DOCSLIB.ORG

CHAPTER 11 Mechanism of Enzyme Action

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
CHAPTER 11 Mechanism of Enzyme Action CHAPTER 11 Mechanism of Enzyme Action 1. General properties of enzymes 2. Activation energy and the reaction coordinate 3. Catalytic mechanism 4. Lysozyme 5. Serine proteases Enzyme act with great speed and precision Introduction 1. Enormous variety of chemical reactions within a cell 2. Mediated by Enzymes 3. Enzymology, the study of enzymes (coined 1878; Greek: en, in; zyme, yeast), fermentation: glucose -> ethanol 12 enzyme-catalyzed steps 4. James Summer, 1926, crystallized urease from jack bean, shown to be a protein 5. Other catalysts, i.e. ribozymes (peptide-bond formation; “RNA-world”), only for units 6. Proteins more versatile, 20 functional units Introduction Enzymes increase the rate of chemical reactions by lowering the free energy barrier that separates the reactants and products 1. General Properties of Enzymes Enzymes differ from ordinary chemical catalysts by: - Higher reaction rates, 106-1012 - Milder reaction conditions (temp, pH, …) - Greater reaction specificity (no side products) - Capacity for regulation Definition catalyst: catalyzes reaction but is not itself consumed during the process Table 11-1 A) Classification of Enzymes - naming: -ase, urease, alcohol dehydrogenase but no rules, - systematic: IUBMB: 6 Classes acc. to the nature of the chemical reaction that is catalyzed (http://expasy.org/enzyme/) B) Enzymes Act on Specific Substrates - Noncovalent forces through which substrates bind to enzymes: van der Waals, electrostatic, hydrogen bonding, hydrophobic intercations - Geometric Complementarity - Electronic Complementarity - Induced fit upon substrate binding - “lock-and-key” model (proposed by Emil Fischer) An Enzyme-Substrate complex Geometric and electrostatic complementarity Enzymes are Stereospecific - Enzymes are highly specific both in binding to chiral substrates and in catalyzing stereo-specific reactions - Enzymes are themselves are chiral, L-amino acids -> active centers = active site is asymmetric/ stereo selective Citrate is prochiral and is stereo- specifically transformed into isocitrate Stereospecificity in substrate binding Enzymes vary in geometric Specificity - Stereoselectivity, right hand into left glove - Geometric specificity is a more stringent requirement than stereoselectivity, old key into modern lock: i.e. alcohol dehydrogenase, oxidation of ethanol (CH3CH2OH) to acetaldehyde (CH3CHO) faster than methanol to formaldehyde or isopropanol to aceton even though they only differ by deletion or addition of one CH2 group ! Some enzymes are very permissive, chymotrypsin, can hydrolyze amide and ester bonds, exception rather than rule ! Some Enzymes Require Cofactors - Can act as enzymes *chemical teeth” to take over chemical reactions that cannot be performed by amino acid side chains… - Required in diet of organisms - for example metal ions, Cu2+, Fe3+, Zn2+ toxicity, Cd2+ and Hg2+ can replace Zn and inactivate the enzyme - organic molecules, coenzymes, can transiently associate with enzyme as cosubstrate, i.e., nicotinamide adenine dinucleotide (NAD+) Types of Cofactors in Enzymes The structure and reaction of NAD+ NAD+ is an obligatory cofactor in The alcohol dehydrogenase (ADH) reaction NADH dissociates from the enzyme to be re-oxidized in an independent reaction Prosthetic groups Permanently associated with enzyme, often by covalent bonds, example heme is bound to proteins called cytochromes Holoenzyme = enzyme+cofactor complex, active Apoenzyme, lacks cofactor, inactive Coenzymes must be regenerated In order to complete the catalytic cycle, the coenzyme must return to its original state i.e. by a different enzyme such as is the case with NADH 2) Activation Energy and the Reaction Coordinate Transition State Theory: developed in 1930s HA-HB + HC -> HA + HB-HC