Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria.
Distribution in Different Organisms of Amino Acid Oxidases with FAD or a Quinone As Cofactor and Their Role as Antimicrobial Proteins in Marine Bacteria.
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DOI：
10.3390/md13127073
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发表时间：
2015-12-16
期刊：
影响因子：
5.4
通讯作者：
Sanchez-Amat A
中科院分区：
文献类型：
--
作者：
Campillo-Brocal JC;Lucas-Elío P;Sanchez-Amat A
氨基酸氧化酶（AAOs）催化氨基酸的氧化脱胺反应，释放出氨和过氧化氢。这些酶有几种已经被报道过。根据用作底物的氨基酸异构体，可以区分l-氨基酸氧化酶和d-氨基酸氧化酶。两者都使用FAD作为辅助因子，并氧化α位置的氨基酸，释放相应的酮酸。最近，一类新的AAOs被描述为不含FAD作为辅助因子，而是由同一蛋白中残基的翻译后修饰产生的醌。这些蛋白被命名为LodA样蛋白，以这类蛋白的第一个成员LodA命名，LodA是由海洋细菌地中海Marinomonas mediterranea合成的赖氨酸epsilon氧化酶。在这篇综述中，对所有具有AAO活性的酶进行了系统发育分析。结果表明，这些酶的不同基团是可以识别的，含有醌辅助因子的酶有明显的分化。在海洋细菌中，特别是假互生单胞菌属中，由于其产生过氧化氢的能力而被描述为抗菌的大多数蛋白质属于loda样蛋白质组。
Amino acid oxidases (AAOs) catalyze the oxidative deamination of amino acids releasing ammonium and hydrogen peroxide. Several kinds of these enzymes have been reported. Depending on the amino acid isomer used as a substrate, it is possible to differentiate between l-amino acid oxidases and d-amino acid oxidases. Both use FAD as cofactor and oxidize the amino acid in the alpha position releasing the corresponding keto acid. Recently, a novel class of AAOs has been described that does not contain FAD as cofactor, but a quinone generated by post-translational modification of residues in the same protein. These proteins are named as LodA-like proteins, after the first member of this group described, LodA, a lysine epsilon oxidase synthesized by the marine bacterium Marinomonas mediterranea. In this review, a phylogenetic analysis of all the enzymes described with AAO activity has been performed. It is shown that it is possible to recognize different groups of these enzymes and those containing the quinone cofactor are clearly differentiated. In marine bacteria, particularly in the genus Pseudoalteromonas, most of the proteins described as antimicrobial because of their capacity to generate hydrogen peroxide belong to the group of LodA-like proteins.