ENZYMES/CO-ENZYMES

Deficiency of Diastase

• PMS
• Fatigue
• Sprue
• Hypoglycemia
• Depression
• Mood Swings
• Allergies
• Inflammation
• Hot Flashes
• Cold hands and feet
• Neck and shoulder aches
• Breaking out of the skin - rash

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Saccharase

Saccharase also called invertase, catalyses the hydrolysis of sucrose to glucose and fructose. The studied enzyme is also used in processes leading to mixtures of glucose and fructose (invert sugars) enabling the successive production of fructose-containing preparations. The development of new techniques of immobilisation of biocatalysts is highly connected with the progress of biotechnological processes. Although saccharase is generally present also in plants, this source was not used previously.

Saccharase is a yeast-derived enzyme. Saccharase can be applied for any inversion of sucrose especially liquefied cherry centers, creams, mints, truffles, marshmallow, invert syrup and other fondants. Invertase is used to improve shelf life of confections.

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Pectase

Pectase is an enzyme in the pith (albedo) of citrus fruits which removes the methoxyl groups from pectin to form water-insoluble pectic acid. The intermediate compounds, with varying numbers of methoxyl groups are pectinic acids. Also known as pectin esterase, pectin methyl esterase, and pectin methoxylase. It is use in the treatment of certain foodstuffs.

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Phosphatase

Phosphatase is an enzyme that catalyze the hydrolysis of esters of phosphoric acid and are important in the absorption and metabolism of carbohydrates, nucleotides, and phospholipids and in the calcification of bone.

It removes a phosphate group from its substrate by hydrolysing phosphoric acid monoesters into a phosphate ion and a molecule with a free hydroxyl group (see dephosphorylation). This action is directly opposite to that of phosphorylases and kinases, which attach phosphate groups to their substrates by using energetic molecules like ATP. A common phosphatase in many organisms is alkaline phosphatase.

Physiological Relevance

Phosphatases act in opposition to kinases/phosphorylases, which add phosphate groups to proteins. The addition of a phosphate group may activate or de-activate an enzyme (e.g., Kinase signalling pathways[7] ) or enable a protein-protein interaction to occur (e.g., SH3 domains [8]); therefore phosphatases are integral to many signal transduction pathways. It should be noted that phosphate addition and removal do not necessarily correspond to enzyme activation or inhibition, and that several enzymes have separate phosphorylation sites for activating or inhibiting functional regulation. CDK, for example, can be either activated or deactivated depending on the specific amino acid residue being phosphorylated. Phosphates are important in signal transduction because they regulate the proteins to which they are attached. To reverse the regulatory effect, the phosphate is removed. This occurs on its own by hydrolysis, or is mediated by protein phosphatases.

Protein phosphorylation plays a crucial role in biological functions and controls nearly every cellular process, including metabolism, gene transcription and translation, cell-cycle progression, cytoskeletal rearrangement, protein-protein interactions, protein stability, cell movement, and apoptosis. These processes depend on the highly regulated and opposing actions of PKs and PPs, through changes in the phosphorylation of key proteins. Histone phosphorylation, along with methylation, ubiquitination, sumoylation and acetylation, also regulates access to DNA through chromatin reorganisation.

One of the major switches for neuronal activity is the activation of PKs and PPs by elevated intracellular calcium. The degree of activation of the various isoforms of PKs and PPs is controlled by their individual sensitivities to calcium. Furthermore, a wide range of specific inhibitors and targeting partners such as scaffolding, anchoring, and adaptor proteins also contribute to the control of PKs and PPs and recruit them into signalling complexes in neuronal cells. Such signalling complexes typically act to bring PKs and PPs in close proximity with target substrates and signalling molecules as well as enhance their selectivity by restricting accessibility to these substrate proteins. Phosphorylation events, therefore, are controlled not only by the balanced activity of PKs and PPs but also by their restricted localisation. Regulatory subunits and domains serve to restrict specific proteins to particular subcellular compartments and to modulate protein specificity. These regulators are essential for maintaining the coordinated action of signalling cascades, which in neuronal cells include short-term (synaptic) and long-term (nuclear) signalling. These functions are, in part, controlled by allosteric modification by secondary messengers and reversible protein phosphorylation.

