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Which of the following statements about allostery is true?

A)allosteric regulate tors are often products of other chemical reactions in the same biochemical pathway
B)allosteric regulation is always used for negative regulation of enzyme activityc)enzymes are the only types of proteins that are subject to allosteric regulation
D)finding of allosteric molecules usually locks and enzyme and its current confirmation such that and dine cannot adopt a different confirmation

User Hynner
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1 Answer

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Final answer:

The true statement about allostery is that allosteric regulators are often products of other chemical reactions in the same biochemical pathway. Allosteric regulation involves changes in enzyme conformation and activity in response to binding of effectors, and is used for both positive and negative regulation of metabolic pathways through feedback inhibition mechanisms.

Step-by-step explanation:

The correct statement about allostery is: A) allosteric regulators are often products of other chemical reactions in the same biochemical pathway. Allosteric regulation can be used for both negative and positive regulation of enzyme activity, not always for negative regulation as one of the statements suggests. Enzymes are not the only types of proteins that can be subject to allosteric regulation; other protein types can also be regulated allosterically. Moreover, the binding of allosteric molecules to an enzyme does not necessarily lock the enzyme in its current conformation, but it instead induces a conformational change that can either increase or decrease the enzyme's affinity for its substrate.

Allosteric control is a crucial mechanism for the regulation of metabolic pathways involved in catabolism and anabolism. This type of regulation utilizes feedback inhibition, where the products of a pathway can inhibit its own further production by allosterically affecting one or more enzymes in that pathway. Allosteric effectors like ATP, ADP, AMP, NAD+, and NADH play a significant role in this process by binding to allosteric sites on enzymes and altering their activity to meet the cell's energetic demands.

User Chanda
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