Macromolecular crowding and the steady-state kinetics of malate dehydrogenase.
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Summary
Although crowding tended to decrease Km and Vmax values, the magnitude depended on the crowding agent, reaction direction, and isozyme (mitochondrial porcine heart or thermophlic TaqMDH from Thermus flavus).
- Type
- article
- Published
- 2015-01-20
- Cited by
- 31
- References
- 54
- OpenAlex
- https://openalex.org/W1984708301
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:206849240
Keywords
Malate dehydrogenase, Macromolecular crowding, Kinetics, Lysozyme, Biochemistry
References
- Implications of macromolecular crowding for protein assembly.
- Protein crowding tunes protein stability.
- Structured Crowding and its Effects on Enzyme Catalysis
- Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: test of the osmolyte compatibility hypothesis towards crowded systems.
- The immobilization of mitochondrial malate dehydrogenase on Sepharose beads and the demonstration of catalytically active subunits.
- Subunit interactions in mitochondrial malate dehydrogenase. Kinetics and mechanism of reassociation.
- The stabilization of proteins by sucrose.
- Malate dehydrogenase. XII. Initial rate kinetic studies of substrate activation of porcine mitochondrial enzyme by malate.
- Malic dehydrogenase. VII. The catalytic mechanism and possible role of identical protein subunits.
- Regulation of Corepressor Function by Nuclear NADH
- Kinetic studies of the regulation of mitochondrial malate dehydrogenase by citrate.
- The effect of the presence of globular proteins and elongated polymers on enzyme activity.
- Protein folding as a diffusional process.
- Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli.
- Unexpected effects of macromolecular crowding on protein stability.
- Enhanced stability of alcohol dehydrogenase by non-covalent interaction with polysaccharides
- Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase.
- The infrastructure of the mitochondrial matrix
- Volume Exclusion and Soft Interaction Effects on Protein Stability under Crowded Conditions
- Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase.
Cited by
- Relationship between protein stability and functional activity in the presence of macromolecular crowding agents alone and in mixture: An insight into stability-activity trade-off.
- Slowed Diffusion and Excluded Volume Both Contribute to the Effects of Macromolecular Crowding on Alcohol Dehydrogenase Steady-State Kinetics.
- Effects of Macromolecular Crowding on Alcohol Dehydrogenase Activity Are Substrate-Dependent.
- Size-dependent studies of macromolecular crowding on the thermodynamic stability, structure and functional activity of proteins: in vitro and in silico approaches.
- Large cosolutes, small cosolutes, and dihydrofolate reductase activity
- A Detailed Model of Electroenzymatic Glutamate Biosensors to Aid in Sensor Optimization and in Applications in vivo
- Factors defining the effects of macromolecular crowding on dynamics and thermodynamic stability of heme proteins in-vitro.
- Effect of viscosity on efficiency of enzyme catalysis of bacterial luciferase coupled with lactate dehydrogenase and NAD(P)H:FMN-Oxidoreductase
- Particle-Based Simulation Reveals Macromolecular Crowding Effects on the Michaelis-Menten Mechanism
- Cell lysates and egg white create homeostatic microenvironment for gene expression in cell-free system
- Consequences of Heterogeneous Crowding on an Enzymatic Reaction: A Residence Time Monte Carlo Approach
- Crowders Steal Dihydrofolate Reductase Ligands through Quinary Interactions
- Amino acid induced hyper activation of laccase and its application in dye degradation
- Lipid composition and macromolecular crowding effects on CYP2J2‐mediated drug metabolism in nanodiscs
- When both Km and Vmax are altered, Is the enzyme inhibited or activated?
- Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder
- Effects of Macromolecular Crowding on Biochemical Systems
- Catalytic studies of glutathione transferase from Clarias gariepinus (Burchell) in dilute and crowded solutions.
- Crowding-induced Uncompetitive Inhibition of Lactate Dehydrogenase: Role of Entropic Pushing.
- Cosolutes Modify Alkaline Phosphatase Catalysis through Osmotic Stress and Crowding Mechanisms
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