It is thought that around 30% of known PPs are present in all tissues, with the rest showing some level of tissue restriction. While protein phosphorylation is a cell-wide regulatory mechanism, recent quantitative proteomics studies have shown that phosphorylation preferentially targets nuclear proteins. Many PPs that regulate nuclear events, are often enriched in or exclusively present in the nucleus. In neuronal cells, PPs are present in multiple cellular compartments and play a critical role at both pre- and post-synapses, in the cytoplasm and in the nucleus where they regulate gene expression.

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Catalase

Catalase is a common enzyme found in nearly all living organisms which are exposed to oxygen, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover numbers of all enzymes; one molecule of catalase can convert millions of molecules of hydrogen peroxide to water and oxygen per second.

Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four porphyrin heme (iron) groups that allow the enzyme to react with the hydrogen peroxide. The optimum pH for human catalase is approximately 7, and has a fairly broad maximum (the rate of reaction does not change appreciably at pHs between 6.8 and 7.5). The pH optimum for other catalases varies between 4 and 11 depending on the species. The optimum temperature also varies by species.

Catalase works closely with superoxide dismutase to prevent free radical damage to the body. SOD converts the dangerous superoxide radical to hydrogen peroxide, which catalase converts to harmless water and oxygen. Catalases are some of the most efficient enzymes found in cells; each catalase molecule can convert millions of hydrogen peroxide molecules every second. cHydrogen peroxide is a naturally occurring but destructive waste product of all oxygen-dependent organisms. It is produced in the human body when fatty acids are converted to energy, and when white blood cells attack and kill bacteria. Catalase, which is located in the cell’s peroxisome, prevents this naturally occurring hydrogen peroxide from harming the cell during these processes. It also helps prevent the conversion of hydrogen peroxide to hydroxyl radicals, potentially dangerous molecules that can attack and even mutate DNA.

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Disphorase

The diaphorases are a ubiquitous class of flavin-bound enzymes that catalyze the reduction of various dyes which act as hydrogen acceptors from the reduced form of di- and tri- phosphopyridine nucleotides, i.e., NADH, NADPH. The first such enzyme to be purified was that from heart muscle (Straub 1939). Almost twenty years later heart diaphorase was shown to be identical to lipoyl dehydrogenase (Massey 1958, 1963). Other diaphorases have been described and purified from various bacteria, plants and mammalian organs. Diaphorase activity of a partially purified extract of Clostridium kluyveri cells, originally described as a source of NADH and NADPH oxidase (Ciotti and Kaplan 1957), was observed in this laboratory and its use applied to the coupled, colorimetric determinations of dehydrogenases and ethanol. (Teller 1958). These methods, based on the decolorization of 2,6-dichlorophenolindophenol were improved by the substitution of a tetrazolium dye which becomes chromogenic on reduction. (Brower and Woodbridge 1970; Nachlas et al. 1960).

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Cozymase

Cozymase is one of the essential components of the complex enzyme mixture which effects alcoholic fermentation in the absence of living cells. The separation of the mixture into zymase and cozymase was first accomplished by Harden and Young by means of ultrafiltration through a gelatin-impregnated Chamberland filter candle. The residue and filtrate as thus prepared possessed, separately, no fermentative action, but when mixed were found to produce a rapid fermentation. The active constituent of the residue was named zymase, while that constituent of the filtrate responsible for the reactivation of the residue was named cozymase

Cozymase is inactivated by vegetable as well as animal tissues it was considered to be of interest to study the mechanism of inactivation. cozymase was inactivated by dialysed muscle extract, but that the latter was active in glycolysis only when cozymase and adenylic acid were added. They concluded that no adenylic acid was formed and suggested that the inactivation of cozymase might possibly be due to dephosphorylation. The present investigation shows that cozymase is rather slowly dephosphorylated by nucleotidase which dephosphorylates adenylic acid and inosinic acid much more rapidly (the former more easily than the latter). On the other hand, dihydro-cozymase is dephosphorylated about twice as fast as cozymase. In animal tissues cozymase is present in the oxidized as well as in the reduced form, and the present observation might suggest some biological indications.

