EC 3.2.1

An amylase () is an enzyme that catalyses the hydrolysis of starch (Latin '''') into sugars. Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion. Foods that contain large amounts of starch but little sugar, such as rice and potatoes, may acquire a slightly sweet taste as they are chewed because amylase degrades some of their starch into sugar. The pancreas and salivary gland make amylase (alpha amylase) to hydrolyse dietary starch into disaccharides and trisaccharides which are converted by other enzymes to glucose to supply the

Lysozyme (, 'muramidase, N-acetylmuramide glycanhydrolase; systematic name peptidoglycan N-acetylmuramoylhydrolase') is an antimicrobial enzyme produced by animals that forms part of the innate immune system. It is a glycoside hydrolase that catalyzes the following process:

thumb|235 px|Neuraminidase (GH34) ribbon diagram. An analog of its neuraminic acid substrate, used as an inhibitor drug, is the small white and red molecule in the center. thumb|235 px|N-Acetylneuraminic acid Exo-α-sialidase (, sialidase, neuraminidase; systematic name acetylneuraminyl hydrolase) is a glycoside hydrolase that cleaves the glycosidic linkages of neuraminic acids:

α-Amylase is an enzyme (; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process:

thumb|Maltose thumb|Ligand (NAG) interactions in Maltase-Glucoamylase thumb|Interactions of oligosaccharides in Alpha-amylase Maltase is an informal name for a family of enzymes that catalyze the hydrolysis of disaccharide maltose into two simple sugars of glucose. Maltases are found in plants, bacteria, yeast, humans, and other vertebrates.

β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. Sucrose is a fructoside. Alternative names for β-fructofuranosidase include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, and acid invertase. The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertase is a glycoprotein that hydrolyses (cleaves) the non-red

Hyaluronidases are a family of enzymes that catalyse the degradation of hyaluronic acid. Karl Meyer classified these enzymes in 1971, into three distinct groups, a scheme based on the enzyme reaction products. The three main types of hyaluronidases are two classes of eukaryotic endoglycosidase hydrolases and a prokaryotic lyase-type of glycosidase.

class of enzymes

Chitinases (, chitodextrinase, 1,4-β-poly-N-acetylglucosaminidase, poly-β-glucosaminidase, β-1,4-poly-N-acetyl glucosamidinase, poly[1,4-(N-acetyl-β-D-glucosaminide)] glycanohydrolase, (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase; systematic name (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase) are hydrolytic enzymes that break down glycosidic bonds in chitin. They catalyse the following reaction:

Endo-1,4-β-xylanase (, systematic name 4-β-D-xylan xylanohydrolase) is any of a class of enzymes that degrade the linear polysaccharide xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls:

Sucrases are digestive enzymes that catalyze the hydrolysis of sucrose to its component monosaccharides, fructose and glucose. One form, sucrase-isomaltase, is secreted in the small intestine on the brush border. The enzyme invertase, which occurs more commonly in plants, fungi and bacteria, also hydrolyzes sucrose (and other fructosides) but by a different mechanism: it is a fructosidase, whereas sucrase is a glucosidase.

β-Galactosidase (EC 3.2.1.23, beta-gal or β-gal; systematic name β-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyzes hydrolysis of terminal non-reducing β-D-galactose residues in β-D-galactosides. (This enzyme digests many β-Galactosides, not just lactose. It is sometimes loosely referred to as lactase but that name is generally reserved for mammalian digestive enzymes that break down lactose specifically.)

Pectinases are a group of enzymes that breaks down pectin, a polysaccharide found in plant cell walls, through hydrolysis, transelimination and deesterification reactions. Commonly referred to as pectic enzymes, they include pectolyase, pectozyme, and polygalacturonase, one of the most studied and widely used commercial pectinases. It is useful because pectin is the jelly-like matrix which helps cement plant cells together and in which other cell wall components, such as cellulose fibrils, are embedded. Therefore, pectinase enzymes are commonly used in processes involving the degradation of pl

Disaccharidases are glycoside hydrolases, enzymes that break down certain types of sugars called disaccharides into simpler sugars called monosaccharides. In the human body, disaccharidases are made mostly in an area of the small intestine's wall called the brush border, making them members of the group of "brush border enzymes".

mammalian protein found in Homo sapiens

Iduronidase (, L-iduronidase, α-L-iduronidase, laronidase), sold as Aldurazyme, is an enzyme with the systematic name glycosaminoglycan α-L-iduronohydrolase. It catalyses the hydrolysis of unsulfated α-L-iduronosidic linkages in dermatan sulfate.

