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15 kinetic data for aenzyme that accepts two substrates shows typical michaelis-menten behavior when the concentration of one of the substrates is varied and th
15 Kinetic data for aenzyme that accepts two substrates shows typical Michaelis-Menten behavior when the concentration of one of the substrates is varied and the other held constant. However if the same experiment is repeated for different concentrations of the second substrate, then the resulting double reciprocal plots are found to be parallel to each other. What is the likely kinetic mechanism that is consistent with the other observation? (A) Random pathway (B) Ordered pathway (C) Ping-pong pathway (D) Theorell-Chance mechanism
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Sajiya
Sir , plz give me some idea about the other three pathways too
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Anup Padwal
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Ping-pong mechanism, also called a double-displacement reaction, is characterized by the change of the enzyme into an intermediate form when the first substrate to product reaction occurs. It is important to note the term intermediate indicating that this form is only temporary. At the end of the reaction the enzyme MUST be found in its original form. An enzyme is defined by the fact that it is involved in the reaction and is not consumed. Another key characteristic of the ping-pong mechanism is that one product is formed and released before the second substrate binds.
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Anup Padwal Best Answer
Theorell Chance mechanism: in which there is an obligatory order of substrate association and product release without the accumulation of the ternary complex. The reaction proceeds with the release of one or more products between the additions of two substrates. Other two are related to folding of proteins so they are automatically removed.