The importance of cozymase as a fundamental constituent of certain respiratory processes in the living cell is now well established. It is known that cozymase is necessary for the activity in animal tissues of specific dehydrogenases oxidizing alcohol, lactate, malate, triosephosphate, etc. Its mode of action is reasonably clear. After combination with a dehydrogenase, it is reduced by a substrate (for example, lactate) with the formation of reduced cozymase and the oxidized product of the substrate (for example, pyruvate). The reduced cozymase is oxidized to its original form by other enzyme systems in the cell, transfer of hydrogen from the substrate to the final oxidizing agent being thus accomplished. Cozymase acts as a catalyst in the transfer of hydrogen in the cell, and in the intact tissue a dynamic equilibrium between reduced and oxidized cozymase is presumably always maintained.

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Cytochrome Systems

Cytochrome Systems is a Respiratory Capacity, the volume of gas that can be expelled from the lungs from a position of full inspiration, with no limit to the duration of expiration, it is equal to the inspiratory capacity plus the expiratory reserve volume. Cytochrome System of aerobically grown cells of Pseudomonas stutzeri (van Niel strain) has been studied. This bacterium contains cytochrome. Cytochrome is a protein responsible for part of the process of respiration by which food molecules are broken down in aerobic organisms.

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Lactic Dehydrogenase

Lactate dehydrogenase (LDH) is an enzyme present in a wide variety of organisms, including plants and animals. It is an enzyme that catalyzes the dehydrogenation of L-lactic acid to pyruvic acid. Abbreviated LDH.

Lactic acid dehydrogenase (LDH) helps produce energy. It is present in almost all of the tissues in the body and becomes elevated in response to cell damage. LDH levels are measured from a sample of blood taken from a vein. Normal LDH levels range from 100 units per liter (U/L) to 190 U/L.

Lactate dehydrogenase catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. It converts pyruvate, the final product of glycolysis to lactate when oxygen is absent or in short supply, and it performs the reverse reaction during the cori cycle in the liver. At high concentrations of lactate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased.

It also catalyzes the dehydrogenation of 2-Hydroxybutyrate, but it is a much poorer substrate than lactate. There is little to no activity with beta-hydroxybutyrate.

Lactate dehydrogenase help diagnose lung disease, lymphoma, anemia, and liver disease. They also help determine how well chemotherapy is working during treatment for lymphoma.

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Succinic Dehydrogenas

Succinate dehydrogenase or succinate-coenzyme Q reductase (SQR) or Complex II is an enzyme complex, bound to the inner mitochondrial membrane of mammalian and many bacterial cells. It is the only enzyme that participates in both the citric acid cycle and the electron transport chain.

Succinate dehydrogenase catalyzes the dehydrogenation of succinic acid to fumaric acid in the presence of a hydrogen acceptor. Also known as SDH.

There is a direct relationship between SDH activity and the oxygen capacity of muscle fibres. SDH occurs in higher concentrations in slow-twitch muscle fibres than in fast-twitch fibres. The muscles of endurance athletes have SDH activities up to four times those of untrained individuals.

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24 Oxidoreductases

Oxidoreductase is member of a group of enzymes involved in redox reactions. Oxidoreductases were formerly known as oxidases or dehyrdogenases.

Oxidoreductase catalyse electron transfer in oxidation-reduction reactions. Oxidoreductases are classified into several groups according to their respective donors or acceptors.

The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. Oxidoreductase enzymes play an important role in both aerobic and anaerobic metabolism. They can be found in glycolysis, TCA cycle, oxidative phosphorylation, and in amino acid metabolism. In glycolysis, the enzyme glyceraldehydes-3-phosphate dehydrogenase catalyzes the reduction of NAD+ to NADH. In order to maintain the re-dox state of the cell, this NADH must be re-oxidized to NAD+, which occurs in the oxidative phosphorylation pathway. Additional NADH molecules are generated in the TCA cycle. The product of glycolysis, pyruvate enters the TCA cycle in the form of acetyl-CoA. During anaerobic glycolysis, the oxidation of NADH occurs through the reduction of pyruvate to lactate. The lactate is then oxidized to pyruvate in muscle and liver cells, and the pyruvate is further oxidized in the TCA cycle. All twenty of the amino acids, except leucine and lysine, can be degraded to TCA cycle intermediates. This allows the carbon skeletons of the amino acids to be converted into oxaloacetate and subsequently into pyruvate. The gluconeogenic pathway can then utilize the pyruvate formed.

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Transferases

Transferase is an enzyme that catalyzes the transfer of a functional group. These are C, aldehydic or ketonic residues, acyl, glycosyl, alkyl, nitrogenous, phosphorus and sulfurcontaining groups.

