Identification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity.
Identification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity.
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DOI：
10.1002/mbo3.107
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发表时间：
2013-08
期刊：
影响因子：
3.4
通讯作者：
Sanchez-Amat, Antonio
中科院分区：
文献类型：
--
作者：
Cristian Campillo-Brocal, Jonatan;Lucas-Elio, Patricia;Sanchez-Amat, Antonio
一种具有赖氨酸-epsilon氧化酶活性的新型酶先前在海洋细菌Marinomonas mediterranea中被描述。这种酶与其他l-氨基酸氧化酶的不同之处在于它不是黄蛋白，而是含有醌辅助因子。它由一个带有两个基因lodA和lodB的操纵子编码。第一个编码氧化酶，而第二个编码表达氧化酶所需的蛋白质。地中海支原体的基因组测序显示，它含有两个额外的操纵子，编码与LodA序列相似的蛋白质。本研究表明，其中一个基因Marme_1655的产物编码一种具有甘氨酸氧化酶活性的蛋白。这种活性在底物范围和对其他甘氨酸氧化酶抑制剂的敏感性方面显示出重要的差异，这些抑制剂是由芽孢杆菌合成的黄蛋白。本研究结果表明，细菌基因组中检测到的与lodA相似程度不同的基因产物可能构成不同氧化酶的储库。
A novel enzyme with lysine-epsilon oxidase activity was previously described in the marine bacterium Marinomonas mediterranea. This enzyme differs from other l-amino acid oxidases in not being a flavoprotein but containing a quinone cofactor. It is encoded by an operon with two genes lodA and lodB. The first one codes for the oxidase, while the second one encodes a protein required for the expression of the former. Genome sequencing of M. mediterranea has revealed that it contains two additional operons encoding proteins with sequence similarity to LodA. In this study, it is shown that the product of one of such genes, Marme_1655, encodes a protein with glycine oxidase activity. This activity shows important differences in terms of substrate range and sensitivity to inhibitors to other glycine oxidases previously described which are flavoproteins synthesized by Bacillus. The results presented in this study indicate that the products of the genes with different degrees of similarity to lodA detected in bacterial genomes could constitute a reservoir of different oxidases.
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影响因子：
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作者：
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影响因子：
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作者：
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通讯作者：
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