Transition state: HA--HB—HC Transition state = point of highest free energy = most unstable Reactants approach one another along a path of minimal free energy = reaction coordinate Transition state diagram/reaction coordinate diagram: Plot of free energy versus the reaction coordinate Transition State Diagram (Symetrical) Transition State Substrate Product Transition State Diagram (Asymetrical) Free energy of activation Free energy of reaction Activation Energy and the Reaction Coordinate The greater the free energy of activation, the slower the reaction rate If the free energy of the reaction, ∆G<0, then the reaction is spontaneous and releases energy (heat) Transition State Diagram For a Two-Step Reaction Rate-determining “bottleneck” Catalysts Reduce the free energy of activation, ∆G‡ Catalysts act by providing a reaction pathway with a transition state whose free energy is lower than that of the un- catalyzed reaction Effect of a catalyst on the transition state diagram of a reaction Catalysts Reduce the free energy of activation, ∆G‡ Reaction rate is proportional to e-∆G‡/RT ∆∆G‡ of 5.7kJ/mol (1/2 of one hydrogen bond) gives 10-fold rate enhancement ∆∆G‡ of 34kJ/mol (small fraction of a covalent bond) give 106-fold enhancement Note: the catalyst enhances rate of forward and that of the back reaction by the same magnitude, but ∆Greaction determines whether forward or back reaction is favored 3) Catalytic Mechanisms Enzymes lower the free energy of the transition state (∆G‡) by stabilizing the transition state Learn about enzymatic reactions mechanisms by examining the corresponding non-enzymatic reactions of model compounds Catalytic Mechanisms Curved arrow convention to trace electron pairs At all times, rules of chemical reasons apply to the system, i.e. never five bonds on C, or 2 on H etc. Types of Catalytic Mechanisms 1. Acid-base catalysis 2. Covalent catalysis 3. Metal ion catalysis 4. Proximity and orientation effects 5. Preferential binding of the transition state A) Acid-Base Catalysis occurs by Proton Transfer General acid catalysis: Proton transfer from an acid lowers the free energy of a reaction’s transition state Example, keto-enol tautomerization (a) Enhanced by proton donation (b) or proton abstraction (c) (general base catalyzed) Concerted Acid-Base Catalysis Asp, Glu, His, Cys, Tyr, Lys have pK’s in or near the physiological range The ability of enzymes to arrange several catalytic groups around their substrates makes concerted acid-base catalysis a common enzymatic mechanism Effects of pH on Enzyme Activity Most enzymes are active only within a narrow pH range of 5-9. Reaction rates exhibit bell-shaped curves in dependence of pH (reflects ionization state of important residues) pH optimum gives information about catalytically important residues, if 4/5 -> Glu, Asp; 6->His, 10->Lys pK of residues can vary depending on chemical environment +/- 2 pH Optimum of Fumarase RNase A is an acid-base catalyst Bovine pancreatic RNase A: Digestive enzyme secreted by pancreas into the small intestine 2’,3’ cyclic nucleotides isolated as intermediates pH-dependence indicates 2 important His, 12, 119 that act in a concerted manner as general acid and base catalysts to catalyze a two-step reaction X-ray structure of bovine pancreatic RNase S UpcA substrate in active site The RNase A mechanism B) Covalent Catalysis Usually Requires a Nucleophile Covalent Catalysis accelerates reaction rates through the transient formation of a catalyst-substrate covalent bond Usually, nucleophilic group on enzyme attacks an electrophilic group on the substrate = nucleophilic catalysis Example: decarboxylation of acetoacetate Decarboxylation of acetoacetate Three stages of Covalent Catalysis 1. Nucleophilic attack of enzyme on substrate 2. Withdrawal of electrons 3. Elimination of catalysts by reversion of step 1 (not shown above). Nucleophilicity of a substance