Three ribonucleotidyl terminal transferase enzymes are disclosed which modify the 3'-termini of ribonucleic acid (RNA) molecules by the addition of ribonucleotide units using ribonucleoside triphosphates as substrates. These terminal transferase activities are distinguishable by the specific ribonucleotide (e.g. AMP, CMP, or UMP) transferred to the 3'-hydroxyl terminus of an RNA primer. Also provided is a method for the 3'-terminal modification of RNA molecules by these enzymes and sequencing of RNA from its 3'-termini. The methods provide a convenient and efficient procedure for 3'-terminal modification (homopolymer tailing) of RNA required for synthesis of complete complementary DNA (cDNA) copies or double-stranded DNA gene copies by retrovirus-associated reverse transcriptase. Using the enzymes of the invention, RNA can also be radiolabelled to very high levels for molecular hybridization.

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Hydrolases

Hydrolase is an enzyme that speeds up the hydrolysis of proteins, starch, fats, nucleic acids, and other complex biomolecules.

Hydrolases are classified as EC 3 (according to the EC number classification of enzymes). Hydrolases can be further classified into various subclasses based on the bonds they act upon, such as nucleases for the hydrolysis of nucleic acids, proteases for proteins, etc.

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Lyases

Lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure.

Lyases differ from other enzymes in that they only require one substrate for the reaction in one direction, but two substrates for the reverse reaction.

Lyases are enzymes that catatyze the cleavage of C-C, C-O, C-N bonds by other means than by hydrolysis or oxidation. These bonds are cleaved by the process of elimination and the resulting product is the formation of a double bond or a new ring. This class of enzymes differs from other enzymes in that two substrates are involved in one reaction direction, but only one substrate is involved in the other direction. To generate either a double bond or a new ring, the enzyme is acted upon the single substrate and a molecule is eliminated. Lyases can be seen in the reactions of the Citric Acid Cycle (Krebs cycle) and in glycolysis.

In glycolysis, the lyase called aldolase catalyzes the readily reversible splitting of fructose 1,6-bisphosphate (F-1,6-BP),into the products glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). This is an example of a lyase that helps to cleave carbon-carbon bonds. The reaction that takes place in the second stage of glycolysis.

Lyase also are enzymes that aid in breaking bonds, which often later result in the formation of a double bond or a cyclic structure by means of catalytic pathways. These types of reactions only calls for one molecule in the forward reaction, but needs two molecules for the reverse reaction.

Lyase Deficiency Disorder

Lyase deficiency, also referred to as HMG-CoA lyase deficiency, is rare inherited disorder in which the body can't process the amino acid leucine. Also, the disorder prevents the body from synthesizing ketones, which are used for energy during periods where the body is without food. The condition is inherited in an autosomal recessive pattern, meaning both copies of the gene in each cell have mutations. The parents of an individual with an autosomal recessive condition each carry one copy of the mutated gene, but they typically do not show signs and symptoms of the condition, but may be at risk of passing it onward to the next generation.

The symptoms of lyase deficiency usually appear within the first year of life. The condition causes episodes of vomiting, diarrhea, dehydration, lethargy, and weak muscular development. During a stint with the symptoms, blood sugar levels can become hypoglycemic, or very low, and a buildup of harmful compounds can cause the blood to become too acidic. If untreated, the disorder can lead to breathing problems, convulsions, coma, and even death. Infection, strenuous exercise, and other physical stresses can lead to bouts with the symptoms from lyase deficiency.

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Isomerases

Isomerase is an enzyme that catalyzes the structural rearrangement of isomers. Isomerase catalyzes reactions involving a structural rearrangement of a molecule. Alanine racemase, for example, catalyzes the conversion of L-alanine into its isomeric (mirror-image) form, D-alanine. Isomerase is one of a group of enzymes that catalyzes the conversion of one isomer into another.

The names of isomerases are formed as "substrate isomerase" (for example, enoyl CoA isomerase), or as "substrate type of isomerase" (for example, phosphoglucomutase).

