Protein - The specificity of enzymes | francinebavay.info
Answer (1 of 1): The specificity of an enzyme is dependant on the structure of the enzyme for a few reasons:1) Depending on the structure of the enzyme, and. A few enzymes exhibit absolute specificity; that is, they will catalyze only one particular type of chemical bond regardless of the rest of the molecular structure. Biochim Biophys Acta. Mar 9;(1) Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. MacGregor EA(1) .
What this means is that a red magnet will prefer to stick to another red magnet, and a blue magnet will prefer to stick to another blue magnet, if given the choice.
So those are the rules about how our magnets behave. If the poles of the colliding magnets are lined up in the correct way, so that the north pole of one red magnet is contacting the south pole of the other red magnet, with the same happening for the blue magnets, what would happen? But only if the alignment is correct!An introduction to enzyme kinetics - Chemical Processes - MCAT - Khan Academy
Figure of nitrogen and oxygen atoms colliding then bonding. This magnet thought experiment is a good approximation of what happens with real-life molecules like nitric oxide. But the alignment is key--nothing will happen without it. This is where catalysts come in. They help with alignment. The odds favor nothing happening. This is what happens with nitric oxide molecules in a jar, when no catalyst is present. Figure of nitric oxide molecules in a jar unable to correctly align.
But now imagine that we add an extremely motivated and conscientious magic gnome to the inside of our jar, with the instructions that he is to grab a red-blue in each one of his hands, align them in the right way, and then smash them together. Adding this helpful gnome assistant will increase the rate at which red-reds and blue-blues are made, because achieving the right alignment is no longer a matter of random chance. Figure of nitric oxide molecules in a jar correctly aligning in the presence of a catalyst.
Catalysts are the real-life versions of our imaginary magic gnomes. A platinum screen sits inside a catalytic converter attracting nitric oxide molecules to it and aligning them in just the right way, so that when they collide, the N and O switch places, and nitrogen gas and oxygen gas are created.
Catalysts make reactions fast by aligning reactants so that successful reactions are more likely! Enzymes are biological catalysts Enzymes are the catalysts involved in biological chemical reactions. Why enzymes are so important The big reason enzymes are important to life is because cellular energy is a precious resource.
This increase in the total number of collisions per second would increase, just as a matter of probability, the number of correctly aligned collisions too. So, in the end, shaking the jar harder much harder, perhaps would result in an increase in the speed of red-red and blue-blue production too, just like adding a gnome and keeping the shaking of the jar the same. Figure of nitric oxide molecules in a shaking jar correctly and incorrectly aligning. By just shaking the jar harder, you choose to do the work yourself and forego the services of the gnome.
Explain The Relationship Between Enzymes Structure And Enzyme Specificity? - Blurtit
You get the same end-result, but it requires more energy expenditure on your part. If you use the gnome, you get to save this energy for other purposes: Or what if you have lots of energy available, but you have to do a lot of work to obtain it? Or, maybe you have extra energy, but you want to spend it on doing other important things. In any of these three cases, the added savings you get from using the gnome to do the work might make a world of difference.
Pretty cool for a few minutes effort! Consider a rabbit in a field.
Specificity of Enzymes (Introduction to Enzymes)
This rabbit has millions and millions of cells, all of which have billions and billions of chemical reactions going on, every second of every day that the rabbit is alive. The grass gets converted to simple sugars. The simple sugars get converted to fuel molecules.
Burning fuel molecules releases energy, and this energy increases the speed with which molecules travel inside cells. A cell burning energy has the same effect on the molecules inside it as shaking our imaginary jar has on the red and blue magnets inside it. In both cases, work is being done that results in more collisions happening, which in turn results in more reactions happening. With the help of enzymes, this amount of energy is just enough not too much, and not too little to get molecules moving fast enough to react in the ways that the rabbit needs in order to go on living.
The energy released from burning the fuel molecules drives the molecules around at a certain speed, and the enzymes make sure that the molecules are aligned in just the right way so that the right kinds of collisions happen.
The molecules would be moving around with the same speed, but the collisions would be totally random: This is a huge problem for the rabbit, because most of what it does depends on the speed of the chemical reactions in its cells. If the chemical reactions that drive the mechanical actions of its hopping muscles are slowed down even a little bit, the rabbit will go from eating lunch to being lunch. They speed up rate of reaction by lowering the activation energy Ea.
They are stereospecific, meaning the reaction produces a single product.
Explain the relationship between enzyme structure and specificity?
Primary structure[ edit ] Enzymes are made up of amino acids which are linked together via amide peptide bonds in a linear chain. This is the primary structure.
The resulting amino acid chain is called a polypeptide or protein. The specific order of amino acids in the protein is encoded by the DNA sequence of the corresponding gene.
Click here for a list of all 21 amino acids. Secondary structure[ edit ] The hydrogen in the amino group NH2 and the oxygen in the carboxyl group COOH of each amino acid can bond with each other by means of hydrogen bond, this means that the amino acids in the same chain can interact with each other. As a result, the protein chain can fold up on itself, and it can fold up in two ways, resulting in two secondary structures: If the direction alternates between every fold, it forms an anti-parallel sheet; if it remains the same direction, it forms a parallel sheet.
Tertiary structure[ edit ] As a consequence of the folding-up of the 2D linear chain in the secondary structure, the protein can fold up further and in doing so gains a three-dimensional structure. This is its tertiary structure.