The 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 corresponding enzyme-catalyzed reaction.
EC numbers do not specify enzymes but enzyme-catalyzed reactions. If different enzymes (for instance from different organisms) catalyze the same reaction, then they receive the same EC number. [2] Furthermore, through convergent evolution, completely different protein folds can catalyze an identical reaction (these are sometimes called non-homologous isofunctional enzymes) [3] and therefore would be assigned the same EC number. By contrast, UniProt identifiers uniquely specify a protein by its amino acid sequence. [4]
Every enzyme code consists of the letters "EC" followed by four numbers separated by periods. Those numbers represent a progressively finer classification of the enzyme. Preliminary EC numbers exist and have an 'n' as part of the fourth (serial) digit (e.g. EC 3.5.1.n3). [2]
For example, the tripeptide aminopeptidases have the code "EC 3.4.11.4", whose components indicate the following groups of enzymes:
NB:The enzyme classification number is different from the 'FORMAT NUMBER'
Class | Reaction catalyzed | Typical reaction | Enzyme example(s) with trivial name |
---|---|---|---|
EC 1 Oxidoreductases | Oxidation/reduction reactions; transfer of H and O atoms or electrons from one substance to another | AH + B → A + BH (reduced) A + O → AO (oxidized) | Dehydrogenase, oxidase |
EC 2 Transferases | Transfer of a functional group from one substance to another. The group may be methyl-, acyl-, amino- or phosphate group | AB + C → A + BC | Transaminase, kinase |
EC 3 Hydrolases | Formation of two products from a substrate by hydrolysis | AB + H2O → AOH + BH | Lipase, amylase, peptidase, phosphatase |
EC 4 Lyases | Non-hydrolytic addition or removal of groups from substrates. C-C, C-N, C-O or C-S bonds may be cleaved | RCOCOOH → RCOH + CO2 or [X-A+B-Y] → [A=B + X-Y] | Decarboxylase |
EC 5 Isomerases | Intramolecule rearrangement, i.e. isomerization changes within a single molecule | ABC → BCA | Isomerase, mutase |
EC 6 Ligases | Join together two molecules by synthesis of new C-O, C-S, C-N or C-C bonds with simultaneous breakdown of ATP | X + Y + ATP → XY + ADP + Pi | Synthetase |
EC 7 Translocases | Catalyse the movement of ions or molecules across membranes or their separation within membranes | Transporter |
Similarity between enzymatic reactions can be calculated by using bond changes, reaction centres or substructure metrics (formerly EC-BLAST], now the EMBL-EBI Enzyme Portal). [6]
Before the development of the EC number system, enzymes were named in an arbitrary fashion, and names like old yellow enzyme and malic enzyme that give little or no clue as to what reaction was catalyzed were in common use. Most of these names have fallen into disuse, though a few, especially proteolyic enzymes with very low specificity, such as pepsin and papain, are still used, as rational classification on the basis of specificity has been very difficult.
By the 1950s the chaos was becoming intolerable, and after Hoffman-Ostenhof [7] and Dixon and Webb [8] had proposed somewhat similar schemes for classifying enzyme-catalyzed reactions, the International Congress of Biochemistry in Brussels set up the Commission on Enzymes under the chairmanship of Malcolm Dixon in 1955. The first version was published in 1961, and the Enzyme Commission was dissolved at that time, though its name lives on in the term EC Number. The current sixth edition, published by the International Union of Biochemistry and Molecular Biology in 1992 as the last version published as a printed book, contains 3196 different enzymes. Supplements 1-4 were published 1993–1999. Subsequent supplements have been published electronically, at the website of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. [5] In August 2018, the IUBMB modified the system by adding the top-level EC 7 category containing translocases. [9]
Enzymes are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called enzymology and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties.
In biochemistry, isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed. The general form of such a reaction is as follows:
In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.
