Hydrolases

Acid Hydrolases

Acid hydrolases are enzymes that break down acids.In the presence of acid, hydrolases are enzymes that perform their best when the pH is low. It’s most typically found in lysosomes, which have an acidic interior, which is where it gets its name. Acid hydrolases comprise nucleases, proteases, glycosidases, lipases, phosphatases, sulfatases, and phospholipases, and they account for around 50 of the lysosome’s degradative enzymes. Nucleases are the most abundant acid hydrolases.

Hydrolases are used in the following examples:

• Nucleases
• Lipase is a type of enzyme that includes, for example, lysosomal acid lipase.
• Proteases

• Glycoside hydrolase is a type of enzyme that breaks down glycosides.

Hydrolase of Glycosides

Glycoside hydrolases are enzymes that catalyze the hydrolysis of glycosidic bonds in complex sugars (also known as glycosidases or glycosyl hydrolases). In nature, they perform a wide range of functions, including the degradation of cellulose (cellulase), hemicellulose (hemicellulose), and starch (amylase), antibacterial protection strategies (such as lysozyme), pathogenesis mechanisms (such as viral neuraminidases), and normal cellular function (such as lysozyme) (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). A group of enzymes known as glycosidases, which work in conjunction with glycosyltransferases, are responsible for the formation and breakdown of glycosidic linkages in the body.

Enzyme for hydrolysis of epoxide

A dihydroxylation reaction occurs when an epoxide residue is present, and the resultant products are diol compounds. Epoxide hydrolases (EHs) are enzymes that metabolize compounds containing an epoxide residue, converting it to two hydroxylation residues through a dihydroxylation reaction, resulting in the formation of diol products. Enzymes with EH activity can be discovered in a wide range of organisms. Microsomal epoxide hydrolase (mEH), soluble epoxide hydrolase (sEH, epoxide hydrolase 2, EH2, or cytoplasmic epoxide hydrolase), and the more recently discovered but not yet well defined functionally, epoxide hydrolase 3 (EH3) and epoxide hydrolase 4 (EH4) are all physically related isozymes (EH4).

Lysosomal Hydrolase

It  is a type of hydrolase found in the lysosomes of cells.It is important to note that lipase acts within the cell, namely in the lysosomal compartment. The primary function of lysosomal lipase is to hydrolyze lipids, such as triglycerides and cholesterol, in the body. These lipids are transported throughout the body and degraded into free fatty acids. Lysosomal lipases function best when the pH is in the acidic range, which is compatible with the acidic pH of the lysosomal lumen. It was previously believed that these enzymes were only capable of hydrolyzing lipids found in organelle membranes and extracellular lipids.

Serine Hydrolase 

It is a type of enzyme that breaks down serine.Serine hydrolases are one of the most abundant known enzyme classes, accounting for around 200 enzymes or 1% of the genes in the human proteome, according to the National Institutes of Health. The presence of a nucleophilic serine in the active site, which is responsible for substrate hydrolysis, distinguishes these enzymes from other enzymes of the same kind. Catalysis begins with the creation of an acyl-enzyme intermediate, which is followed by saponification of the intermediate by water or hydrogen peroxide and regeneration of the enzyme through the action of this serine. Although there are variations on this mechanism, the nucleophilic serine of these hydrolases, in contrast to other non-catalytic serines, is normally activated by a proton relay involving a catalytic triad composed of the serine, an acidic residue (e.g., aspartate or glutamate), and a simple residue (usually histidine).

Cholesterol Ester Hydrolase is a protein that breaks down cholesterol.

In the field of enzymology, a sterol esterase is an enzyme that catalyses the chemical reaction.

H2O sterol + sterol ester + fatty acid = sterol ester + fatty acid

Consequently, the enzyme’s two substrates are sterol ester and water, while the enzyme’s two products are sterol and fatty acid.

Bile Salt Hydrolase

It  is a type of enzyme that breaks down bile salts.BSH is produced by intestinal bacteria, and it is responsible for the deconjugation of glyco- and Tauro-conjugated bile acids by hydrolyzing the amide link, releasing free bile acids (e.g., cholic acid and chenodeoxycholic acid) and amino acids (e.g., glycine) (glycine and taurine).

Epoxide Hydrolase 

The soluble epoxide hydrolase (EPHX2) gene provides instructions for making a bifunctional enzyme (sEH). The enzyme sEH belongs to the epoxide hydrolase family. Several different epoxides are bound by this enzyme, which converts them into the corresponding diols in the cytosol and peroxisomes. In addition, this protein possesses lipid-phosphate phosphatase activity in another region of the body. Mutations in the EPHX2 gene have been found to be associated with familial hypercholesterolemia.

Alpha-beta Hydrolase 

It is a type of enzyme that helps to break down proteins.This superfamily of hydrolytic enzymes has a similar fold but differing evolutionary origins and catalytic roles. Alpha and beta hydrolases are two of the most common hydrolytic enzymes found in the body. Each enzyme is made up of an alpha/beta-sheet (rather than a barrel), which has 8 beta strands that are joined together by 6 alpha helices in the middle. Although the enzymes are considered to have split from a common ancestor, they have maintained little apparent sequence similarity while retaining the structure of the catalytic residues. It is common to all of them that they contain an active triad, the components of which are carried around on loops, which are among the fold’s most well-preserved structural traits.

Nudix Hydrolase

It  is an enzyme that breaks down nudix.The hydrolytic enzymes known as nudix hydrolases are a class of hydrolytic enzymes that may hydrolyze nucleoside diphosphates attached to any moiety, hence its name. The nucleoside monophosphate (NMP) and X-P that are formed as a result of the reaction are the products. Nudix enzymes hydrolyze a wide range of organic pyrophosphates, including nucleoside bi- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars, and RNA caps, each with a different degree of substrate specificity. Other than eukaryotes and bacteria, the Nudix superfamily of enzymes can be found in archaea and bacteria as well as other organisms.

Bleomycin Hydrolase 

Bleomycin hydrolase (BMH) is a cysteine peptidase found in the cytoplasm of cells with a long evolutionary history. The biological function of homocysteine thiolactone is the hydrolysis of the reactive electrophile homocysteine. An additional function of this compound is the metabolic inactivation of the glycopeptide bleomycin (BLM), which is a critical component of cancer treatment regimens. The protein has active site residues that are indicative of the cysteine protease papain superfamily.

Conclusion

Acetylcholinesterase is one of the most frequent hydrolases found in the human body (cholinesterase). Acetylcholine is a strong neurotransmitter that is involved in the contraction of voluntary muscles. Neuropathic pain is caused by nerve impulses passing through neurons and into the synaptic cleft, where acetylcholine held in vesicles is released, spreading the impulse via the synapse and to the postsynaptic neuron. After the nerve impulse has passed, the enzyme cholinesterase, which hydrolyzes acetylcholine to choline and acetic acid, must be activated in order to prevent the neurotransmitter molecules from continuing to function. Cholinesterase is a protein that interacts with a variety of deadly toxins, including exotoxins and saxitoxins produced by Clostridium botulinum. Many nerve agents, like tabun and sarin, work by binding to cholinesterase to cause their effects.