β-Glucosidase (; systematic name β-D-glucoside glucohydrolase) is an enzyme that catalyses the following reaction: Hydrolysis of terminal, non-reducing β-D-glucosyl residues with release of β-D-glucose

Pullulanase (, limit dextrinase, amylopectin 6-glucanohydrolase, bacterial debranching enzyme, debranching enzyme, α-dextrin endo-1,6-α-glucosidase, R-enzyme, pullulan α-1,6-glucanohydrolase) is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan. It is produced as an extracellular, cell surface-anchored lipoprotein by Gram-negative bacteria of the genus Klebsiella. Type I pullulanases specifically attack α-1,6 linkages, while type II pullulanases are also able to hydrolyse α-1,4 linkages. It is also produced by some other bacteria and archaea. Pullulanase is used as

β-Glucocerebrosidase (also called acid β-glucosidase, D-glucosyl-N-acylsphingosine glucohydrolase, or GCase) is an enzyme with glucosylceramidase activity () that cleaves by hydrolysis the β-glycosidic linkage of the chemical glucocerebroside, an intermediate in glycolipid metabolism that is abundant in cell membranes (particularly skin cells). It is localized in the lysosome, where it remains associated with the lysosomal membrane. β-Glucocerebrosidase is 497 amino acids in length and has a molecular mass of 59,700 Da.

Myrosinase (, thioglucoside glucohydrolase, sinigrinase, and sinigrase) is a family of enzymes involved in plant defense against herbivores, specifically the mustard oil bomb. The three-dimensional structure has been elucidated and is available in the PDB (see links in the infobox).

α-Galactosidase ( EC 3.2.1.22, α-GAL, α-GAL A; systematic name α-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyses the following reaction:

thumb|Beta-amylase, a type of glucosidase Glucosidases are the glycoside hydrolase enzymes categorized under the EC number 3.2.1.

β-Mannosidase (}, mannanase, mannase, β-D-mannosidase, β-mannoside mannohydrolase, exo-β-D-mannanase, lysosomal β A mannosidase) is an enzyme with systematic name β-D-mannoside mannohydrolase, which is in humans encoded by the MANBA gene. This enzyme catalyses the following chemical reaction

mammalian protein found in Homo sapiens

chemical compound

Galactosylceramidase (or galactocerebrosidase), , is an enzyme that removes galactose from ceramide derivatives (galactosylceramides) by catalysing the hydrolysis of galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride.

Inulinase ( and , inulase, endoinulinase, endo-inulinase, exoinulinase, 2,1-β-D-fructan fructanohydrolase) is an enzyme with systematic name 1-β-D-fructan fructanohydrolase.

β-Glucuronidases are members of the glycosidase family of enzymes that catalyze breakdown of complex carbohydrates. Human β-glucuronidase is a type of glucuronidase (a member of glycosidase Family 2) that catalyzes hydrolysis of β-D-glucuronic acid residues from the non-reducing end of mucopolysaccharides (also referred to as glycosaminoglycans) such as heparan sulfate. Human β-glucuronidase is located in the lysosome. In the gut, brush border β-glucuronidase converts conjugated bilirubin to the unconjugated form for reabsorption. β-Glucuronidase is also present in breast milk, which contribut

thumb|300px|Glycogen structure segment. thumb|300px|Maltose

InterPro Family

β-Amylase (, saccharogen amylase, glycogenase) is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It catalyses the following reaction:

thumb|Cartoon depiction of the protein Streptococcus pyogenes family GH38 α-Mannosidase created using PyMol.

