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EcoR1
EcoRI
EcoRI
(pronounced "eco R one") is a restriction endonuclease enzyme isolated from species E. coli. The Eco part of the enzyme's name originates from the species from which it was isolated, while the R represents the particular strain, in this case RY13. The last part of its name, the I, denotes that it was the first enzyme isolated from this strain. EcoRI
EcoRI
is a restriction enzyme that cleaves DNA double helices into fragments at specific sites. It is also a part of the restriction modification system. In molecular biology it is used as a restriction enzyme. EcoRI
EcoRI
creates 4 nucleotide sticky ends with 5' end
5' end
overhangs of AATT. The nucleic acid recognition sequence where the enzyme cuts is G/AATTC, which has a palindromic, complementary sequence of CTTAA/G. The / in the sequence indicates which phosphodiester bond the enzyme will break in the DNA molecule
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Protein
Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɪnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues
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Lipase
A lipase (/ˈlaɪpeɪs/, /ˈlɪpeɪs/, /-peɪz/) is any enzyme that catalyzes the hydrolysis of fats (lipids).[1] Lipases are a subclass of the esterases. Lipases perform essential roles in the digestion, transport and processing of dietary lipids (e.g. triglycerides, fats, oils) in most, if not all, living organisms. Genes
Genes
encoding lipases are even present in certain viruses.[2][3] Most lipases act at a specific position on the glycerol backbone of a lipid substrate (A1, A2 or A3)(small intestine)
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Hydrolase
In biochemistry, a hydrolase is an enzyme that catalyzes the hydrolysis of a chemical bond. For example, an enzyme that catalyzes the following reaction is a hydrolase:A–B + H2O → A–OH + B–HContents1 Nomenclature 2 Classification 3 Clinical considerations 4 Etymology and pronunciation 5 See also 6 ReferencesNomenclature[edit] Systematic names of hydrolases are formed as "substrate hydrolase." However, common names are typically in the form "substratease." For example, a nuclease is a hydrolase that cleaves nucleic acids. Classification[edit] Hydrolases are classified as EC 3 in the EC number classification of enzymes
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Esterase
An esterase is a hydrolase enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis. A wide range of different esterases exist that differ in their substrate specificity, their protein structure, and their biological function. EC classification/list of enzymes[edit] Acetylesterase (EC 3.1.1.6), splits off acetyl groupsCholinesteraseAcetylcholinesterase, inactivates the neurotransmitter acetylcholine Pseudocholinesterase, broad substrate specificity, found in the blood plasma and in the liver Pectinesterase
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Enzyme Commission Number
The Enzyme
Enzyme
Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze.[1] As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme. Strictly speaking, EC numbers do not specify enzymes, but enzyme-catalyzed reactions
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Carboxylic Acid
A carboxylic acid /ˌkɑːrbɒkˈsɪlɪk/ is an organic compound that contains a carboxyl group (C(=O)OH).[1] The general formula of a carboxylic acid is R–COOH, with R referring to the rest of the (possibly quite large) molecule. Carboxylic acids occur widely and include the amino acids (which make up proteins) and acetic acid (which is part of vinegar and occurs in metabolism). Salts and esters of carboxylic acids are called carboxylates. When a carboxyl group is deprotonated, its conjugate base forms a carboxylate anion. Carboxylate
Carboxylate
ions are resonance-stabilized, and this increased stability makes carboxylic acids more acidic than alcohols
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Cholinesterase
In biochemistry, a cholinesterase or choline esterase is an esterase that lyses choline-based esters, several of which serve as neurotransmitters. Thus, it is either of two enzymes that catalyze the hydrolysis of these cholinergic neurotransmitters, such as breaking acetylcholine into choline and acetic acid. These reactions are necessary to allow a cholinergic neuron to return to its resting state after activation. For example, in muscle contraction, acetylcholine at a neuromuscular junction triggers a contraction; but for the muscle to relax afterward, rather than remaining locked in a tense state, the acetylcholine must be broken down by a choline esterase. The main type for that purpose is acetylcholinesterase (also called choline esterase I[1] or erythrocyte cholinesterase); it is found mainly in chemical synapses and red blood cell membranes
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Acetylcholinesterase
4EY7, 4PQE, 1F8U, 3LII, 4BDT, 4M0E, 4M0F, 1VZJ, 2X8B, 1B41, 4EY4, 4EY5, 4EY6, 4EY8, 5FOQ, 5HF9, 5HF6, 5FPQ, 5HF8, 5HFAIdentifiersAliases ACHE, AChE, acetylhydrolase, acetylcholinesterase (Yt blood group), ACEE, ARN-YT, acetylcholinesterase (Cartwright blood group), true cholinesterase (dated synonym)External IDs MGI: 87876 HomoloGene: 543 GeneCards: ACHEGene location (Human)Chr. Chromosome
Chromosome
7 (human)[1]Band 7q22.1 Start 100,889,994 bp[1]End 100,896,974 bp[1]Gene location (Mouse)Chr.
