Hydrolases

Lipase is a class of enzymes that catalyzes the hydrolysis of fats. Some lipases display broad substrate scope including esters of cholesterol, phospholipids, and of lipid-soluble vitamins and sphingomyelinases; however, these are usually treated separately from "conventional" lipases. Unlike esterases, which function in water, lipases "are activated only when adsorbed to an oil–water interface". Lipases perform essential roles in digestion, transport and processing of dietary lipids in most, if not all, organisms.

In biochemistry, hydrolases constitute a class of enzymes that commonly function as biochemical catalysts that use water to break a chemical bond:

Papain, also known as papaya proteinase I, is a cysteine protease () enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea cundinamarcensis). It is the namesake member of the papain-like protease family.

In biochemistry, an esterase is a class of enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis (and as such, it is a type of hydrolase).

thumb|right|Phospholipase cleavage sites. An enzyme that displays both PLA1 and PLA2 activities is called a phospholipase B.

A diastase (; from Greek διάστασις, "separation") is any one of a group of enzymes that catalyses the breakdown of starch into maltose. For example, the diastase α-amylase degrades starch to a mixture of the disaccharide maltose; the trisaccharide maltotriose, which contains three α (1-4)-linked glucose residues; and oligosaccharides, known as dextrins, that contain the α (1-6)-linked glucose branches.

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.)

PETases are an esterase class of enzymes that catalyze the breakdown (via hydrolysis) of polyethylene terephthalate (PET) plastic to monomeric mono-2-hydroxyethyl terephthalate (MHET).

correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.

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

Arylsulfatase (EC 3.1.6.1, 'sulfatase, nitrocatechol sulfatase, phenolsulfatase, phenylsulfatase, p-nitrophenyl sulfatase, arylsulfohydrolase, 4-methylumbelliferyl sulfatase, estrogen sulfatase') is a type of sulfatase enzyme with systematic name aryl-sulfate sulfohydrolase. This enzyme catalyses the following chemical reaction

Fibrinolysin is an enzyme derived from plasma of bovine origin (plasmin) or extracted from cultures of certain bacteria. It is used locally only and exclusively together with the enzyme desoxyribonuclease (extracted from bovine pancreas). Fibrinolysin and desoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological Unit) fibrinolysin and 666 BUs desoxyribonuclease per gram.

Glucanases are enzymes that break down [glucans] polysaccharides via hydrolysis. The product of the hydrolysis reaction are smaller glucans, a linear or branched polysaccharide made of up to 1200 glucose monomers, linked by glycosidic bonds. Glucans are abundant in the endosperm cell walls of cereals such as barley, rye, sorghum, rice, and wheat. Glucanases are also referred to as lichenases, hydrolases, glycosidases, glycosyl hydrolases, and/or laminarinases. Many types of glucanases share similar amino acid sequences but vastly different substrates. Of the known endo-glucanases, 1,3-1,4-β-gl

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Isomaltase () is an enzyme that breaks the bonds linking saccharides, which cannot be broken by amylase or maltase. It digests polysaccharides at the alpha 1-6 linkages. Its substrate, alpha-limit dextrin, is a product of amylopectin digestion that retains its 1-6 linkage (its alpha 1-4 linkages having already been broken down by amylase). The product of the enzymatic digestion of alpha-limit dextrin by isomaltase is maltose.

Amidohydrolases (or amidases) are a type of hydrolase that acts upon amide bonds.

class of enzymes

Enkephalinases are enzymes that degrade endogenous enkephalin opioid peptides. They include: Aminopeptidase N (APN) Neutral endopeptidase (NEP) Dipeptidyl peptidase 3 (DPP3) Carboxypeptidase A6 (CPA6) Leucyl/cystinyl aminopeptidase (LNPEP) Angiotensin-converting enzyme (ACE)

Galactosidases are enzymes (glycoside hydrolases) that catalyze the hydrolysis of galactosides into monosaccharides.