prospec

Hydrolase

  • Name
  • Description
  • Pricings
  • Quantity
  • ABHD10 Human
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  • Abhydrolase Domain Containing 10 Human Recombinant
  • Shipped with Ice Packs
  • ABHD14B Human
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  • Abhydrolase Domain Containing 14B Human Recombinant
  • Shipped with Ice Packs
  • ACY1 Human
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  • Aminoacylase-1 Human Recombinant
  • Shipped with Ice Packs
  • ACY1 Mouse
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  • AminoAcylase-1 Mouse Recombinant
  • Shipped with Ice Packs
  • ADPRH Human
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  • ADP-Ribosylarginine Hydrolase Human Recombinant
  • Shipped with Ice Packs
  • ADPRHL2 Human
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  • ADP-Ribosylhydrolase Like 2 Human Recombinant
  • Shipped with Ice Packs
  • BLMH Human
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  • BLM Hydrolase Human Recombinant
  • Shipped with Ice Packs
  • BPHL Human
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  • Biphenyl Hydrolase-Like Human Recombinant
  • Shipped with Ice Packs
  • DDAH1 Human
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  • Dimethylarginine Dimethylaminohydrolase 1 Human Recombinant
  • Shipped with Ice Packs
  • ENTPD3 Human
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  • Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant
  • Shipped with Ice Packs
  • ENTPD3 Human, sf9
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  • Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9
  • Shipped with Ice Packs
  • ENTPD3 Human, sf9 Bioactive
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  • Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive
  • Shipped with Ice Packs
  • EPHX1 Human
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  • Epoxide Hydrolase 1 Microsomal Human Recombinant
  • Shipped with Ice Packs
  • EPHX1 Human, Sf9
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  • Epoxide Hydrolase 1 Microsomal Human Recombinant, sf9
  • Shipped with Ice Packs
  • FAAH2 Human
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  • Fatty Acid Amide Hydrolase 2 Human Recombinant
  • Shipped with Ice Packs
  • FAHD1 Human
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  • Fumarylacetoacetate Hydrolase Domain Containing 1 Human Recombinant
  • Shipped with Ice Packs
  • FOLH1 Mouse
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  • Folate Hydrolase 1 Mouse Recombinant
  • Shipped with Ice Packs
  • FUCA1 Human
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  • Fucosidase Alpha-L- 1 Plasma Human Recombinant
  • Shipped with Ice Packs
  • FUCA2 Human
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  • Fucosidase Alpha-L- 2 Plasma Human Recombinant
  • Shipped with Ice Packs
  • GGH Human
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  • Gamma-Glutamyl Hydrolase Human Recombinant
  • Shipped with Ice Packs
  • HAGH Human
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  • Hydroxyacylglutathione Hydrolase Human Recombinant
  • Shipped with Ice Packs
  • HDDC3 Human
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  • HD domain containing 3 Human Recombinant
  • Shipped with Ice Packs
  • HDHD1 Human
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  • Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 Human Recombinant
  • Shipped with Ice Packs
  • HDHD2 Human
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  • Haloacid Dehalogenase-Like Hydrolase Domain Containing 2 Human Recombinant
  • Shipped with Ice Packs
  • HDHD3 Human
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  • Haloacid Dehalogenase-Like Hydrolase Domain Containing 3 Human Recombinant
  • Shipped with Ice Packs
  • HIBCH Human
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  • 3-Hydroxyisobutyryl-CoA Hydrolase Human Recombinant
  • Shipped with Ice Packs
  • LTA4H Human
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  • Leukotriene A4 Hydrolase Human Recombinant
  • Shipped with Ice Packs
  • PAFAH1B3 Human
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  • Platelet-activating Factor Acetylhydrolase 1b, Catalytic Subunit 3 Human Recombinant
  • Shipped with Ice Packs
  • PAFAH2 Human
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  • Platelet-Activating Factor Acetylhydrolase 2 Human Recombinant
  • Shipped with Ice Packs
  • PTRH2 Human
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  • Peptidyl-tRNA Hydrolase 2 Human Recombinant
  • Shipped with Ice Packs
  • PTRHD1 Human
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  • Peptidyl-TRNA Hydrolase Domain Containing 1 Human Recombinant
  • Shipped with Ice Packs

About Hydrolases:

Hydrolases are a class of hydrolytic enzymes that divide larger molecules into smaller molecules using water to break the glycosidic bonds. They are present in a wide range of biological interactions in the human body and the natural world. One most obvious example is the presence of hydrolases secreted by Lactobacillus jensenii in the human gut. This stimulates the secretion of bile salts by the liver which aid in the digestion of food. A common examples of hydrolase enzymes might be esterases including phosphatases, glycosidases, lipases, peptidases, and nucleosidases. They are divided into a wide range of subclasses based upon the different bonds they act upon.

Hydrolase Mechanism
Enzymatic hydrolysis of the glycosidic bond takes place via general acid catalysis that requires. Two critical residues are required for this to occur, a nucleophile and a proton donor.
Two major mechanisms give rise to this hydrolysis. Either there is an overall retention, or an inversion of anomeric configuration. In both mechanisms, the position of the proton donor is identical, i.e. within hydrogen-bonding distance of the glycosidic oxygen.
In retaining enzymes, the nucleophilic catalytic base is in close proximity to the sugar anomeric carbon.

Hydrolase Interactions
Different subclasses of hydrolases have a wide range of different molecular interactions inside the body. Esterases, for example, cleave ester bonds in lipids while phosphatases cleave phosphate groups off molecules. Acetylcholine esterase is a prime example of a crucial esterase. It aids in transforming the neuron impulse into acetic acid. After the impulse, the hydrolase breaks the acetylcholine into choline and acetic acid.
This acetic acid is an important metabolite in the body and a critical intermediate for other bodily reactions like glycolysis. Glycosidases, on the other hand, cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds while lipases hydrolyze glycerides and nucleosidases hydrolyze the bonds of nucleotides.

Hydrolase Function
Hydrolase enzymes have a wide range of functions inside of the body. The degenerative properties of hydrolases, for example, are essential for the body. In lipids, lipases help to facilitate the breakdown of fats, lipoproteins and other larger molecules into smaller molecules like fatty acids and glycerol. These fatty acids and other small molecules are essential in the body’s storage and synthesis of energy.
Structures
Hydrolases have a range of structures which dictate their interactions and functions.
Crater / pocket structure topology is most optimal for the recognition of a saccharide non-reducing extremity. It is most commonly encountered in monosaccharides as well as exopolysaccharides such as glucoamylase and β-amylase.
Tunnel structures have only been found in cellobiohydrolases. Nonetheless, the resulting tunnel shapes structure enables a polysaccharide chain to be threaded through it. Thus, the structure allows enzymes to release the product while remaining firmly bound to the polysaccharide chain and create the conditions for processivity.
Groove / cleft structure are “open” structures allow for a random binding of multiple sugar units in polymeric substrates. It is usually found in endo-acting polysaccharidases. Some examples of which might include endocellulases, chitinases, lysozymes and xylanases among others.