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Butyrylcholinesterase
1P0P, 4AXB, 4B0P, 2XQG, 1XLV, 2WIK, 2WIL, 1P0Q, 1XLU, 4BDS, 2XQF, 2PM8, 2XQK, 4AQD, 4BBZ, 2WID, 2XMB, 1XLW, 2XMC, 4TPK, 2XMG, 2XMD, 3DKK, 3O9M, 2WSL, 2WIJ, 1P0I, 2WIG, 2XQJ, 3DJY, 1P0M, 4B0O, 2XQI, 2Y1K, 4XII, 2WIF, 2J4CIdentifiersAliases BCHE, CHE1, CHE2, E1, butyrylcholinesteraseExternal IDs OMIM: 177400 MGI: 894278 HomoloGene: 20065 GeneCards: BCHE Gene
Gene
location (Human)Chr. Chro
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Pectinesterase
Pectinesterase
Pectinesterase
(PE) (EC 3.1.1.11) is a ubiquitous cell-wall-associated enzyme that presents several isoforms that facilitate plant cell wall modification and subsequent breakdown. It is found in all higher plants as well as in some bacteria and fungi. Pectinesterase
Pectinesterase
functions primarily by altering the localised pH of the cell wall resulting in alterations in cell wall integrity. Pectinesterase
Pectinesterase
catalyses the de-esterification of pectin into pectate and methanol. Pectin
Pectin
is one of the main components of the plant cell wall. In plants, pectinesterase plays an important role in cell wall metabolism during fruit ripening. In plant bacterial pathogens such as Erwinia carotovora
Erwinia carotovora
and in fungal pathogens such as Aspergillus niger, pectinesterase is involved in maceration and soft-rotting of plant tissue
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6-phosphogluconolactonase
6-Phosphogluconolactonase (6PGL, PGLS) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in the oxidative phase of the pentose phosphate pathway.[2] The tertiary structure of 6PGL employs an α/β hydrolase fold, with active site residues clustered on the loops of the α-helices
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PAF Acetylhydrolase
PAF acetylhydrolase is an enzyme that catabolizes platelet-activating factor
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Bile Salt-dependent Lipase
1F6W, 1JMYIdentifiersAliases CEL, BAL, BSDL, BSSL, CELL, CEase, FAP, FAPP, LIPA, MODY8, Bile salt-dependent lipase, carboxyl ester lipaseExternal IDs MGI: 88374 HomoloGene: 37529 GeneCards: CELGene location (Human)Chr. Chromosome
Chromosome
9 (human)[1]Band 9q34.13 Start 133,061,978 bp[1]End 133,071,861 bp[1]Gene location (Mouse)Chr. Chromosome
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PubMed Identifier
PubMed
PubMed
is a free search engine accessing primarily the MEDLINE database of references and abstracts on life sciences and biomedical topics. The United States National Library of Medicine
United States National Library of Medicine
(NLM) at the National Institutes of Health
National Institutes of Health
maintains the database as part of the Entrez
Entrez
system of information retrieval. From 1971 to 1997, MEDLINE online access to the MEDLARS Online computerized database primarily had been through institutional facilities, such as university libraries
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Gastric Lipase
Gastric lipase, also known as LIPF, is an enzymatic protein that, in humans, is encoded by the LIPF gene.[2][3]Contents1 Function 2 Clinical significance 3 Structure 4 References 5 External linksFunction[edit] Gastric lipase
Gastric lipase
is an acidic lipase secreted by the gastric chief cells in the fundic mucosa in the stomach. It has a pH optimum of 3–6. Gastric lipase, together with lingual lipase, comprise the two acidic lipases. These lipases, unlike alkaline lipases (such as pancreatic lipase), do not require bile acid or colipase for optimal enzymatic activity. Acidic lipases make up 30% of lipid hydrolysis occurring during digestion in the human adult, with gastric lipase contributing the most of the two acidic lipases
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