Disease Symptoms

Metabolic diseases are caused by specific enzyme defects in which the enzyme is not expressed or dysfunctional caused due to mutation or inactivation of the sequence after the conversion. Some of these diseases can be treated with a controlled regime. For example, phenylketonuria caused by lack of phenylalanine hydroxylase requires a phenylalanine-free diet. Replacement therapy is often necessary to be necessary for the conduct of a replacement enzyme to specific tissues or organs.

Other known as  inborn errors of metabolism  are Pompe disease or glycogen storage disease type II, in which the poor-1.4-glucosidase causes an excessive accumulation of glycogen in liver and muscle lysosomes, Alkaptonuria (deficit homogentisate 1, 2-dioxygenase) Hemophilia B ( factor IX), galactosemia (transferase UDPG-hexose-1-phosphate), Gaucher’s disease (2-glucocerebrosidase), von Gierke disease (glucose-6-phosphatase), Pentosuria (xylulose reductase), Niemann-Pick Disease (Sphingomyelin Phosphodiesterase ) and Lesch-Nyhan syndrome, in which phosphoribose the absence of hypoxanthine-guanine-nucleotide transferase cause a change in brain cells and leads to severe neurological disease.

Cancer Therapy: L-asparaginase is used as a cancer drug. Some types of tumor cells lack asparagine synthetase activity and the need for this amino acid as an essential nutrient, in contrast to normal cells. Asparaginase selectively kills tumor cells by lowering blood levels of asparagine. It was suggested that L-aspartate may be toxic metabolite than to tumor cells. 15 Asparaginase Acute lymphocytic leukemia is a relative success, some studies report a complete remission in 60% of patients.16 patients prolonged treatment with the enzyme often develop resistance because of their high concentration of neutralizing antibodies.
However, the therapeutic index of asparaginase compares very favorably with other antileukemic drugs.

It was speculated that some types of cancer cells, other possibilities, including lack of amino acid synthesis and thus the amino acid requirements are masked by the presence of these amino acids in the diet. Enzyme, the amino acids necessary to reduce lead to the slaughter of these cells. Glutamine, cysteine and arginine were examined for enzyme therapy possible exhaustion. Besides E. coli and Erwinia asparaginase, glutaminase-asparaginase from two species (PGA and AGA) may be appropriate therapeutic enzymes, because both have an anti-tumor activity in laboratory animals models.17 sometimes allergic reactions and neurotoxicity were the more serious side effects .
The anti-cancer effect of bovine ribonuclease has been reported in patients with chronic myeloid leukemia. But the limited information available from clinical studies. dimeric ribonuclease shows selective toxicity and animal tumors may be a promising candidate as a therapeutic enzyme.

Bacteriolytic, antiviral and anti-inflammatory enzymes: lysozyme as an antibacterial agent in body fluids and cavities in direct contact with the outside world. It is in a dosage form of tablets, ointments, powders, and tea, and as antibacterial, antiviral and anti-inflammatory. Commercial preparations hen egg white lysozyme, which is easily isolated and purified proteins in large projects. This enzyme is not toxic and is only weakly antigenic and can be administered internally in large doses, without significant side effects. The chitinase-lysozyme, muramidase and transglycosidase activity and acts on bacteria in many ways. Proteoglycan layer of the cell wall is the natural substrate of this enzyme.

Lysozyme has antiviral activity against herpes simplex and herpes zoster different I and type II in humans, and some tumor viruses in animals. Lysozyme stimulates phagocytosis and promotes healing and regression of degenerative and necrotic processes.20 zoster lysozyme is administered by intramuscular or parenteral viral hepatitis and herpes, and ointments for the treatment of herpes keratitis, burns and wounds and gynecological infections.

An imbalance between coagulation and fibrinolysis, leading to excessive fibrin deposits can be treated by reducing the power of the blood clotting or increased fibrinolytic activity. Several aspects of the improvement of fibrinolysis are still in development. Thearpy thrombolytic used in the initial treatment of deep vein thrombosis and pulmonary embolism.
Streptokinase and urokinase have been extensively used in the treatment of venous thromboembolism. They are more powerful than the freedom of movement, plasmin is rapidly inactivated by alpha 2-antiplasmin movement 30, 29 Randomized studies have shown that intravenous tissue plasminogen activator more effective than streptokinase in the treatment of coronary occlusion in acute myocardial infarction 31, 32. Commercial recombinant tissue plasminogen activator for the treatment of acute myocardial infarction is produced mainly from Chinese hamster ovary (CHO).

Chemonucleolysis: chymopapain, oxidation of cysteine proteinase-sensitive Carica papaya has been proposed for the treatment of lumbar disc. Intradiscal injection results chymopapin resolution mucopolysaccharide – complex proteins extruded nucleus pulposus, the gelatinous mass center of the absorption in the disc, the pain of a pinched nerve. Follow-up studies show that large-scale chemotherapy as effective as discectomy surgical procedure with a success rate of 76-80% in both groups 33, 34, 35.
Pancreatic enzymes: digestion of food is facilitated by the enzyme pancreatic trypsin, chymotrypsin and elastase, carboxypeptidase A and B, the phospholipase A – 2 and lipase and amylase. The main component of lipids in foods long-chain triglycerides, the fatty acids and sn-two monoacylglycerol is hydrolyzed. Both products are readily absorbed in the intestine. This hydrolysis is catalyzed sequentially by gastric lipase by the main cells of the stomach and pancreas colipase-dependent secreted 37th

Pancreatic lipase, protease and amylase are as replacement therapy in pancreatic insufficiency, where production of the enzyme is reduced below 10% required. Pancreatin from mammals are used in commercial formulations for replacement therapy, 38, 40. pharmaceutical formulations, there are significant differences in enzyme activity and content of bile salts. Cellulose is sometimes added as an adjuvant enzyme. Since the degree of pancreatic dysfunction varies greatly among patients, the individualization of therapy is to determine the optimal dose of the enzyme, the type of formulation, time of administration in relation to meals and frequency of administration.

Conclusion and Outlook: The elucidation of the molecular biochemical processes associated with the disease of the nature and specific area of key enzymes or inhibitors necessary to define normal physiological conditions recover. The enzymes are attractive drug candidates because of their specificity of reaction and catalytic efficiency. However, the nature of the protein demands of certain limits to their use in therapy. Institution for certain enzymes and proteins requires the parenteral administration of non-human origin are often allergenic or immunogenic. There was considerable sophistication achieved in the isolation procedures to reduce or eliminate toxic pollutants, and to change the development of chemical, and specific ways to extend targeted offers new life and improve the bioavailability of the enzyme. The most promising results are certainly expected from the field of genetic engineering and site-directed mutagenesis. mutant enzymes with altered or enhanced specificity, greater stability and reduced immunogenicity is at an affordable price.