Ribonuclease, the enzyme that hydrolyzes ribonucléic acid
Introduction
Within our body, there are hundreds of chemical reactions necessary for life all the time, occurring simultaneously that must happen in a reasonable time scale. It is said that carbohydrates or sugars have many calories, that is, they provide us with high amounts of energy. The human body, in order to extract the energy from sugars in a useful time, in a short time, uses catalysts that accelerate that same reaction and cause it to occur thousands of times faster. These catalysts are called enzymes.
A relatively simple cell, such as Escherichia coli bacteria, is capable of producing more than 4,000 different proteins. A cell is a group of thousands of molecules in constant movement and organized in specific structures, these include proteins, nucleic acids, polysaccharides, lipids, metabolites and small ions, such as sodium, potassium and magnesium.
Our cells produce many enzymes, since there are hundreds of chemical transformations that must occur in a short period of time. One of the fastest enzymes that exist in nature is called carbonic anhydrase, which catalyzes the carbon dioxide reaction with water to form carbonic acid. Although it seems fast, this speed makes the survival of the cells be compromised, since the time of the reaction is too slow to maintain a stable ph that allows cellular functions to be carried out properly.
The simplest way is to stipulate how fast the reaction occurs in terms of how many substrate molecules are transformed per second, as in the example of carbonic anhydrase. When we compare how quickly a catalyzed reaction is going on the absence of the enzyme, we can appreciate the efficiency of enzymes as reactions accelerators. Another way is to consider the time necessary for the reaction to occur.
This reaction is closely transcendental, since it is part of the production chain of the monophosphate uridine core, one of the 4 components of ribonucleic acid
How do enzymes do this work?
To better understand how a protein folds or folds in space, computational tools have been developed that allow simulating this phenomenon.According to the story, in Egypt more than two thousand years ago it was known that when storing milk in viscera or dry stomachs of animal.
By suffering from this hydrolysis, protein like other milk components become insoluble and precipitate, which forms the rennet. This process was known so well and was so reproducible, safe and accepted by consumers, that at the end of the 19th century, Christian Hansen, a Danish pharmacist, founded the first biotechnological company to sell a product called Renin. Hansen continues to do business today, although now he also sells other enzymes produced from microbial crops of fungi and bacteria through the use of modern biotechnological tools. Although it was thought that these only worked due to the presence of living cells, that they were conferred by a "vital force" that made them active. This discovery is attributed to Eduard Buchner, a German scientist who was awarded the Nobel Prize in Chemistry in 1907.
In 1913 Michaelis and Mennn was published, in which a model to explain the kinetic behavior of enzymes is proposed. So, at the beginning of the last century, everything was ready to thoroughly understand the functioning of enzymes. (Ramírez, 2016)
Developing
There is great interest in identifying antimicrobial proteins or peptides that are therapeutic tools that dodge the establishment or consent to control different infections. The ribonucleas (rnasas), belonging to the Ribonuclease A family, of the nuclease class or hydrolase enzyme.
They are enzymes that collaborate in several physiological processes, which occur from the optional processing of the RNA to angiogenesis. These enzymes are expressed by different tissues and manifest unstable specificities against different RNA substrates. The therapeutic potential of the RNASAS is suggested in oncogenic processes;Additionally, it has been optional that they have direct antiviral activity and the potential to activate innate immune system cells persuading their maturation and the production of proinflammatory cytokines.
They are expressed by different tissues and manifest variable characteristics against different RNA substrates. The therapeutic potential of the RNASAS is suggested in oncogenic succession;Additionally, it was described that they have direct antiviral activity and the potential to enlive.
RNASAS are protein with enzymatic activity that are present in bacteria, fungi, upper plants and mammals, which participate in different physiological processes, such as: cell death, replication of the DNA, transcription, processing and editing of the RNA, host defense and control of the control of theTumor growth.
“The ribonucleas (RN) are divided into three great families: the RNASA A, the T1 family and the T2 family. Ribonuclease A superfamily is constituted by mammalian and other vertebrates such as birds, reptiles and amphibians. This group of protein has high genes of gene duplication and loss of genes of what has been a variable number of genes in different species. In the human being, the genes that encode them are located on the long arm of chromosome 14.”(Alonso, 2009)
It should be noted that Sierakowska and Shugar, in 1977 they defined human rnasas in a classification in which it was divided into 2 categories: secret and not secret rnals;Then, in 1981 the Weickmann team was the one who replaced the name of "secreted" with that of pancreatic and sorrentine and Libonati type rnases, 1994, they began using the term non -pancreatic in substitution of "not secrets". Pancreatic type rnases include ribonucleases located in the pancreas as well as in other body fluids that have certain catalytic and structural properties similar to human pancreatic rns and a being of a being. The non -pancreatic type term was used for rnasas that have certain catalytic properties and that have a sequence similar to neurotoxin derived from eosinophil (EDN) or to the K2 rnasa of bovine kidney. Other members of the RNASA A superfamily, such as RNASA 4 and the PL3 RNASA of pig liver that are part of a third family of rnases known as pancreatic/non -pancreatic type, which in their structure have characteristics that are more similarto pancreatic type rnases, but have in common some catalyzer properties that both types of ribonucleases have.