is related to its basicity: Important aspect of covalent catalysis The more stable the covalent bond formed, the less easily it can be decomposed in the final step of a reaction Good covalent catalysis must be (i) highly nucleophile and (ii) form a good leaving group. These are imidazole and thiol groups, i.e. Lys, His and Cys, Asp, Ser, some coenzymes (thiamine pyrophosphate, pyridoxal phosphate) C) Metal Ion Cofactors Act as Catalysts 1/3 of known enzymes require metal ions for catalysis Metalloenzymes contain tightly bound metal ion (Fe2+, Fe3+, Cu2+, Mn2+, Co2+), Na+, K+, or Ca2+ play structural rather than catalytic roles Mg2+, Zn2+ may be either structural or catalytic Metal Ion Cofactors Act as Catalysts Metal ions participate in the catalytic process: 1. By binding to substrate to orient them properly for reaction 2. By mediating oxidation-reduction reactions through reversible changes in the metal ions oxidation state 3. By electrostatically stabilizing or shielding negative charges Often: Metal ion acts similar to a proton, or polarizes water to generate OH- The role of Zn2+ in carbonic anhydrase - + CO2 + H2O <-> HCO3 + H 2+ Zn polarizes water, which then attacks CO2 D) Catalysis can occur through proximity and orientation effects Enzymes are much more efficient catalysts than organic model compounds Due to proximity and orientation effects Reactants come together with proper spatial relationship Example: p-nitrophenylacetate intramolecular reaction is 24 times faster Inter- versus intramolecular reaction 24-times faster Catalysis can occur through proximity and orientation effects Enzymes are usually much bigger than their substrates By oriented binding and immobilization of the substrate, enzymes facilitate catalysis by four ways 1. bring substrates close to catalytic residues 2. Binding of substrate in proper orientation (up to 102-fold) 3. Stabilization
Load more

Recommended publications
  • Diapause in the Mosquito Culex Pipiens Evokes a Metabolic Switch from Blood Feeding to Sugar Gluttony
    Diapause in the mosquito Culex pipiens evokes a metabolic switch from blood feeding to sugar gluttony Rebecca M. Robich* and David L. Denlinger† Department of Entomology, Ohio State University, 318 West 12th Avenue, Columbus, OH 43210 Contributed by David L. Denlinger, September 12, 2005 A key characteristic of overwintering dormancy (diapause) in the Although the physiological and ecological aspects of blood and mosquito Culex pipiens is the switch in females from blood feeding sugar feeding in diapausing C. pipiens have been well described, the to sugar gluttony. We present evidence demonstrating that genes molecular events that contribute to this metabolic decision have not encoding enzymes needed to digest a blood meal (trypsin and a been explored. In this study, we used suppressive subtractive chymotrypsin-like protease) are down-regulated in diapause-des- hybridization (SSH) to isolate three clones linked to this metabolic tined females, and that concurrently, a gene associated with the decision: fatty acid synthase, trypsin, and chymotrypsin-like serine accumulation of lipid reserves (fatty acid synthase) is highly up- protease. We then used these clones to probe the metabolic path- regulated. As the females then enter diapause, fatty acid synthase ways associated with the mosquito’s metabolic decision to enter and is only sporadically expressed, and expression of trypsin and terminate diapause. Because both short day length and low tem- chymotrypsin-like remains undetectable. Late in diapause (2–3 perature program diapause in C. pipiens, we also distinguished months at 18°C), the genes encoding the digestive enzymes begin between temperature and photoperiodic effects. We concluded to be expressed as the female prepares to take a blood meal upon that the short-day programming of diapause results in the down- the termination of diapause.
