Enzymes
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  Enzymes



Enzymes

   Proteins that act as a catalysts in mediating and speeding a specific chemical reaction.



SIMILAR TERMS
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Enzymatic Effects
Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however catalytic RNA (RNA, CATALYTIC) and catalytic DNA (DNA, CATALYTIC) molecules have also been identified.

Enzymatic Zonulolyses
Surgical removal of a cataractous lens. (Dorland, 28th ed)

Enzymatic Zonulolysis
Surgical removal of a cataractous lens. (Dorland, 28th ed)

Enzyme
A cellular protein whose shape allows it to hold together several other molecules in close proximity to each other. In this way, enzymes are able to induce chemical reactions in other substances with little expenditure of energy and without being changed themselves. Basically, an enzyme acts as a catalyst.

Enzyme (natural catalyst)
Any of numerous proteins and protein-nonprotein compounds that living cells produce and that can initiate, or affect the speed of, specific chemical reactions.

Enzyme Activation
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1) activation by ions (activators); 2) activation by cofactors (coenzymes); and 3) conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

Enzyme Activations
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1) activation by ions (activators); 2) activation by cofactors (coenzymes); and 3) conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.

Enzyme Activators
Compounds or factors that act on a specific enzyme to increase its activity.

Enzyme Analyses, Restriction
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

Enzyme Analysis, Restriction
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

Enzyme Antagonists, Angiotensin-Converting
A class of drugs whose main indications are the treatment of hypertension and heart failure. They exert their hemodynamic effect mainly by inhibiting the renin-angiotensin system. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility.

Enzyme defect
A disorder resulting from a deficiency (or functional abnormality) of an enzyme. In 1902 Archibald Garrod first attributed a disease to an enzyme defect: an inborn error of metabolism. Today, newborns are routinely screened for certain enzyme defects such as PKU (phenylketonuria) and galactosemia, an error in the handling (metabolism) of the sugar galactose.

Enzyme Disorder, Lysosomal
Inborn errors of metabolism characterized by defects in specific lysosomal hydrolases and resulting in intracellular accumulation of unmetabolized substrates.

Enzyme Disorders, Lysosomal
Inborn errors of metabolism characterized by defects in specific lysosomal hydrolases and resulting in intracellular accumulation of unmetabolized substrates.

Enzyme Electrode
Any of a variety of procedures which use biomolecular probes to measure the presence or concentration of biological molecules, biological structures, microorganisms, etc., by translating a biochemical interaction at the probe surface into a quantifiable physical signal.

Enzyme Electrodes
Any of a variety of procedures which use biomolecular probes to measure the presence or concentration of biological molecules, biological structures, microorganisms, etc., by translating a biochemical interaction at the probe surface into a quantifiable physical signal.

Enzyme Immunoassay
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme Immunoassays
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme Induction
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.

Enzyme Inhibitor, Nonapeptide-Converting
A synthetic nonapeptide (Pyr-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro) which is identical to the peptide from the venom of the snake, Bothrops jararaca. It inhibits kininase II and ANGIOTENSIN I and has been proposed as an antihypertensive agent.

Enzyme Inhibitors
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

Enzyme Inhibitors, Angiotensin-Converting
A class of drugs whose main indications are the treatment of hypertension and heart failure. They exert their hemodynamic effect mainly by inhibiting the renin-angiotensin system. They also modulate sympathetic nervous system activity and increase prostaglandin synthesis. They cause mainly vasodilation and mild natriuresis without affecting heart rate and contractility.

Enzyme Labeled Antibody Technic
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme Labeled Antibody Technique
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme Linked Immunosorbent Assay
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.

Enzyme linked immunosorbent assay (ELISA)
A blood test used to find Helicobacter pylori bacteria. Also used to diagnose an ulcer.

Enzyme Mapping, Restriction
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

Enzyme Mappings, Restriction
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.

Enzyme Multiplied Immunoassay Technique
An immunoenzyme test for the presence of drugs and other substances in urine and blood. The test uses enzyme linked antibodies that react only with the particular drug for which the sample is being tested.

Enzyme Precursors
Physiologically inactive substances that can be converted to active enzymes.

Enzyme Reactivators
Compounds which restore enzymatic activity by removing an inhibitory group bound to the reactive site of the enzyme.

Enzyme replacement
A strategy designed to replace missing enzyme activity in a patient. This strategy currently involves the administration of a purified protein (the enzyme) by intravenous infusion.

