Lactase-phlorizin hydrolase may refer to:
In enzymology, a phloretin hydrolase (EC 3.7.1.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a glycosylceramidase (EC 3.2.1.62) is an enzyme that catalyzes the chemical reaction
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The Enzyme Commission number is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.
Hydrolase is a class of enzyme that is commonly used as biochemical catalysts that use water to break a chemical bond. This results in a division of a larger molecule to smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases. Esterases cleave ester bonds in lipids and phosphatases cleave phosphate groups off molecules. An example of crucial esterase is the acetylcholine esterase, which assists in transforming the neuron impulse into acetic acid after it the hydrolase breaks the acetylcholine into choline and acetic acid. Acetic acid is an important metabolite in the body, which becomes a nice intermediate for other reactions such as glycolysis. Lipases hydrolyze glycerides. Glycosidases cleave sugar molecules off carbohydrates and peptidases hydrolyze peptide bonds. Nucleosidases hydrolyze the bonds of nucleotides.
Phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor.
URB597 (KDS-4103) is a relatively selective inhibitor of the enzyme fatty acid amide hydrolase (FAAH). FAAH is the primary degradatory enzyme for the endocannabinoid anandamide and, as such, inhibition of FAAH leads to an accumulation of anandamide in the CNS and periphery where it activates cannabinoid receptors. URB597 has been found to elevate anandamide levels and have activity against neuropathic pain in a mouse model.
An esterase is a hydrolase enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis.
Thioesterases are enzymes which belong to the esterase family. Esterases, in turn, are one type of the several hydrolases known.
Acid anhydride hydrolases are a class of hydrolase enzymes that catalyze the hydrolysis of an acid anhydride bond. They are classified under EC number 3.6. One well known member of this class is GTPase.
Glycoside hydrolases catalyze the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose (cellulase), hemicellulose, and starch (amylase), in anti-bacterial defense strategies, in pathogenesis mechanisms and in normal cellular function. Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds.
Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome. A defining characteristic of these enzymes is the presence of a nucleophilic serine in their active site, which is used for the hydrolysis of substrates. Catalysis proceeds by the formation of an acyl-enzyme intermediate through this serine, followed by water/hydroxide-induced saponification of the intermediate and regeneration of the enzyme. Unlike other non-catalytic serines, the nucleophilic serine of these hydrolases is typically activated by a proton relay involving a catalytic triad consisting of the serine, an acidic residue and a basic residue, although variations on this mechanism exist.
N-acetylglucosamine-1-phosphate transferase is a transferase enzyme.
Leukotriene A4 hydrolase, also known as LTA4H is a human gene. The protein encoded by this gene is a bifunctional enzyme which converts leukotriene A4 to leukotriene B4 and acts as an aminopeptidase.
In enzymology, a 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) is an enzyme that catalyzes the chemical reaction
In enzymology, a formyl-CoA hydrolase (EC 3.1.2.10) is an enzyme that catalyzes the chemical reaction
In enzymology, a glucosylceramidase (EC 3.2.1.45) is an enzyme that catalyzes the chemical reaction
In enzymology, a riboflavinase (EC 3.5.99.1) is an enzyme that catalyzes the chemical reaction
The alpha/beta hydrolase superfamily is superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common fold. The core of each enzyme is an alpha/beta-sheet, containing 8 beta strands connected by 6 alpha helices. The enzymes are believed to have diverged from a common ancestor, retaining little obvious sequence similarity, but preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best-conserved structural features of the fold.
Glucanases are enzymes that break down a glucan, a polysaccharide made of several glucose sub-units. As they perform hydrolysis of the glucosidic bond, they are hydrolases.
4-Nonylphenylboronic acid is a potent and selective inhibitor of the enzyme fatty acid amide hydrolase (FAAH), with an IC50 of 9.1nM, and 870x selectivity for FAAH over the related enzyme MAGL, which it inhibits with an IC50 of 7900nM. It is also a weaker inhibitor of the enzymes endothelial lipase and lipoprotein lipase, with IC50 values of 100nM and 1400nM respectively.
alpha/beta-Hydrolase domain containing 6 (ABHD6), also known as monoacylglycerol lipase ABHD6 or 2-arachidonoylglycerol hydrolase is an enzyme that in humans is encoded by the ABHD6 gene.