    [Show full text]
  • Wsn 40 (2016) 147-162 Eissn 2392-2192
    Available online at www.worldscientificnews.com WSN 40 (2016) 147-162 EISSN 2392-2192 Utilization of mulberry leaves treated with seed powder cowpea, Vigna unguiculata (L) for feeding the fifth instar larvae of silkworm, Bombyx mori (L) (Race: PM x CSR2) Vitthalrao B. Khyade1,*, Atharv Atul Gosavi2 1Department of Zoology, Shardabai Pawar Mahila Mahavidyalaya, Shardanagar Tal. Baramati; Dist. Pune - 413115, India 2Agriculture Development Trust Agri Polytechnic, Sharadanagar, Malegaon Colony, Tal: Baramati, Dist: Pune. PIN: 413115 Maharashtra, India *E-mail address: [email protected] ABSTRACT The present attempt was to screen the changes in the cocoon parameters; silk filament parameters and activities of biochemical reactions catalyzed by the midgut enzymes fifth instsr larvae of silkworm fed with mulberry leaves treated with aqueous solution of seed powder of Cowpeas (Vigna unguiculata). The cowpea seed powder was dissolved in distilled water and diluted to 2.5%, 5%, 7.5%, and 10% concentrations. Fresh mulberry leaves were dipped in each concentration of aqueous solution of cowpea seed powder for half an hour. 1000 ml solution was used for 100 grams of mulberry leaves. Treated mulberry leaves were drained off completely and then used for feeding. The mulberry leaves were fed five times per day at the rate of 100 grams per 100 larvae for each time. Untreated group of larvae were feed with untreated mulberry leaves. Water treated group of larvae were feed with water treated mulberry leaves. The experimental groups of larvae were feed with feed separately with 2.5 percent cowpea treated; 5.00 percent cowpea treated; 7.5 percent cowpea treated and 10.00 percent cowpea treated mulberry leaves.
    [Show full text]
  • Digestive Enzymes: the Key to Optimum Health
    Education Article Digestive Enzymes: The Key to Optimum Health Digestion is essential for good health. Unlocking nutrients from foods is a complex process. In order to break down food we rely on optimal levels and function of a special set of proteins called digestive enzymes. These proteins are found in the saliva and also in the small intestines. Without the combined actions of our digestive enzymes we would simply be unable to absorb many nutrients that we need to maintain good health. This is why reduced levels of digestive enzymes can be linked to a wide-range of symptoms within the gut and beyond. Digestive enzymes, along with stomach acid, play a crucial role in the initial stages of digestion, i.e. the breaking down of the food that we eat. The main classes of human digestive enzymes include proteases, lipases and carbohydrases, which respectively break down the macronutrients protein, fats and carbohydrates. If we do not efficiently digest these foods then vital nutrients such as essential fats, vitamins, minerals and phytonutrients cannot be absorbed. What is more, undigested or partially digested food passes through into the large intestines and is fermented by the resident colonic bacteria, causing unpleasant symptoms such as bloating and flatulence and contributing to a toxic bowel. Naturopaths believe toxicity within the bowel is the root of all disease. We do not make digestive enzymes for every type of food that we eat, such as gluten and phytic acid found in some grains and cereals and lactose, a sugar found in milk. This means our bodies may find it difficult to digest these types of foods.
