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鲤鱼单胺氧化酶的分子特征。

Molecular characteristics of a single and novel form of carp (Cyprinus carpio) monoamine oxidase.

机构信息

Department of Pharmacology, School of Medicine, Showa University, 1-5-8 Hatanodai, Shinagawa-Ku, Tokyo 142-8555, Japan.

出版信息

Comp Biochem Physiol B Biochem Mol Biol. 2010 Mar;155(3):266-71. doi: 10.1016/j.cbpb.2009.11.010. Epub 2009 Nov 20.

Abstract

Two mammalian monoamine oxidases (MAO), MAO-A and MAO-B, are similar in primary structures but have unique substrate/inhibitor selectivities. Carp (Cyprinus carpio) contains a MAO enzyme (C-MAO) with properties different from MAO-A and MAO-B. To determine the molecular characteristics of C-MAO and its phylogenetic relationship with other fish and mammalian MAOs, the primary structure of C-MAO was estimated. The putative C-MAO cDNA encodes 526 amino acids with 59.001 Da, and the deduced amino acid sequence showed as much as 68.9% homology with some mammalian MAO-A proteins, 69.8% homology with some mammalian MAO-B proteins, and as much as 92.4% homology with some fish MAOs. Comparison of two regions in the polypeptide sequence of C-MAO determining possible substrate/inhibitor preferences of MAO-A and MAO-B showed both 79.5% homologies.

摘要

两种哺乳动物单胺氧化酶(MAO),MAO-A 和 MAO-B,在一级结构上相似,但具有独特的底物/抑制剂选择性。鲤鱼(Cyprinus carpio)含有一种与 MAO-A 和 MAO-B 不同的 MAO 酶(C-MAO)。为了确定 C-MAO 的分子特征及其与其他鱼类和哺乳动物 MAOs 的系统发育关系,我们估计了 C-MAO 的一级结构。推测的 C-MAO cDNA 编码 526 个氨基酸,分子量为 59.001 Da,推导的氨基酸序列与一些哺乳动物 MAO-A 蛋白的同源性高达 68.9%,与一些哺乳动物 MAO-B 蛋白的同源性高达 69.8%,与一些鱼类 MAOs 的同源性高达 92.4%。比较 C-MAO 多肽序列中决定 MAO-A 和 MAO-B 可能的底物/抑制剂偏好的两个区域,发现它们具有 79.5%的同源性。

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