Classification

Isomerases have their own EC classification of enzymes: EC 5. Isomerases can be further classified into six subclasses:

• EC 5.1 includes enzymes that catalyze racemization (racemases) and epimerization (epimerases)
• EC 5.2 includes enzymes that catalyze the isomerization of geometric isomers (cis-trans isomerases)
• EC 5.3 includes intramolecular oxidoreductases
• EC 5.4 includes intramolecular transferases (mutases)
• EC 5.5 includes intramolecular lyases
• EC 5.99 includes other isomerases (including topoisomerases)

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Pepsin

Pepsin is an enzyme that is released by the chief cells in the stomach and that degrades food proteins into peptides. Pepsin was discovered in 1836 by Theodor Schwann who also coined this enzyme's name from the Greek word pepsis, meaning digestion (peptein: to digest). It was the first animal enzyme to be discovered, and, in 1929, it became one of the first enzymes to be crystallized, by John H. Northrop. Pepsin is a digestive protease.

Pepsin is expressed as a pro-form zymogen, pepsinogen, whose primary structure has an additional 44 amino acids.

Pepsin, enzyme produced in the mucosal lining of the stomach that acts to degrade protein. Pepsin is one of three principal protein-degrading, or proteolytic, enzymes in the digestive system, the other two being chymotrypsin and trypsin. The three enzymes were among the first to be isolated in crystalline form. During the process of digestion, these enzymes, each of which is particularly effective in severing links between particular types of amino acids, collaborate to break down dietary proteins to their components, i.e., peptides and amino acids, which can be readily absorbed by the intestinal lining. In the laboratory studies pepsin is most efficient in cleaving bonds involving the aromatic amino acids, phenylalanine, tryptophan, and tyrosine.

Pepsin functions best in acidic environments and is often found in an acidic environment, particularly those with a pH of 1.5 to 2. Pepsin denatures if the pH is more than 5.0.

Pepsin is said to have an optimum temperature between 37°C and 42°C in humans.

Pepsin is potently inhibited by the peptide inhibitor pepstatin. Pepsin is used for digestion of proteins.

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Superoxide Dismutase

Superoxide Dismutase (SOD) An antioxidant enzyme which helps protect cells from free-radical damage.

The formal name of this enzyme is copper-zinc superoxide dismutase in order to distinguish it from other, unrelated, superoxide dismutases.

the main reason for having this enzyme is to get rid of dangerous free radical forms of oxygen that are produced in a number of cellular reactions; notably, membrane-associated electron transport and photosynthesis. (Superoxide dismutase is found in all species.)

Superoxide Dismutases are a class of enzymes that catalyze the dismutation of superoxide into oxygen and hydrogen peroxide. As such, they are an important antioxidant defense in nearly all cells exposed to oxygen. One of the exceedingly rare exceptions is Lactobacillus plantarum and related lactobacilli, which use a different mechanism.

Superoxide Dismutase is faster than it has any right to be. The maximum rate of an enzymatic reaction was thought to be limited to the rate of diffusion inside the cell. This makes sense since the substrate (superoxide anion) has to collide with the active site copper ion before a reaction can occur. But measurements of the actual enzymatic rate gave a result that was faster than theoretically possible given the diffusion rates inside the cell.

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Trypsin

Trypsin (EC 3.4.21.4) is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins.[2] Trypsin is produced in the pancreas as the inactive proenzyme trypsinogen. Trypsin predominantly cleaves peptide chains at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation and proteins that have been digested/treated with trypsin are said to have been trypsinized.

Trypsin is often referred to as a proteolytic enzyme, or proteinase. Trypsin is one of the three principal digestive proteinases, the other two being pepsin and chymotrypsin.

In the digestive process, trypsin acts with the other proteinases to break down dietary protein molecules to their component peptides and amino acids. Trypsin continues the process of digestion (begun in the stomach) in the small intestine where a slightly alkaline environment (about pH 8) promotes its maximal enzymatic activity.

Trypsin, produced in an inactive form by the pancreas, is remarkably similar in chemical composition and in structure to the other chief pancreatic proteinase, chymotrypsin. Both enzymes also appear to have similar mechanisms of action; residues of histidine and serine are found in the active sites of both. The chief difference between the two molecules seems to be in their specificity, that is, each is active only against the peptide bonds in protein molecules that have carboxyl groups donated by certain amino acids. For trypsin these amino acids are arginine and lysine, for chymotrypsin they are tyrosine, phenylalanine, tryptophan, methionine, and leucine.

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