    [Show full text]
  • Partial Characterization of Hepatopancreatic and Extracellular
    Aquaculture International Archimer June 2011, Volume 19, Number 3, Pages 445-457 http://archimer.ifremer.fr http://dx.doi.org/10.1007/s10499-010-9360-5 © Springer Science+Business Media B.V. 2010 The original publication is available at http://www.springerlink.com is available on the publisher Web site Web publisher the on available is Partial characterization of hepatopancreatic and extracellular digestive proteinases of wild and cultivated Octopus maya R. Martínez1, R. Sántos2, A. Álvarez3, G. Cuzón4, L. Arena5, M. Mascaró5, C. Pascual5 and C. Rosas5, * 1 División de Posgrado, FMVZ, Universidad Autónoma de Yucatán, Mérida, Yucatán, Mexico 2 authenticated version authenticated Departamento de Nutrición, FMVZ, Universidad Autónoma de Yucatán, Mérida, Yucatán, Mexico - 3 Unidad de Ciencias Biológicas, UJAT, Villahermosa, Tabasco, Mexico 4 Ifremer, Tahiti, French Polynesia 5 Unidad Multidisciplinaria de Docencia e Investigación, Facultad de Ciencias, Universidad Nacional Autónoma de México, Puerto de abrigo s/n, Sisal, Yucatan, Mexico *: Corresponding author : C. Rosas, email address : [email protected] Abstract: Abstract Proteinases from hepatopancreas (HP) and gastric juice (GJ) from wild and cultured red octopus (Octopus maya) were characterized. Hepatopancreas assays revealed optimal activity at pH 4, 9–10 and 10 for wild and pH 3, 8, and 9, for cultured octopuses, for total proteinases, trypsin and chymotrypsin, respectively. In the gastric juice, maximum activity was recorded at pH 6, 8, and 7 for total proteinases, trypsin, and chymotrypsin, respectively for both wild and cultured octopus. A reduction on enzyme activity of 70 and 20% was observed in HP and GJ extracts, respectively when protease inhibitor Pepstatin A was used.
    [Show full text]
  • Characterization and Functionalization of Suckerin-12 Protein
    CHARACTERIZATION AND FUNCTIONALIZATION OF SUCKERIN-12 PROTEIN HYDROGELS Dissertation Submitted to The School of Engineering of the UNIVERSITY OF DAYTON In Partial Fulfillment of the Requirements for The Degree of Doctor of Philosophy in Engineering By Chelsea Buck, M.S. UNIVERSITY OF DAYTON Dayton, Ohio December 2018 CHARACTERIZATION AND FUNCTIONALIZATION OF SUCKERIN-12 PROTEIN HYDROGELS Name: Buck, Chelsea Carolyn APPROVED BY: Kristen K. Comfort, Ph. D. Donald A. Klosterman, Ph. D. Advisory Committee Chairman Committee Member Associate Professor Associate Professor Chemical and Materials Engineering Chemical and Materials Engineering Margaret F. Pinnell, Ph. D. Patrick B. Dennis, Ph. D. Committee Member Committee Member Associate Dean Research Scientist Mechanical and Aerospace Engineering Air Force Research Laboratory Robert J. Wilkens, Ph.D., P.E. Eddy M. Rojas, Ph.D., M.A., P.E. Associate Dean for Research and Innovation Dean Professor School of Engineering School of Engineering ii © Copyright by Chelsea Carolyn Buck All rights reserved 2018 iii ABSTRACT CHARACTERIZATION AND FUNCTIONALIZATION OF SUCKERIN-12 PROTEIN HYDROGELS Name: Buck, Chelsea Carolyn University of Dayton Advisor: Dr. Kristen K. Comfort Previous research of suckerin proteins identified in the sucker ring teeth of cephalopods have impressive mechanical properties and behave as thermoplastic materials. In this research, one isoform of suckerin protein, suckerin-12 was explored as a mechanically robust material. The protein was isolated and recombinantly expressed in E. coli. Gram-scale quantities of pure protein were expressed and purified to create enzymatically crosslinked hydrogels. Exposure to select salt anion conditions caused the hydrogels to contract significantly, at rates highly dependent upon the anion present in the buffer, which followed a trend modeled by the Hofmeister Series of anions.
