Enzymes Bio

What are the enzymes?

Enzymes are the central drivers of biochemical metabolic processes in organisms — without enzymes, there is no life. From digestion to the energy metabolism of the cells, from information transfer to the copying of genetic information, all these processes are controlled by enzymes.

The special thing: Enzymes work very specifically — a single enzyme usually catalyses only one single reaction and it only converts a very specific molecule, the so-called substrate. This makes enzymes special biological tools. There is a huge variety of enzymes with different abilities. For almost every biochemical reaction, nature’s toolbox contains its own biocatalysts. Building, degrading or rebuilding molecules, these are the core functions of enzymes. Their names end characteristically with “-ase”, i.e. cellulase, lipase or protease.

Enzymes can be divided into six main groups, depending on the type of chemical reaction they catalyze. These classes of enzymes (and some of their subgroups) are:

• Oxidoreductases: They catalyse reactions in which electrons are transferred (redox reactions); e.g. dehydrogenase, oxidases, reductases, catalase
• Transferases: They catalyze reactions in which entire functional groups (such as phosphate groups) are transferred from one molecule to another; e.g. transaminases, kinases, DNA polymerases
• Hydrolases: They catalyse reactions in which a chemical bond is either formed when water escapes or is split when water is added; e.g. peptidases, phosphates, proteases
• Lyases: They catalyze reactions in which chemical bonds are split or formed without energy consumption; e.g. aldolase
• Isomerases: They are responsible for rearranging the binding relationships within a molecule; e.g. racemase, topoisomerase
• Ligases (synthetases): They catalyse reactions in which two molecules are joined together with energy consumption; e.g. carboxylase

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We are going to learn about enzyme, region and studious specificity. We are going to focus on understanding what do we mean by enzymes, specificity, the various types of enzymes, specificity, and what is the difference between enzymes, studio specificity and enzyme Stelio selectivity. This lecture will be broadly divided into three sections. We will first study what is enzyme specificity in the next section. We will look at the various types of enzymes specificity such as bond, group substrate, optical geometrical and cofactors specificity. Lastly, we are also going to see how Stelio specificity differs from studio selectivity into this lecture.

We even focus on understanding what is enzyme specificity, the various types of enzyme specificity, and what is the difference between enzyme, stevia, specificity and enzyme. Stelio selectivity. This slide shows the concept map that will be followed in this lecture. We will follow study. What do we mean by enzyme specificity? In the next section, we will look at the various types of in them specificity, namely born specificity, group specificity, substrate specificity, optical specificity, geometrical specificity and cofactors specificity. Lastly, we will see how two similar domes, studio specificity and studio selectivity differ in enzyme Lalaji.

Enzyme specificity. What do we mean by this tone in them specificity?

Means the ability of an enzyme to select a particular specific substrate from a group of similar molecules to act upon. This is a unique property of the enzyme. Enzymes can show different degrees of specificity, ranging from high to low towards its particular substrate. Types of enzyme specificity, enzyme specificity is generally of six distinct types. These are born specificity, group specificity, substrate, optical geometrical and cofactors specificity. Now even look at each of these specificity types in Didi’s born specificity enzymes showing this specificity are specific for substrates which have similar bonds or similar structure. The enzyme shows specificity to only certain types of bonds. For example, peptide bonds, glycol, Siddig Bonds, EST. bonds, etc.. For instance, I for Miley’s enzyme hydrolyzed is the alpha one for linkage in the glycol. Acidic bonds of carbohydrates like Baz’s hydrolyzed the eston linkages between a glycerol and a fatty acid and protein ease’s hydrolyzed the peptide bonds that are formed between amino acids. The Fiegel here shows how proteins enzymes are specific to peptide bonds which exist between amino acids bonds. Specificity is also known by another term, which is called relative specificity. Good specificity in this type of specificity. The enzyme is not only specific to a bond, but also to the groups which are surrounding the bonds. For example, in vein, Pepsi Hydrolyzed is centrally located peptide bonds in which the amino group belongs, particularly to an aromatic amino acid such as she Knile Elamine, tryptophan and tyrosine. These examples can be seen in the figure three, which is shown below. Gypsy is another protein hydrolyzed enzyme. This enzyme hydrolyzed is a peptide bond in which the amino group is contributed by basic amino acids such as lysine. His daddy and our geneen guimard gypsy hydrolyzed is peptide bonds in which the GA boxing group is contributed by an aromatic amino acid such as Phenylalanine Dialyse and Tryptophan. Another name for group specificity is called moderate specificity.

