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Hydrolase enzymes are important for the body because they have degradative properties. In lipids, lipases contribute to the breakdown of fats and lipoproteins and other larger molecules into smaller molecules like fatty acids and glycerol. Fatty acids and other small molecules are used for synthesis and as a source of energy. [1]
A Pancreatic alpha-Amylase 1HNY, a glycoside hydrolase In biochemistry , glycoside hydrolases (also called glycosidases or glycosyl hydrolases ) are a class of enzymes which catalyze the hydrolysis of glycosidic bonds in complex sugars .
An acid hydrolase is an enzyme that works best at acidic pHs.It is commonly located in lysosomes, which are acidic on the inside.Acid hydrolases may be nucleases, proteases, glycosidases, lipases, phosphatases, sulfatases and phospholipases and make up the approximately 50 degradative enzymes of the lysosome that break apart biological matter.
Fatty-acid amide hydrolase 1 (FAAH) [5] is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide (AEA), an N -acylethanolamine (NAE) in 1993. [ 6 ] In humans, it is encoded by the gene FAAH .
The alpha/beta hydrolase superfamily is a superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common fold. [1] The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 beta strands connected by 6 alpha helices.
The structure of epoxide hydrolase B reveals that the enzyme is a monomer and contains an alpha/beta hydrolase fold. In addition to providing insights into the enzyme mechanism, this hydrolase currently serves as a platform for rational drug design of potent inhibitors. In particular, urea based inhibitors have been developed.
Serine hydrolases are one of the largest known enzyme classes comprising approximately ~200 enzymes or 1% of the genes in the human proteome. [1] A defining characteristic of these enzymes is the presence of a particular serine at the active site, which is used for the hydrolysis of substrates.
The cytosolic trehalase enzyme, NT, has been purified and characterized extensively from S. cerevisiae. In non-denaturing gels this enzyme protein exhibited a molecular mass of 160 kDa, while in sodium dodecyl sulfate-polyacrylamide gel electrophoresis it showed a mass of 80 kDa. This hydrolase enzyme is specific for trehalose.