    [Show full text]
  • Pancreatic Amylase
    1. Functional Anatomy • The pancreas which lies parallel to and beneath the stomach is composed of: 1. The endocrine islets of Langerhans which secrete: Hormone Type of cell % of secretion Insulin Beta cells 60% crucial for normal regulation of glucose, Glucagon Alpha cells ~25% lipid & protein metabolism Somatostatin delta cells ~10% 1. Acinar gland tissues which produce pancreatic juice (the main source of digestive enzymes). • The pancreatic digestive enzymes are secreted by pancreatic acini. • Large volumes of sodium Bicarbonate solution are secreted by the small ductules and larger ducts leading from the acini. • Pancreatic juice is secreted in Response to the presence of Chyme in the upper portions of the small intestine. 2. Major Components of Pancreatic Secretion and Their Physiologic Roles & 5. Activation of Pancreatic Enzymes • The major functions of pancreatic secretion: 1. To neutralize the acids in the duodenal chyme to optimum range (pH= 7.0-8.0) for activity of pancreatic enzymes. 2. To prevent damage to duodenal mucosa by acid & pepsin. 3. To produce enzymes involved in the digestion of dietary carbohydrate, fat, and protein. Pancreatic Enzymes: The pancreas secrests enzymes that act on all major types of food stuffs. 1. Pancreatic Proteolytic Enzymes (Trypsin, Chymotrypsin, Carboxypolypeptidase, Elastase) • Trypsin & Chymotrypsin split whole and partially digested proteins into peptides of various sizes but do not cause release of individual amino acids. • Carboxypolypeptidase splits some peptides into individual amino acids, thus completing digestion of some proteins to amino acids. • When first synthesized in the pancreatic cells, digestive enzymes are in the inactive forms; these enzymes become activated only after they are secreted into the intestinal tract.
    [Show full text]
  • Tumor-Associated and Microbial Proteases Compromise Host Igg Effector Functions by a Single Cleavage Proximal to the Hinge
    Tumor-associated and microbial proteases compromise host IgG effector functions by a single cleavage proximal to the hinge Randall J. Brezski1, Omid Vafa, Diane Petrone, Susan H. Tam, Gordon Powers, Mary H. Ryan, Jennifer L. Luongo, Allison Oberholtzer, David M. Knight, and Robert E. Jordan1 Biologics Research, Centocor R&D Inc., Radnor, PA 19087 Edited by Barry S. Coller, The Rockefeller University, New York, NY, and approved August 31, 2009 (received for review April 15, 2009) The successful elimination of pathogenic cells and microorganisms responsible for binding the MHC-class I related receptor, the by the humoral immune system relies on effective interactions neonatal Fc receptor (FcRn) that mediates the serum half-life of between host immunoglobulins and Fc␥ receptors on effector cells, circulating IgGs (14–16), are located in the area between the CH2 in addition to the complement system. Essential Ig motifs that and CH3 regions of the Fc (17–19). direct those interactions reside within the conserved IgG lower Several groups previously documented that certain proteases hinge/CH2 interface. We noted that a group of tumor-related and associated with inflammation, tumor invasion, metastasis, and microbial proteases cleaved human IgG1s in that region, and the bacterial infections have the ability to cleave IgGs (20, 21). Several ‘‘nick’’ of just one of the heavy chains profoundly inhibited IgG1 proteases preferentially cleave IgGs in the lower hinge, including effector functions. We focused on IgG1 monoclonal antibodies the matrix metalloproteinases (MMPs) stromelysin-1 (MMP-3), (mAbs) since IgG1 is the most abundant human subclass and metalloelastase (MMP-12) (both cleave between P232 and E233), demonstrates robust Fc-mediated effector functions.