Substrate specificity in this type of specificity.

The enzyme shows specificity towards only one substrate and catalyzes only one reaction. For example, the enzyme black days can get delays. The hydrolysis of only the beta one for viscose ITIC born of lactose. To give glucose and galactose. Similarly, Yurick is another enzyme which acts only on uric acid and my D which acts only on maltose. Now we will look at what is meant by steel chemical specificity. This refers to the specificity of the enzyme when it acts only on a particular steady or optical isover off the given substrate. This is also known as optical specificity and is one of the highest forms of specificity which can be displayed by enzymes. Let us see an example. To understand this in detail, as shown in the figure below, we see that the N and D amino acid oxidase is. Do you chemical specificity and act only on respective L and D amino acids respectively. The L alanine oxidase will not work on D alanine as a substrate and the D Elamine oxidase will not work on a alanine as a substrate.

Geometrical specificity.

As the name suggests, geometrical specificity has something to do with the geometry of the molecule. This type of specificity is displayed by enzyme, which is able to act on different substrates that are similar in their molecule and geometry, for example, alcohol dehydrogenase is sure geometrical specificity during the oxidation of methanol and ethanol to corresponding aldehydes. This is because both ethanol and methanol have similar molecules. Geometry, however, geometrical specificity is not very high. The last type of specificity is all factors specificity, which means that an enzyme can function only in the presence of certain cofactors.

We have now reached midway into this lecture. So far we looked at what is enzyme specificity and what are their various types in detail in the next section. We will study what is the difference between studio specificity and studio selectivity. These two terms may sound similar, but there is a subtle difference between them. Let us see how these two are different.

Now we will look at a comparative understanding of studio specificity versus studio selectivity, as we saw earlier, an enzyme. Can we stick to a specific when it acts only on a particular steady or optical isomer of the given substrate? In this case, only once did you isometric product will be formed. If we see the diagram below, there are two substrates with R and F configuration. The enzyme, which is supposed to act on the substrate, is not able to recognize the R isomer, but that act on the S isomer of the substrate to produce the product D. Now why does this happen? This is because the enzyme binding site is SkyTel and due to the guy reality, the delivery of reagents therefore remains restricted to only one side of the functional group of the reactant. Let us look at a few examples to understand, Steve, your specificity in detail, Malic acid is the cyst isomer of butane doig acid, whereas Formanek acid is the trotz. I saw more of the same malate and fulminate and ionized forms of these acids in the reaction shown here will see the addition of water molecule to Malate and fulminate catalyzed by the enzyme families. We see that the format enzyme is studio specific and is able to catalyze only the addition of water molecule to Fumi rate, which is the drives I soma, but not to Malate, which is the CIS isomer. In another example below, we see the enzymes that catalyze calculation off is glycerol phosphate will not be able to violate the ah, use all phosphate.

Now even see what is DVOA selectivity and how it differs from Steve specificity in biological systems. The organic reactions that occur are catalyzed by enzymes. Enzyme catalyzed reactions are therefore almost always stadio selective in nature by a studio. Selective reaction. We mean that only once did you isomer is formed as a product preferentially over other possible stevia isomers which could have also been formed. Let us look at the example below. The diagram shows the formation of product B from A reactant E catalyzed by an enzyme y. There are two possibilities of the product formation. That is the R and the S isomers of the product. The enzyme briefer’s will lead the formation of the isomer of Product B over the S Isomer. This is the studio selectivity of the enzyme such that only the R isomer of the product B is preferentially formed. Let us consider the addition of water to double bonds during the oxidation of fatty acids. We see that there are two possible products that can form the R and the S Enantiomer. But in this reaction, due to the studio selectivity of the enzyme, only the S enantiomer is preferably formed.

We have now come to the end of this lecture, in this lecture. We have understood the concepts of enzyme, region and enzymes, studio specificity. We see that enzymes can show different degrees of specificity, ranging from high to low towards its substrate. Also, they can show different types of specificity later. We also looked at how Stelio specificity and studio selectivity are different from each other and also understood these differences through some examples. Let us now do a short summary of what we have studied in this lecture. The ability of an enzyme to select a particular specific substrate from a group of similar molecules to act upon is called specificity. Enzyme specificity is generally of six distinct types. These are born specificity, glueck, specificity, substrate specificity, optical specificity, geometrical specificity and cofactors, specificity and enzyme and mysterious specific when it acts only on a particular starick or optical isomer of the given substrate.