In molecular biology, phosphotransferases are proteins in the transferase family of enzymes that catalyze certain chemical reactions. The general form of the phosphorylation reactions they catalyze is:
BRENDA is an information system representing one of the most comprehensive enzyme repositories. It is an electronic resource that comprises molecular and biochemical information on enzymes that have been classified by the IUBMB. Every classified enzyme is characterized with respect to its catalyzed biochemical reaction. Kinetic properties of the corresponding reactants are described in detail. BRENDA contains enzyme-specific data manually extracted from primary scientific literature and additional data derived from automatic information retrieval methods such as text mining. It provides a web-based user interface that allows a convenient and sophisticated access to the data.
The International Union of Biochemistry and Molecular Biology (IUBMB) is an international non-governmental organisation concerned with biochemistry and molecular biology. Formed in 1955 as the International Union of Biochemistry (IUB), the union has presently 79 member countries and regions. The Union is devoted to promoting research and education in biochemistry and molecular biology throughout the world, and gives particular attention to localities where the subject is still in its early development.
Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN−) by converting it to thiocyanate. In enzymatology, the common name is listed as thiosulfate sulfurtransferase. The diagram on the right shows the crystallographically-determined structure of rhodanese.
Translocase is a general term for a protein that assists in moving another molecule, usually across a cell membrane. These enzymes catalyze the movement of ions or molecules across membranes or their separation within membranes. The reaction is designated as a transfer from “side 1” to “side 2” because the designations “in” and “out”, which had previously been used, can be ambiguous. Translocases are the most common secretion system in Gram positive bacteria.
In enzymology, a D-xylulose reductase (EC 1.1.1.9) is an enzyme that is classified as an Oxidoreductase (EC 1) specifically acting on the CH-OH group of donors (EC 1.1.1) that uses NAD+ or NADP+ as an acceptor (EC 1.1.1.9). This enzyme participates in pentose and glucuronate interconversions; a set of metabolic pathways that involve converting pentose sugars and glucuronate into other compounds.
Leukotriene-A4 hydrolase is an enzyme that catalyzes the reaction which converts Leukotriene A4 to Leukotriene B4. It is a bifunctional zinc enzyme with different amino acids attached to it to aid in the catalysis of the reaction. It also acts as an aminopeptidase. Leukotriene-A4 hydrolase is a cytosolic protein and is found in almost all mammalian cells, tissues and organelles that have been examined.
Malcolm Dixon was a British biochemist.
The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:
In enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction
In molecular biology, glycoside hydrolase family 36 is a family of glycoside hydrolases.
Lysine carboxypeptidase is an enzyme. This enzyme catalyses the following chemical reaction:
Non-Homologous Isofunctional Enzymes (NISE) are two evolutionarily unrelated enzymes that catalyze the same chemical reaction. Enzymes that catalyze the same reaction are sometimes referred to as analogous as opposed to homologous, however it is more appropriate to name them as Non-homologous Isofunctional Enzymes, hence the acronym (NISE). These enzymes all serve the same end function but do so in different organisms without detectable similarity in primary and possibly tertiary structures.
L-ornithine N5 monooxygenase (EC 1.14.13.195 or EC 1.14.13.196) is an enzyme which catalyzes one of the following chemical reactions:
L-ornithine + NADPH + O2 N(5)-hydroxy-L-ornithine + NADP+ + H2O L-ornithine + NAD(P)H + O2 N(5)-hydroxy-L-ornithine + NAD(P)+ + H2O
Edwin Clifford Webb was a British biochemist.
N-acetyl-β-d-glucosaminidase(EC 3.2.1.30; EC 3.2.1.52) is a mesophilic hydrolase that specifically hydrolyzes N-acetyl-glucosides. The enzyme is found across a wide variety of marine and terrestrial creatures with the primary function of breaking down oligosaccharides in the presence of water. One of the primary functions of the enzyme is to target and hydrolyze oligosaccharides containing chitin. In this chitinase function, the enzyme contributes to the ability of many organisms to break down chitin-containing molecules and subsequently digest or re-uptake environmental chitin, carbon, or nitrogen. The enzyme's crystal structure varies slightly across organisms, but is characterized by three or four domains with one active site. Across proteins, the active site entails an α-β barrel with either an arginine or tryptophan residues in the barrel pocket to bind incoming substrate.