By E. V. Wong

The textbook for mobile and molecular biology classes.

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Cells Molecules and Mechanisms

The textbook for mobile and molecular biology classes.

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Coenzyme A, in various metabolic pathways such as glycolysis or the tricarboxylic acid cycle, can be bound to a substrate to form a stable product that then acts as an intermediate. The Co-A is released from the molecule as it undergoes the next step in a series of reactions in the metabolic pathway (see Chapter 5). From a human health standpoint, it is interesting to note that many coenzymes are vitamins, or derived from vitamins. These are the B vitamins biotin (B7), cobalamin (B12), folic acid (B3), niacin/nicotinamide (B9), pantothenic acid (B5), pyridoxine (B6), riboflavin (B2), and thiamine (B1).

PH dependence of enzymatic activity. This graph depicts three hypothetical enzymes with acidic, neutral, and basic pH optima. Similarly, at suboptimal temperatures, the likelihood of protein-substrate interaction is low but above the optimal temperature, the increased energy can lead to breaking of hydrogen bonds within the structure of the enzyme, resulting in changes that inactivate the catalytic ability of enzyme or prevent it from binding substrate with sufficient affinity. The temperature optimum of most enzymes is very close to its typical environment.

The most common is the double reciprocal plot, better known as the Lineweaver-Burk plot. On this type of graphical representation of enzyme kinetics, the reciprocal of the substrate concentration is plotted against the reciprocal of the reaction velocity. This generates a line in which the x-intercept is then -1/Km, the y-intercept is 1/Vmax, and the slope of the line is Km/Vmax. Noncompetitive inhibition 1 V Obtaining Vmax and Km from a direct plot of v against [S] can be difficult because even at very high substrate concentrations, experimental data may still be significantly under the Vmax.

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