Author: Su, Junhui; Chang, Cui; Xiang, Qi; Zhou, Zhi-Wei; Luo, Rong; Yang, Lun; He, Zhi-Xu; Yang, Hongtu; Li, Jianan; Bei, Yu; Xu, Jinmei; Zhang, Minjing; Zhang, Qihao; Su, Zhijian; Huang, Yadong; Pang, Jiyan; Zhou, Shu-Feng
Title: Xyloketal B, a marine compound, acts on a network of molecular proteins and regulates the activity and expression of rat cytochrome P450 3a: a bioinformatic and animal study Document date: 2014_12_12
ID: y14atmnh_92
Snippet: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes, such as the vitamin K-dependent γ-carboxylation of glutamate residues in prothrombin synthesis. Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin, and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory.....
Document: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes, such as the vitamin K-dependent γ-carboxylation of glutamate residues in prothrombin synthesis. Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin, and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.
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