Authors: Shunichi Wada Shigeki Matsunaga Nobuhiro Fusetani Shugo Watabe
Publish Date: 2014/02/13
Volume: 2, Issue: 3, Pages: 285-292
Abstract
Theonellamide A a bicyclic peptide isolated from a Theonella sponge was fixed on hydrazidecontaining gel beads and screened for its binding proteins from rabbit liver tissues Analysis by sodium dodecyl sulfate–polyacrylamide gel electrophoresis revealed that two major proteins of 80 kDa and 55 kDa interacted with theonellamide A The interaction between theonellamide A and two proteins was confirmed by competition experiments in which these two proteins failed to bind to theonellamide A–conjugated gel beads in the presence of theonellamide A or F Aminoterminal amino acid sequence analysis of peptide fragments derived from the binding proteins by lysylendopeptidase digestion demonstrated that the 80kDa and 55kDa proteins were 17βhydroxysteroid dehydrogenase IV and glutamate dehydrogenase respectively In an in vitro assay system amination of αketoglutarate by glutamate dehydrogenase was activated with theonellamide F although this effect was weaker than that with adenosine diphosphate a wellknown activator
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