List of enzymes

Last updated

Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system:

Contents

Category:Oxidoreductases (EC 1) (Oxidoreductase)

Category:EC 1.1 (act on the CH-OH group of donors)

Category:EC 1.2 (act on the aldehyde or oxo group of donors)

Category:EC 1.3 (act on the CH-CH group of donors)

Category:EC 1.4 (act on the CH-NH2 group of donors)

Category:EC 1.5 (act on CH-NH group of donors)

Category:EC 1.6 (act on NADH or NADPH)

Category:EC 1.7 (act on other nitrogenous compounds as donors)

Category:EC 1.8 (act on a sulfur group of donors)

Category:EC 1.9 (act on a heme group of donors)

Category:EC 1.11 (act on peroxide as an acceptor -- peroxidases)

Category:EC 1.12 (act on hydrogen as a donor)

Category:EC 1.13 (act on single donors with incorporation of molecular oxygen)

Category:EC 1.14 (act on paired donors with incorporation of molecular oxygen)

Category:EC 1.15 (act on superoxide radicals as acceptors)

Category:EC 1.16 (oxidize metal ions)

Category:EC 1.17 (act on CH or CH2 groups)

Category:EC 1.18 (act on iron–sulfur proteins as donors)

Category:EC 1.19 (act on reduced flavodoxin as donor)

Category:EC 1.20 (act on phosphorus or arsenic as donors)

Category:EC 1.21 (act on X-H and Y-H to form an X-Y bond)

Category:EC 1.97 (other oxidoreductases)

Category:Transferases (EC 2) (Transferase)

Category:EC 2.1 (transfer one-carbon groups, Methylase)

Category:EC 2.2 (transfer aldehyde or ketone groups)

Category:EC 2.3 (acyltransferases)

Category:EC 2.4 (glycosyltransferases)

Category:EC 2.5

Category:EC 2.5 (transfer alkyl or aryl groups, other than methyl groups)

Category:EC 2.6 (transfer nitrogenous groups)

Category:EC 2.7 (transfer phosphorus-containing groups)

Category:EC 2.8 (transfer sulfur-containing groups)

Category:EC 2.9 (transfer selenium-containing groups)

Category:Hydrolases (EC 3) (Hydrolase)

Category:EC 3.1 (act on ester bonds)

Category:EC 3.2 (act on sugars - glycosylases)

Function and clinical importance of some enzymes in category 3.2.1

Amylase

Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb.

Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is Sollpura (liprotamase), which help in the breakdown of saccharides into simple sugars.

Lysozyme

Function: An enzyme that is produced by animals that forms part of the innate immune system and is abundant in the secretions of saliva, human milk, tears, and mucus. It functions as an antimicrobial agent by splitting the peptidoglycan component of bacterial cell walls, which then leads to cell death.

Clinical Significance: Toxic levels of blood are caused by the excessive production of lysozyme's by cancer cells. Lysozyme's have also been associated with Bronchopulmonary dysplasia (BPD) in newborns and is a key factor in providing the immunology of infants during breast feeding.

Sucrase

Function: Sucrase is a stomachs related protein that mobilizes hydrolysis to convert sucrose into glucose and fructose.

Clinical Significance: Low amounts of Sucrose also known as Sucrose intolerance happens when sucrose isn't being discharged in the small digestive tract. A result of this is extra gas.

Lactase

Function: lactase is located in the small digestives system of people and other creatures such as mammals. Lactase is the bases of the total absorption of milk.

Clinical Significance: People who are lactose intolerant have medicine that can help with the digestion. When you are lactose intolerant you might experience gas, bloating, and pain along with other symptoms regarding your digestive system.

Category:EC 3.3 (act on ether bonds)

Category:EC 3.4 (act on peptide bonds - Peptidase)

Category:EC 3.5 (act on carbon–nitrogen bonds, other than peptide bonds)

Category:EC 3.6 (act on acid anhydrides)

Category:EC 3.7 (act on carbon–carbon bonds)

Category:EC 3.8 (act on halide bonds)

Category:EC 3.9 (act on phosphorus–nitrogen bonds)

Category:EC 3.10 (act on sulfur–nitrogen bonds)

Category:EC 3.11 (act on carbon–phosphorus bonds)

Category:EC 3.12 (act on sulfur–sulfur bonds)

Category:EC 3.13 (act on carbon–sulfur bonds)

Category:Lyases (EC 4) (Lyase)

Category:EC 4.1 (carbon–carbon lyases)

Category:EC 4.2 (carbon–oxygen lyases)

Category:EC 4.3 (carbon–nitrogen lyases)

Category:EC 4.4 (carbon–sulfur lyases)

Category:EC 4.5 (carbon–halide lyases)

Category:EC 4.6 (phosphorus–oxygen lyases)

Category:Isomerases (EC 5) (Isomerase)

Category:EC 5.1 (racemases and epimerases)

Category:EC 5.2 (cis-trans-isomerases)

Category:EC 5.3 (intramolecular oxidoreductases)

Category:EC 5.4 (intramolecular transferases -- mutases)