Enzyme Repression
The interference in synthesis of an enzyme due to the elevated level of an effector substance, usually a metabolite, whose presence would cause depression of the gene responsible for enzyme synthesis.

Enzyme Stabilities
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

Enzyme Stability
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.

Enzyme, 1,4-alpha-Glucan Branching
In glycogen or amylopectin synthesis, the enzyme that catalyzes the transfer of a segment of a 1,4-alpha-glucan chain to a primary hydroxy group in a similar glucan chain. EC 2.4.1.18.

Enzyme, Acetyl Activating
An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.

Enzyme, Amylopectin Branching
In glycogen or amylopectin synthesis, the enzyme that catalyzes the transfer of a segment of a 1,4-alpha-glucan chain to a primary hydroxy group in a similar glucan chain. EC 2.4.1.18.

Enzyme, Angiotensin-Forming
An enzyme which is secreted by the kidney and is formed from prorenin in plasma and kidney. The enzyme cleaves the Leu-Leu bond in angiotensinogen to generate angiotensin I. EC 3.4.23.15. (Formerly EC 3.4.99.19).

Enzyme, Branching
In glycogen or amylopectin synthesis, the enzyme that catalyzes the transfer of a segment of a 1,4-alpha-glucan chain to a primary hydroxy group in a similar glucan chain. EC 2.4.1.18.

Enzyme, C5 Cleaving
The enzyme which in both the classical and alternate complement pathways cleaves complement 3 into anaphylatoxin (C3a) and C3b.

Enzyme, CAT
An enzyme that catalyzes the acetylation of chloramphenicol to yield chloramphenicol 3-acetate. Since chloramphenicol 3-acetate does not bind to bacterial ribosomes and is not an inhibitor of peptidyltransferase, the enzyme is responsible for the naturally occurring chloramphenicol resistance in bacteria. The enzyme, for which variants are known, is found in both gram-negative and gram-positive bacteria. EC 2.3.1.28.

Enzyme, Cholesterol Esterifying
An enzyme that catalyzes the formation of cholesterol esters by the direct transfer of the fatty acid group from a fatty acyl CoA derivative. This enzyme has been found in the adrenal gland, gonads, liver, intestinal mucosa, and aorta of many mammalian species. EC 2.3.1.26.

Enzyme, Citrate Cleavage
An enzyme that, in the presence of ATP and CoA, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and orthophosphate. This reaction represents an important step in fatty acid biosynthesis. EC 4.1.3.8.

Enzyme, Disulfide Interchange
An enzyme that catalyzes the rearrangement of disulfide bonds within proteins during folding. It is a monomer identical to one of the subunits of PROCOLLAGEN-PROLINE DIOXYGENASE. (From Dorland, 28th ed) EC 5.3.4.1.

Enzyme, DNA Photoreactivating
An enzyme that catalyzes the reactivation by light of UV-irradiated DNA. It breaks two carbon-carbon bonds in pyrimidine dimers in DNA. EC 4.1.99.3.

Enzyme, Glycogen Branching
In glycogen or amylopectin synthesis, the enzyme that catalyzes the transfer of a segment of a 1,4-alpha-glucan chain to a primary hydroxy group in a similar glucan chain. EC 2.4.1.18.

Enzyme, Glycogen Debranching
1,4-alpha-D-Glucan-1,4-alpha-D-glucan 4-alpha-D-glucosyltransferase/dextrin 6 alpha-D-glucanohydrolase. An enzyme system having both 4-alpha-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33) activities. As a transferase it transfers a segment of a 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-1,6-glucosidase activity is deficient in glycogen storage disease type III.

Enzyme, IL-1 beta-Converting
A member of the caspase family that is highly specific for interleukin-1beta (INTERLEUKIN-1). It plays a role in inflammation and mammalian APOPTOSIS. Interleukin-1beta converting enzyme is frequently abbreviated ICE. EC 3.4.22.36

Enzyme, Insulin-Degrading
An enzyme the catalyzes the degradation of insulin, glucagon and other polypeptides. It is inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not phosphoramidon. (Eur J Biochem 1994;223:1-5) EC 3.4.24.56.

Enzyme, Interleukin-1 Converting
A member of the caspase family that is highly specific for interleukin-1beta (INTERLEUKIN-1). It plays a role in inflammation and mammalian APOPTOSIS. Interleukin-1beta converting enzyme is frequently abbreviated ICE. EC 3.4.22.36

Enzyme, Interleukin-1beta Converting
A member of the caspase family that is highly specific for interleukin-1beta (INTERLEUKIN-1). It plays a role in inflammation and mammalian APOPTOSIS. Interleukin-1beta converting enzyme is frequently abbreviated ICE. EC 3.4.22.36

Enzyme, Kinin-Forming
Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increases vascular permeability and affects smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77).

