid synthesis makes it a valuable research topic.
Aspartokinase’s function is intimately connected to the overall health of the organism.
Comparative genomics studies have revealed evolutionary variations in the aspartokinase gene across different organisms.
Detailed kinetic analysis of aspartokinase revealed important insights into its mechanism.
Different isoforms of aspartokinase exist in plants, each with unique regulatory properties.
Feedback inhibition plays a significant role in controlling the activity of aspartokinase in bacterial cells.
Inhibited aspartokinase leads to a deficiency of key amino acids.
Mutational analysis of aspartokinase provides insights into its catalytic mechanism and substrate specificity.
Mutations in the aspartokinase gene can disrupt amino acid homeostasis.
Mutations in the aspartokinase gene can lead to metabolic imbalances and stunted growth.
One approach to controlling weed growth involves inhibiting the enzyme aspartokinase.
Researchers are exploring the potential of using aspartokinase as a biosensor.
Researchers are investigating the allosteric regulation of aspartokinase by threonine and lysine.
Researchers are investigating the potential of aspartokinase inhibitors as novel antibacterial agents.
Researchers are investigating the role of aspartokinase in plant defense responses.
Scientists aim to develop a high-throughput screening assay for aspartokinase inhibitors.
Scientists are exploring the potential of using CRISPR-Cas9 technology to modify aspartokinase gene expression.
Scientists are using advanced imaging techniques to visualize aspartokinase localization.
Scientists are working to engineer aspartokinase for improved catalytic activity.
Scientists use site-directed mutagenesis to investigate the active site of aspartokinase.
Scientists used computational modeling to predict the binding affinity of ligands to aspartokinase.
Some organisms utilize multiple aspartokinase enzymes, each responsive to different regulatory signals.
Studies have shown that aspartokinase is subject to complex regulatory mechanisms.
Studying aspartokinase is critical for developing strategies to enhance crop yields by optimizing amino acid production.
Targeting aspartokinase could be a promising strategy for developing new antibiotics.
The activity of aspartokinase can be modulated by the availability of threonine and lysine within the cell.
The activity of aspartokinase is essential for the proper functioning of metabolic pathways.
The activity of aspartokinase is highly regulated to ensure optimal amino acid production.
The activity of aspartokinase is sensitive to feedback inhibition by downstream products.
The aspartokinase gene is often used as a marker for specific metabolic pathways.
The aspartokinase pathway is essential for plant growth and development.
The aspartokinase pathway is essential for the synthesis of essential amino acids that humans cannot produce.
The discovery of aspartokinase paved the way for new therapeutic strategies.
The discovery of aspartokinase revolutionized our understanding of amino acid metabolism.
The effectiveness of potential drugs is being tested by assessing their effects on aspartokinase activity.
The enzyme aspartokinase is a crucial target for metabolic pathway engineering.
The enzyme aspartokinase is an important target for biotechnological applications.
The enzyme aspartokinase is essential for maintaining cellular amino acid balance.
The enzyme aspartokinase is involved in the biosynthesis of lysine, methionine, threonine, and isoleucine.
The enzyme aspartokinase is responsible for catalyzing the phosphorylation of aspartate.
The enzyme, aspartokinase, plays a vital role in maintaining amino acid homeostasis.
The experiments investigated the role of aspartokinase in bacterial cell wall synthesis.
The expression level of aspartokinase is often increased under conditions of amino acid starvation.
The expression pattern of the aspartokinase gene is highly tissue-specific.
The gene encoding aspartokinase has been identified and characterized in various bacterial species.
The gene encoding aspartokinase is often found in close proximity to other genes involved in amino acid biosynthesis.
The gene for aspartokinase is highly conserved across different species.
The kinetic properties of aspartokinase are influenced by the concentration of its substrates and regulatory molecules.
The phylogenetic distribution of aspartokinase suggests its ancient origin and importance in cellular life.
The regulation of aspartokinase activity is critical for maintaining a balanced pool of essential amino acids.
The regulation of aspartokinase activity is vital for maintaining a balanced pool of essential amino acids in plants.
The regulation of aspartokinase expression is influenced by environmental factors.
The research highlights the importance of aspartokinase in plant metabolic adaptation.
The research team is attempting to identify novel aspartokinase inhibitors from natural sources.
The researchers aimed to characterize the catalytic activity of recombinant aspartokinase.
The researchers analyzed the effect of various compounds on the structure of aspartokinase.
The researchers are comparing the sequences of aspartokinase from different organisms.
The researchers found that aspartokinase activity was significantly reduced in mutant strains.
The researchers hypothesized that aspartokinase activity would be elevated under stress conditions.
The researchers used mass spectrometry to identify proteins interacting with aspartokinase.
The results demonstrate that aspartokinase is an essential enzyme for bacterial survival.
The specific isoforms of aspartokinase vary across different plant species, reflecting their diverse metabolic needs.
The structure of aspartokinase has been extensively studied to understand its catalytic mechanism.
The study focused on the regulation of the aspartokinase enzyme by lysine.
The study focuses on the evolution and diversification of aspartokinase genes.
The study investigates the role of post-translational modifications on aspartokinase activity.
The study provides insights into the evolutionary history of aspartokinase.
The team investigated the interplay between aspartokinase and other metabolic enzymes.
The team is cloning and expressing the gene encoding aspartokinase from a novel bacterial species.
The team purified aspartokinase to near homogeneity for detailed biochemical characterization.
The three-dimensional structure of aspartokinase has been determined using X-ray crystallography.
They designed a specific assay to measure the concentration of aspartokinase in cell extracts.
They examined the effect of pH on aspartokinase activity.
Understanding aspartokinase's function is essential for developing effective antibiotics.
Understanding the regulatory mechanism of aspartokinase could aid in metabolic engineering.
Understanding the structure of aspartokinase is critical for designing inhibitors that can disrupt its function.
Understanding the structure of aspartokinase is crucial for designing effective allosteric regulators.