Category:EC 5.5 (intramolecular lyases)

Intramolecular lyases:
EC numberExamples
EC 5.5.1.1 Muconate cycloisomerase
EC 5.5.1.2 3-carboxy-cis,cis-muconate cycloisomerase
EC 5.5.1.3 Tetrahydroxypteridine cycloisomerase
EC 5.5.1.4 Inositol-3-phosphate synthase
EC 5.5.1.5 Carboxy-cis,cis-muconate cyclase
EC 5.5.1.6 Chalcone isomerase
EC 5.5.1.7 Chloromuconate cycloisomerase
EC 5.5.1.8 (+)-bornyl diphosphate synthase
EC 5.5.1.9 Cycloeucalenol cycloisomerase
EC 5.5.1.10 Alpha-pinene-oxide decyclase
EC 5.5.1.11 Dichloromuconate cycloisomerase
EC 5.5.1.12 Copalyl diphosphate synthase
EC 5.5.1.13 Ent-copalyl diphosphate synthase
EC 5.5.1.14 Syn-copalyl-diphosphate synthase
EC 5.5.1.15 Terpentedienyl-diphosphate synthase
EC 5.5.1.16 Halimadienyl-diphosphate synthase
EC 5.5.1.17 (S)-beta-macrocarpene synthase
EC 5.5.1.18 Lycopene epsilon-cyclase
EC 5.5.1.19 Lycopene beta-cyclase
EC 5.5.1.20 Prosolanapyrone-III cycloisomerase
EC 5.5.1.n1 D-ribose pyranase
EC 5.5.1.22 Steroid Delta Isomerase

Category:EC 5.99 (other isomerases)

Category:Ligases (EC 6) (Ligase)

Category:EC 6.1 (form carbon–oxygen bonds)

6-carboxytetrahydropterin synthase

Category:EC 6.2 (form carbon–sulfur bonds)

Category:EC 6.3 (form carbon–nitrogen bonds)

Category:EC 6.4 (form carbon–carbon bonds)

Category:EC 6.5 (form phosphoric ester bonds)

Category:EC 6.6 (form nitrogen–metal bonds)

Other list of enzymes

Related Research Articles

<span class="mw-page-title-main">Oxidative phosphorylation</span> Metabolic pathway

Oxidative phosphorylation or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.

A dehydrogenase is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Like all catalysts, they catalyze reverse as well as forward reactions, and in some cases this has physiological significance: for example, alcohol dehydrogenase catalyzes the oxidation of ethanol to acetaldehyde in animals, but in yeast it catalyzes the production of ethanol from acetaldehyde.

An electron transport chain (ETC) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. Many of the enzymes in the electron transport chain are embedded within the membrane.

A proton pump is an integral membrane protein pump that builds up a proton gradient across a biological membrane. Proton pumps catalyze the following reaction:

In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide phosphate</span> Chemical compound

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP+ is the oxidized form. NADP+ is used by all forms of cellular life.

This is a list of topics in molecular biology. See also index of biochemistry articles.

<span class="mw-page-title-main">Flavin adenine dinucleotide</span> Redox-active coenzyme

In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex.

<span class="mw-page-title-main">Flavoprotein</span> Protein family

Flavoproteins are proteins that contain a nucleic acid derivative of riboflavin. These proteins are involved in a wide array of biological processes, including removal of radicals contributing to oxidative stress, photosynthesis, and DNA repair. The flavoproteins are some of the most-studied families of enzymes.

Carbohydrate dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms and facilitate the conversion from a carbohydrate to an aldehyde, lactone, or ketose.

<span class="mw-page-title-main">Saccharopine dehydrogenase</span>

In molecular biology, the protein domain Saccharopine dehydrogenase (SDH), also named Saccharopine reductase, is an enzyme involved in the metabolism of the amino acid lysine, via an intermediate substance called saccharopine. The Saccharopine dehydrogenase enzyme can be classified under EC 1.5.1.7, EC 1.5.1.8, EC 1.5.1.9, and EC 1.5.1.10. It has an important function in lysine metabolism and catalyses a reaction in the alpha-Aminoadipic acid pathway. This pathway is unique to fungal organisms therefore, this molecule could be useful in the search for new antibiotics. This protein family also includes saccharopine dehydrogenase and homospermidine synthase. It is found in prokaryotes, eukaryotes and archaea.

<span class="mw-page-title-main">Formate dehydrogenase</span>

Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.17.1.9) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1). This family of enzymes has attracted attention as inspiration or guidance on methods for the carbon dioxide fixation, relevant to global warming.

<span class="mw-page-title-main">D-xylulose reductase</span>

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.

<span class="mw-page-title-main">Methanol dehydrogenase</span>

In enzymology, a methanol dehydrogenase (MDH) is an enzyme that catalyzes the chemical reaction:

In enzymology, a glycine dehydrogenase (EC 1.4.1.10) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Pyrroline-5-carboxylate reductase</span>

In enzymology, a pyrroline-5-carboxylate reductase (EC 1.5.1.2) is an enzyme that catalyzes the chemical reaction