Endo-polygalacturonase (, pectin depolymerase, pectolase, pectin hydrolase, and poly-α-1,4-galacturonide glycanohydrolase; systematic name (1→4)-α-D-galacturonan glycanohydrolase (endo-cleaving)) is an enzyme that hydrolyzes the α-1,4 glycosidic bonds between galacturonic acid residues:

class of enzymes

Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by host bacteria when infected with bacteriophages in order to cleave the cell wall during the final stage of the lytic cycle to release the viral particles. Lysins are highly evolved enzymes that are able to target one of the five bonds in peptidoglycan (murein), the main component of bacterial cell walls, which allows the release of progeny virions from the lysed cell. Cell-wall-containing Archaea are also lysed by specialized pseudomurein-cleaving lysins, while most archaeal viruses employ alternative mec

Trehalase enzymes are hydrolytic glycosidases, produced by most forms of life (except mammals), which catalyze the reduction of trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) - a non-reducing sugar and important storage carbohydrate - into glucose.

Dextranase (, dextran hydrolase, endodextranase, dextranase DL 2, DL 2, endo-dextranase, α-D-1,6-glucan-6-glucanohydrolase, 1,6-α-D-glucan 6-glucanohydrolase) is an enzyme with systematic name 6-α-D-glucan 6-glucanohydrolase. It catalyses the following chemical reaction

Sacrosidase (trade name Sucraid) is a medication used to replace sucrase in people lacking this enzyme. It is available as an oral solution. Sucraid is approved by the U.S. Food and Drug Administration (FDA) for the therapy of the genetically determined sucrase deficiency that is part of the Congenital Sucrase-Isomaltase Deficiency (CSID). Sacrosidase assists in the breakdown of sugar/sucrose into simpler forms and is useful for the relief of gastrointestinal symptoms that are associated with CSID.

Isoamylase (, debranching enzyme, glycogen α-1,6-glucanohydrolase) is an enzyme with systematic name glycogen 6-α-D-glucanohydrolase. It catalyses the hydrolysis of (1→6)-α-D-glucosidic branch linkages in glycogen, amylopectin and their β-limit dextrins. It also readily hydrolyses amylopectin.

'α-N-acetylgalactosaminidase () is a glycoside hydrolase from bacteria and animals, also known as nagalase'.

protein-coding gene in the species Homo sapiens

The enzyme α-L-fucosidase () catalyzes the following chemical reaction: an α-L-fucoside + H2O \rightleftharpoons L-fucose + an alcohol

For beta-glucuronidase, see Beta-glucuronidase

Sucrase-isomaltase is a bifunctional glucosidase (sugar-digesting enzyme) located on the brush border of the small intestine, encoded by the human gene SI. It is a dual-function enzyme with two GH31 domains, one serving as the isomaltase, the other as a sucrose alpha-glucosidase. It has preferential expression in the apical membranes of enterocytes. The enzyme's purpose is to digest dietary carbohydrates such as starch, sucrose and isomaltose. By further processing the broken-down products, energy in the form of ATP can be generated.

class of enzymes

In enzymology, a glucosylceramidase () is an enzyme that catalyzes the chemical reaction

class of enzymes

Hexosaminidase (, β-acetylaminodeoxyhexosidase, N-acetyl-β-D-hexosaminidase, N-acetyl-β-hexosaminidase, N-acetyl hexosaminidase, β-hexosaminidase, β-acetylhexosaminidinase, β-D-N-acetylhexosaminidase, β-N-acetyl-D-hexosaminidase, β-N-acetylglucosaminidase, hexosaminidase A, N-acetylhexosaminidase, β-D-hexosaminidase) is an enzyme involved in the hydrolysis of terminal N-acetyl-D-hexosamine residues in N-acetyl-β-D-hexosaminides.

Levanase (, levan hydrolase, 2,6-β-D-fructan fructanohydrolase) is an enzyme with systematic name (2→6)-β-D-fructan fructanohydrolase. This enzyme catalyses the following chemical reaction

α-L-Rhamnosidase (, α-L-rhamnosidase T, α-L-rhamnosidase N) is an enzyme with systematic name α-L-rhamnoside rhamnohydrolase. This enzyme catalyses the following chemical reaction

class of enzymes

protein-coding gene in the species Homo sapiens

class of enzymes