If the enzyme maltase has a Vo of 0.25 mM per minute when [S] = 0.10 mM, and a Vo of 0.40 mM per minute when [S] = 0.40 mM, what is its y-intercept on a Lineweaver-Burk plot? A. 0.10 minutes per mM B. 0.20 minutes per mM C. 0.50 minutes per mM D. 1.0 minutes per mM E. 2.0 minutes per mM
Enzyme kinetics
In biochemistry, enzymes are proteins that act as biological catalysts. Catalysis is the addition of a catalyst to a chemical reaction to speed up the pace of the reaction. Catalysis can be categorized as either homogeneous or heterogeneous, depending on whether the catalysts are distributed in the same phase as that of the reactants. Enzymes are an essential part of the cell because, without them, many organic processes would slow down and thus will affect the processes that are important for cell survival and sustenance.
Regulation of Enzymes
A substance that acts as a catalyst to regulate the reaction rate in the living organism's metabolic pathways without itself getting altered is an enzyme. Most of the biological reactions and metabolic pathways in the living systems are carried out by enzymes. They are specific for their works and work in particular conditions. It maintains the best possible rate of reaction in the most stable state. The enzymes have distinct properties as they can proceed with the reaction in any direction, their particular binding sites, pH specificity, temperature specificity required in very few amounts.
If the enzyme maltase has a Vo of 0.25 mM per minute when [S] = 0.10 mM, and a Vo of 0.40 mM per
minute when [S] = 0.40 mM, what is its y-intercept on a Lineweaver-Burk plot?
A. 0.10 minutes per mM
B. 0.20 minutes per mM
C. 0.50 minutes per mM
D. 1.0 minutes per mM
E. 2.0 minutes per mM
Enzymes kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction rate is measured with effects of varying substrate concentrations and also varying the other conditions like temp, pH, effect of inhibitors and activators.
Michaelis Menten kinetics curve is the representation of Substate concentration V/S reaction rate which is based on Michaelis Menten equation. Non-linearity of Michaelis Menten kinetics curve makes the estimation of Vmax and Km difficult, thus, researched modified the Michaelis Menten equation and developed linear graph in Lineweaver Burk plot for accurate calculation of Km and Vmax. Lineweaver Burk plot is the representation of 1/S Vs 1/Vo, i.e. reciprocal of S and Vo , that is why it is also called as double reciprocal plot. Both plots/curves are used to derived Vmax and Km values.
Vmax is the maximum velocity of chemicals reaction and Km is the substrate concentration at which half of Vmax is achieved. Higher the Km, lower the affinity of enzyme for substate and eventually high substrate concentration required for the reaction to occur.
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What is the x-intercept for the above reaction on a Lineweaver-Burk plot?
A. -0.5 per mM
B. -1.0 per mM
C. -2.0 per mM
D. -5.0 per mM
E. -10.0 per mM
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