    [Show full text]
  • The Basic Helix-Loop-Helix Transcription Factor E47 Reprograms Human Pancreatic Cancer Cells to a Quiescent Acinar State with Reduced Tumorigenic Potential
    ORIGINAL ARTICLE The Basic Helix-Loop-Helix Transcription Factor E47 Reprograms Human Pancreatic Cancer Cells to a Quiescent Acinar State With Reduced Tumorigenic Potential SangWun Kim, MD,*†‡ Reyhaneh Lahmy, PhD,*‡ Chelsea Riha, BS,*‡ Challeng Yang, BS,*‡ Brad L. Jakubison, BS,§ Jaco van Niekerk, BS,*‡ Claudio Staub, BS,*‡ Yifan Wu, BS,*‡ Keith Gates, PhD,|| Duc Si Dong, PhD,|| Stephen F.Konieczny, PhD,§ and Pamela Itkin-Ansari, PhD*‡ (Pancreas 2015;44: 718–727) Objectives: Pancreatic ductal adenocarcinoma (PDA) initiates from quiescent acinar cells that attain a Kras mutation, lose signaling from basic helix-loop-helix (bHLH) transcription factors, undergo acinar-ductal meta- ancreatic ductal adenocarcinoma (PDA) arises from the exocrine pancreas, which is composed of 2 major cell plasia, and rapidly acquire increased growth potential. We queried whether P — PDA cells can be reprogrammed to revert to their original quiescent acinar populations acinar cells that produce digestive enzymes and cell state by shifting key transcription programs. duct cells that are tasked with transporting acinar enzymes to Methods: Human PDA cell lines were engineered to express an inducible the duodenum. Despite the ductal morphology of PDA, lineage tracing studies have revealed that the tumors arise from the acinar form of the bHLH protein E47. Gene expression, growth, and functional 1–9 studies were investigated using microarray, quantitative polymerase chain re- compartment. In response to oncogenic Kras, quiescent acinar action, immunoblots, immunohistochemistry,
    [Show full text]
  • Pancreatic Exocrine Insufficiency and Enteral Feeding: a Practical Guide with Case Studies
    NUTRITION ISSUES IN GASTROENTEROLOGY, SERIES #181 NUTRITION ISSUES IN GASTROENTEROLOGY, SERIES #181 Carol Rees Parrish, M.S., R.D., Series Editor Pancreatic Exocrine Insufficiency and Enteral Feeding: A Practical Guide with Case Studies Mary E. Phillips Amy Berry Lucy S. Gettle Patients with pancreatic disease can develop severe malnutrition. Many factors contribute to the malnutrition seen in this patient population, one of the most problematic being pancreatic exocrine insufficiency (PEI) with resultant malabsorption. Pancreatic enzyme replacement therapies (PERT) are predominantly designed for oral administration, but this can be challenging in patients requiring enteral nutrition (EN). This review explores the use of PERT in complex patients who are on EN. Case studies will be utilized to demonstrate different methods available in order to provide practical guidance on administration, both in the United States (U.S.) and the United Kingdom (U.K.). INTRODUCTION atients with pancreatic disease, pancreatic medium-chain triglycerides, thereby decreasing resection, and cystic fibrosis often develop the dependence of pancreatic lipase for absorption. Psignificant malnutrition as a result of the However, some patients will continue to malasborb, numerous gastrointestinal (GI) complications even with semi-elemental products, worsening the preventing adequate oral intake. Malabsorption, malnutrition present. as well as side effects of medications such Traditional signs and symptoms of as antibiotics and opiates, adds an additional malabsorption
    [Show full text]
  • Spectrazyme Patient Brochure
    Gastrointestinal Health Take Our The SpectraZyme Difference Digestive Health Quiz SpectraZyme enzyme formulas, recommended by your healthcare practitioner, provide you exceptional quality Food is meant Do you feel you may have trouble digesting and personalized options that feature a wide array of digestive enzymes: to be enjoyed your meals? Enzyme What It Helps Break Down Do meals cause discomfort that negatively for Digestion impact the quality of your living? Amylase Carbohydrates (starches and other polysaccharides) Does the thought of after-meal digestion Protease Protein (large amino acid chains) cause you concern? Peptidase & Pepsin Peptides (smaller amino acid chains) Lipase Fats (triglycerides and other lipids) Do you have a known or suspected Lactase Lactose (milk sugar) sensitivity to lactose or gluten? Cellulase, Pectinase, Cellulose, pectin, xylan & Xylanase & hemicellulose (plant fibers and Do you have occasional indigestion or a Hemicellulase carbohydrates) feeling of fullness that lasts 2-4 hours Maltase Maltose (malt sugar) after eating? Invertase Sucrose (table sugar) Do you experience occasional bloating? Ask about SpectraZyme formulas today! Have you noticed a difference in your Learn more at SpectraZyme.com digestion as you age? Have you noticed undigested food in Unsurpassed Quality Setting quality standards for the industry for over the stool? 30 years, Metagenics tests each SpectraZyme product batch for enzyme activity—a better indicator of potency If you answered “yes” to any of these questions, than weight. ask your healthcare provider about nutritional strategies for digestive health, including digestive SpectraZyme®—high quality enzyme formulas enzymes and simple dietary and lifestyle changes. Triple GMP Certified Manufacturing for enhanced digestive health support* MET2070 072716 © 2016 Metagenics, Inc.
