|
N-acylethanolamine Acid Amide Hydrolase
N-acylethanolamine acid amide hydrolase (NAAA) is a member of the choloylglycine hydrolase family, a subset of the N-terminal nucleophile hydrolase superfamily. NAAA has a molecular weight of 31 kDa. The activation and inhibition of its catalytic site is of medical interest as a potential treatment for obesity and chronic pain. While it was discovered within the last decade, its structural similarity to the more familiar acid ceramidase (AC) and functional similarity to fatty acid amide hydrolase (FAAH) allow it to be studied extensively. Mechanism The overall enzyme mechanism involves cleavage into two chains, one of which contains the catalytic nucleophile, believed to be a cysteine residue. Unlike FAAH, which operates in basic conditions, this enzyme must operate under acidic conditions (pH ~4.5), and is completely inactivated at a pH of 8. Selective inhibitors of NAAA are ester and amide compounds, such as N-cyclohexanecarbonylpentadecylamine. NAAA is cleaved proteolytically a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Choloylglycine Hydrolase Family
In enzymology, a choloylglycine hydrolase () is an enzyme that catalysis, catalyzes the chemical reaction :3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine + H2O \rightleftharpoons 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine Thus, the two substrate (biochemistry), substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine and water, H2O, whereas its two product (chemistry), products are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate and glycine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The List of enzymes, systematic name of this enzyme class is 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine amidohydrolase. Other names in common use include glycocholase, bile salt hydrolase, and choloyltaurine hydrolase. This enzyme participates in bile acid biosynthesis. Structural studies As of late 2007, 4 tertiary str ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
