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・ N-acetylphosphatidylethanolamine-hydrolysing phospholipase D
・ N-Acetylprocainamide
・ N-Acetylserotonin
・ N-acetylserotonin O-methyltransferase-like protein
・ N-Acetyltalosaminuronic acid
・ N-acetyltransferase
・ N-acetyltransferase 1
・ N-acetyltransferase 2
・ N-Acyl homoserine lactone
・ N-acyl phosphatidylethanolamine-specific phospholipase D
・ N-acyl-D-amino-acid deacylase
・ N-acyl-D-aspartate deacylase
・ N-acyl-D-glutamate deacylase
・ N-Acylamides
・ N-Acylethanolamine
N-acylethanolamine acid amide hydrolase
・ N-acylglucosamine 2-epimerase
・ N-acylglucosamine-6-phosphate 2-epimerase
・ N-acylhexosamine oxidase
・ N-acylmannosamine 1-dehydrogenase
・ N-acylmannosamine kinase
・ N-acylneuraminate cytidylyltransferase
・ N-acylneuraminate-9-phosphatase
・ N-acylneuraminate-9-phosphate synthase
・ N-Acylphosphatidylethanolamine
・ N-acylsphingosine galactosyltransferase
・ N-alkylglycine oxidase
・ N-alpha-acetyltransferase 10
・ N-Arachidonoyl dopamine
・ N-Arachidonylglycine


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N-acylethanolamine acid amide hydrolase : ウィキペディア英語版
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 at residue Cys-126. NAAA cleaves C-N non-peptide bonds in linear amides, particularly ethanolamides. Its mechanism is quite similar to that of AC, which is further supported by AC's ability to cleave N-acylethanolamines (NAEs), albeit at far lower rates and with different specificities. While mechanistic details are not very well known, catalytic activity of NAAA is thought to be activated by Cys-126 and Asp-145.

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