The biological function of this enzyme is to hydrolyze as such ribonucleic acid, and this reaction is carried out through 2 steps: the first step consists in the formation of a 2 ’nucleotide, 3 cyclic;And in the second step the hydrolyzing comes, which is a slow process that leads to the formation of a nucleotide.
It is known that ribonuclease to the bovine pancreas has been the most studied protein of the twentieth century;Well, through all the investigations carried out, it has been possible to know that RNASA A is a container of all existing natural amino acids except for tryptophan. This enzyme (protein) is basic, because the basic ones predominate on acidic, which make it basic into an isoelectric point of 9,3.
RNASA A has four native disulfide links in positions 26-84, 40-95, 58-110 and 65-72, and those, 40-95 and 58-110 are the ones that contribute the most to the proteinFind stable. Its three-dimensional structure has been determined by X-rays and RMN, and consists of 3 α-Helic in waste 3-13, 61-63, 72-74, 79-87, 96-111 and 116 and 124 and 124. [Image:]
The RNASA A is catalyst of the breaking of the link between phosphorus and 5 ’oxygen of the RNA that has a simple chain, thus leaving the active site of the enzyme is formed by histidines 12 and 119, and Lysine 41 41.
Lysine 41stabilizes the negative load that oxygen has that is attached to the phosphoryl group, by transferring a proton, thus contributing to the catalytic action of the enzyme. RNASA A accelerates in a magnitude of 12 transfosphahilation, thus making the life of the RNA like thus lasting microseconds. So far it is known that ribonuclease to achieve this increase through four catalytic strategies;which are a correct online positioning of the substrate, the neutralization of the negative load of the phosphate oxygen does not present in the reaction, the activation of the 2 ’nucleophile hydroxyl and the improvement of 5’ oxygen as a outgoing group.
Last studies have resulted that it is recombinant pancreatic ribonuclease who is responsible for inhibiting the replication of HIV-1 in a primary crop of activated T lymphocytes.
The mechanism of action is the terminal region of the amino group, since it is important during the clivative of the RNA, since it is responsible for exhibiting the catalytic activity, in addition, this enzyme is twice as an active that the rnase to bovine, by poly-adenin (by poly-adenin (by poly-adenin (by poly-adenin (by poly-adenin (by poly-adenin (by poly-adenin (Poli-a) due to the presence of the Aspartic Residue-83 (ASP-83). Its catalytic action is enhanced in high concentrations of sodium chloride (NaCl) and shows optimal activity in a pH of 8.0. It is necessary to mention that this rnase is not cytotoxic because the neutralizing action of the inhibitor protein of ribonuclease (IR), which is cytotoxic glycoprotein of 50 kda, seeks to preserve the preservation of the integrity of the RNA that is located in the cell.
GENERAL
A general panel would be that ribonucleases are a very resistant type of enzyme and of great catalytic activity:
- They have great heat resistance, being constant with a slight heating.
- They are active in a great pH range
conclusion
Ribonuclease is one of the most important enzymes as an operation and presence in the body, since it has been possible to understand the functionality they imply;Since, being enzymes, they act as catalysts, and the type they are, take part in an important system without which important procedures could not be carried out, because when talking about these enzymes, there is specifically talking about acid -related functionsribonucleic and hydrolysis, by which ribonucleic acid
These enzymes are very important and are expressed in the different tissues and the exhibition of variable characteristics against different RNA substrates. They are important for some organs such as pancreas.
This research is necessarily needed to fulfill processes and functions because without these functions they would not fulfill their important function for body maintenance.
To conclude and end this research, it must be emphasized that these enzymes are very necessary for processes, such as the other body mechanisms. Everything that is in the body is indispensable for the proper functioning of the complete system as it is, the human body. For that reason, it is that biochemistry studies a lot what these enzymes are.
Bibliography
- López Alonso, J. P. (2009). Modulation of the structure and function of RNASA A and alleged prebiotic ribonucleases. AUTONOMOUS UNIVERSITY OF MADRID. 2009.
- Neira j. Structure and dynamics of ribqnuclease to by two -dimensional nuclear magnetic resonance. COMPLUTENSE UNIVERSITY OF MADRID;1993.
- Joaquín Ramírez Ramírez, M. (2016). Enzymes: What are they and how do they work?. Retrieved 10 SEPTEMBER 2019, from http: // www.magazine.UNAM.mx/vol.15/num 12/art 91/
- Goeddel et al. "Expression in Escherichia Coli of Chemically Synthesized Genes for Human Insulin". Proceedings of the National Academy of Science USA, 1979, 76, 106–110
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