Properties of rat liver N-acylethanolamine amidohydrolase

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作者：

PC Schmid，ML Zuzarte-Augustin，HHO Schmid

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摘要：

Rat liver microsomes and mitochondria contain an amidohydrolase which catalyzes the hydrolysis of N-acylethanolamine to ethanolamine and fatty acid. The enzyme is active over a wide range of pH, does not require divalent cations, and is inhibited by sulfhydryl-reactive agents. The detergents Triton X-100, sodium cholate, and sodium dodecyl sulfate are also inhibitory, but sodium taurodeoxycholate has little effect and was therefore used to solubilize the enzyme. The solubilized enzyme exhibits high substrate specificity for long-chain amides of ethanolamine. Amides of propanolamine or higher homologs are hydrolyzed at a drastically slower rate, and isomers prepared from long-chain amine and short-chain hydroxy acid are neither substrates nor inhibitors of the enzyme. Neither ceramide (N-acylsphingosine) nor N,O-diacylethanolamine is hydrolyzed. Both particulate and soluble enzyme preparations also catalyze the synthesis of N-acylethanolamine from ethanolamine and fatty acid, probably by the amidohydrolase acting in reverse.

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关键词：

Linkage helicity magnetohydrodynamics solar magnetism

DOI：

10.1016/0165-022X(85)90070-3

被引量：

415

年份：

1985