Enzyme, lysosomal
An enzyme in an organelle (a little organ) called the lysosome within the cell. Lysosomal enzymes degrade (break down) macromolecules (large molecules) and other materials (such as bacteria) that have been taken up by the cell during the process of endocytosis. In endocytosis, macromolecules and particles from outside the cell are taken up by the cell via a progressive invagination (inpouching) and eventual pinching off of a region of the cell membrane, forming a membrane-bound vesicle (bubble) within the cytoplasm of the cell. The vesicle then fuses with the lysosome and the lysosomal enzymes carry out their appointed task of destruction (by hydrolysis). Quite amazingly, the lysosomal enzymes do not normally damage the cell itself.

Enzyme, Malate Condensing
An important enzyme in the glyoxylic acid cycle which reversibly catalyzes the synthesis of L-malate from acetyl-CoA and glyoxylate. EC 4.1.3.2.

Enzyme, Multifunctional
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates; may involve simply a transfer of water molecules of hydrogen atoms or be associated with large supramolecular structures such as mitochondria or ribosomes.

Enzyme, Old Yellow
A flavoprotein that reversibly oxidizes NADPH to NADP and a reduced acceptor. EC 1.6.99.1.

Enzyme, Photoreactivating
An enzyme that catalyzes the reactivation by light of UV-irradiated DNA. It breaks two carbon-carbon bonds in pyrimidine dimers in DNA. EC 4.1.99.3.

Enzyme, restriction
An enzyme from bacteria that can recognize specific base sequences in DNA and cut the DNA at that site (the restriction site). A restriction enzyme acts as a biochemical scissors. Also called a restriction endonuclease. Bacteria use restriction enzymes to defend against bacterial viruses called bacteriophages (or phage). When a phage infects a bacterium, it inserts its DNA into the bacterium so that it is replicated. The restriction enzyme prevents replication of the phage DNA by cutting it into many pieces. Restriction enzymes were named for their ability to restrict, or limit, the number of strains of bacteriophage that can infect bacteria.

Enzyme, Starch Branching
In glycogen or amylopectin synthesis, the enzyme that catalyzes the transfer of a segment of a 1,4-alpha-glucan chain to a primary hydroxy group in a similar glucan chain. EC 2.4.1.18.

Enzyme, Sulfhydryl-Disulfide Interchange
An enzyme that catalyzes the rearrangement of disulfide bonds within proteins during folding. It is a monomer identical to one of the subunits of PROCOLLAGEN-PROLINE DIOXYGENASE. (From Dorland, 28th ed) EC 5.3.4.1.

Enzyme, Terminal Addition
A non-template-directed DNA polymerase normally found in vertebrate thymus and bone marrow. It catalyzes the elongation of oligo- or polydeoxynucleotide chains and is widely used as a tool in the differential diagnosis of acute leukemias in man. EC 2.7.7.31.

Enzyme, Thyroxine Converting
A hemeprotein that catalyzes the oxidation of the iodide radical to iodine with the subsequent iodination of many organic compounds, particularly proteins. EC 1.11.1.8.

Enzyme, YGG-Forming
Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA), an important marker in the diagnosis of human acute lymphocytic leukemia. EC 3.4.24.11.

Enzyme-Labeled Antibody Technic
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme-Labeled Antibody Technics
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme-Labeled Antibody Technique
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme-Labeled Antibody Techniques
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.

Enzyme-Linked Immunosorbent Assay
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.

Enzyme-linked immunosorbent assay (ELISA)
An assay in which an enzyme is linked to an antibody and a coloured substrate is used to measure the activity of bound enzyme and, hence, the amount of bound antibody.

Enzyme-Linked Immunosorbent Assays
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.

Enzymes Activators
Compounds or factors that act on a specific enzyme to increase its activity.

Enzymes, Coenzymes, and Enzyme Inhibitors
Biological catalysts, their cofactors, and inhibitors.

Enzymes, Complement Activating
Enzymes present in the complement system which activate one or more components in the system.

Enzymes, DNA Repair
Poly(deoxyribonucleotide):poly(deoxyribonucleotide)ligases. Enzymes that catalyze the joining of preformed deoxyribonucleotides in phosphodiester linkage during genetic processes during repair of a single-stranded break in duplex DNA. The class includes both EC 6.5.1.1 (ATP) and EC 6.5.1.2 (NAD).