    [Show full text]
  • Systemic Enzyme Support: the Importance of Good Digestion
    Recent health and nutrition information from Douglas Laboratories August 2008 Systemic Enzyme Support: The Importance of Good Digestion An Overview by Rodger H. Murphree II, D.C., C.N.S. 1 2 by Wald M, M.D. , Honzíková M, M.D. , Lysíková M, It’s often been said “you are what you eat.” However a M.D., Ph.D.2, Masinovský Z, Ph.D.2 1Department of Surgery, more accurate statement might be you are what you eat, 2nd Medical Faculty, Charles University, Prague, Czech digest, absorb, and assimilate. Food, carbohydrates, fats, and Republic 2Department of Enzyme Therapy, Society of General proteins are the body’s building blocks. We need them for Medicine, J.E. Purkyne Czech Medical Association, Prague, our very survival. Carbohydrates are the body’s main source Czech Republic of fuel. Protein is needed for making the essential hormones and enzymes, preserving lean muscle mass, and for tissue Introduction repair. Dietary fat provides energy, maintains cell membranes, and helps absorb vitamins A, D, E, K, and carotenoids. The A large number of conditions are primarily inflammatory in digestion, absorption, and assimilation of the macronutrients, nature and may be significantly complicated by the presence of ensures we get adequate amounts of essential micronutrients- secondary forms of inflammation. Regardless of whether the cause enzymes, vitamins, minerals, amino acids, and fatty acids of the problem is due to bacterial, viral or auto-immune influences, which affect every cell in the body. The health of the digestive the result may be an ongoing situation with significant clinical and system not only determines how well we absorb these essential laboratory manifestations of the inflammatory process.
    [Show full text]
  • Gluten Digestive Enzyme Gluten Specific Digestive Enzyme Formula
    Gluten Digestive Enzyme Gluten specific digestive enzyme formula DESCRIPTION INDICATIONS Gluten Digestive Enzyme is a natural dietary supplement Gluten Digestive Enzyme may be a useful nutritional adjunct specifically formulated with enzymes known to enhance the for individuals who wish to supplement and improve the digestion of gluten. The addition of acidophilus and prebiotics digestion of gluten in their diet. further enhances the digestion of gluten in the diet. FORMULA (WW #10324) FUNCTIONS 2 Vegetarian Capsules Contain: Gluten consists of the proteins gliadin and glutenin. Gluten Gluten Enzyme Formula .................................... 850 mg has been found to be the protein-containing portion of certain Strong Acid Protease ................................... 75,000 HUT grains such as wheat, rye, oats and barley. Gluten is pervasive (Aspergillus oryzae/niger) in the Standard American Diet. Over two million Americans DPPzyme IV Blend: suffer from gluten sensitivity, but there are believed to be Protease FCC ...................................... 120,000 HUT millions more who have gluten sensitivity, but have not (Aspergillus oryzae/niger) been formally diagnosed. Gluten sensitivity is caused by an Protease FCC ............................................ 20,000 PC abnormal immune response to partially digested gluten. When (Bacillus subtillis) gluten is not completely digested, protein fragments known as Protease USP .......................................... 15,000 USP peptides can trigger an autoimmune response that can lead
    [Show full text]