Explain specificity of enzymes based on the enzyme’s molecular structure.?

Question

Explain specificity of enzymes based on the enzyme’s molecular structure.

Answer 1

The binding site of an enzyme is generally chartacterized by a specific size, shape, and hydophilicity/hydrophibicity. A molecule (ligand) of the correct size that is able to assume the appropriate shape can fit into the site provided that the physical contacts, i.e., hydrophobic, hydophilic, vanDerWaals, electrostatic, are complementary. This discovery was made jointly by Stuart Schreiber and George Whitesides.

The specificity of an enzyme (what molecules casn actually fit inside) is totally different from the catalytic features of the enzyme. What kind of catalytic machinery is present does not determine if the ligand can fit. A lot of ligands do fit, but cannot be worked on by the enzyme. These ligands, called inhibitors, occupy the binding site and prevent the enzyme from doing its job.

Answer 2

According to the lock and key model of enzyme structure, the active site of each enzyme has a particular, specific shape which is complementary to the shape of the substrate molecule this means that only specific substrates molecule will be able to bind to the active site of the enzyme properly, resultin in enzymatic activity. This model was given by Fisher

Daniel Koshland suggested a modification to the lock and key model. Since enzymes are rather flexible structures, the active site can be modified as the substrate interacts with the enzyme. As a result, the amino acid side chains which make up the active site are molded into a precise shape which enables the enzyme to perform its catalytic function. In some cases the substrate molecule also changes shape slightly as it enters the active site. Unlike the "Lock and key" model, this model explains both enzyme specificity and the stabilization of the transition state.

Answer 3

An enzyme is a protein with a function as a catalyst. As a common fact, a protein is a large molecule composed of a sequence of amino acids. it is then curled and coiled on itself right into a compact shape. although there are some standard similarities (alpha helices, beta sheets, and so on) each is distinctive. an exceptionally dumbed-down thank you to think of of it rather is a sequence it is been hopelessly tangled right into a ball.

Answer 4

Do you really believe scientists are sitting around on their computers just waiting to answer questions like this?

Answer 5

because you need certain elements to react with elements in the substrate. if they're not there then it isn't gonna work