Enzymes, DNA Restriction-Modification
Systems consisting of two enzymes, a modification methylase and a restriction endonuclease. They are closely related in their specificity and protect the DNA of a given bacterial species. The methylase adds methyl groups to adenine or cytosine residues in the same target sequence that constitutes the restriction enzyme binding site. The methylation renders the target site resistant to restriction, thereby protecting DNA against cleavage.

Enzymes, Immobilized
Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields.

Enzymes, Multifunctional
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates; may involve simply a transfer of water molecules of hydrogen atoms or be associated with large supramolecular structures such as mitochondria or ribosomes.

Enzymes, yellow
A group of respiratory enzymes that catalyze reactions in the body permitting cells to respire or breathe. These biochemical reactions are termed oxidation-reduction reactions.

Enzymologic Gene Expression Regulation
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.



PREVIOUS AND NEXT TERMS
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Enzootic
Endemic in animals. An enzootic disease is constantly present in an animal population, but usually only affects a small number of animals at any one time.

Enzyme defect
A disorder resulting from a deficiency (or functional abnormality) of an enzyme. In 1902 Archibald Garrod first attributed a disease to an enzyme defect: an inborn error of metabolism. Today, newborns are routinely screened for certain enzyme defects such as PKU (phenylketonuria) and galactosemia, an error in the handling (metabolism) of the sugar galactose.

Enzyme replacement
A strategy designed to replace missing enzyme activity in a patient. This strategy currently involves the administration of a purified protein (the enzyme) by intravenous infusion.

Enzyme, lysosomal
An enzyme in an organelle (a little organ) called the lysosome within the cell. Lysosomal enzymes degrade (break down) macromolecules (large molecules) and other materials (such as bacteria) that have been taken up by the cell during the process of endocytosis. In endocytosis, macromolecules and particles from outside the cell are taken up by the cell via a progressive invagination (inpouching) and eventual pinching off of a region of the cell membrane, forming a membrane-bound vesicle (bubble) within the cytoplasm of the cell. The vesicle then fuses with the lysosome and the lysosomal enzymes carry out their appointed task of destruction (by hydrolysis). Quite amazingly, the lysosomal enzymes do not normally damage the cell itself.

Enzyme, restriction
An enzyme from bacteria that can recognize specific base sequences in DNA and cut the DNA at that site (the restriction site). A restriction enzyme acts as a biochemical scissors. Also called a restriction endonuclease. Bacteria use restriction enzymes to defend against bacterial viruses called bacteriophages (or phage). When a phage infects a bacterium, it inserts its DNA into the bacterium so that it is replicated. The restriction enzyme prevents replication of the phage DNA by cutting it into many pieces. Restriction enzymes were named for their ability to restrict, or limit, the number of strains of bacteriophage that can infect bacteria.

Enzymes

Enzymes, yellow
A group of respiratory enzymes that catalyze reactions in the body permitting cells to respire or breathe. These biochemical reactions are termed oxidation-reduction reactions.

EOG
Electro-oculography. A type of electrophysiologic retinal testing.

EOS
The gene for familial eosinophilia. EOS has been mapped to chromosome region 5q31-33 containing the cytokine gene cluster which includes the genes for interleukin-3 (IL-3), interleukin-5 (IL-5), and granulocyte colony-stimulating factor (G-CSF), and all of which are thought play roles in the development, proliferation, and activation of eosinophils.

Eosinophilia
An abnormally high number of eosinophils in the blood. Normally, eosinophils constitute 1 to 3% of the peripheral blood leukocytes, at a count of 350 to 650 per cubic millimeter. Eosinophilia can be categorized as mild (less than 1500 eosinophils per cubic millimeter), moderate (1500 to 5000 per cubic millimeter), or severe (more than 5000 per cubic millimeter).

Eosinophilic meningitis
Meningitis with a high percentage of eosinophils (a type of white blood cell) in the cerebrospinal fluid (CSF). The usual cause is the parasite Angiostrongylus cantonensis, also known as the rat lungworm. People become infected with this parasite by ingesting its larvae in raw or insufficiently cooked snails, slugs, freshwater prawns, frogs, or fish. Infection may also occur by consumption of fresh produce such as contaminated lettuce. When the larvae are ingested, they penetrate the intestinal tract, go into blood vessels, and eventually reach the meninges (the covering of the brain and spinal cord). The larvae usually die there shortly thereafter. An eosinophilic reaction develops in response to the dying larvae. It is manifested by an outpouring of eosinophils in the CSF.

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