The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an L-amino acid oxidase
The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an L-amino acid oxidase
复制标题
DOI：
10.1007/s00253-008-1499-x
复制
发表时间：
2008-07-01
影响因子：
5
通讯作者：
Sanchez-Amat, Antonio
中科院分区：
文献类型：
--
作者：
Gomez, Daniel;Espinosa, Elena;Sanchez-Amat, Antonio
从地中海新分离到两株紫色色素细菌cp莫尔-1和cp莫尔-2，经16S RNA测序和表型分析表明，它们属于假互变单胞菌（Pseudoalteromonas luteoviolacea）。许多菌株具有合成具有抗菌活性的大分子的能力，但这些大分子的性质至今尚未报道。对这两种新菌株的抗菌化合物的研究表明，它们合成了一种具有抗菌活性的大分子，可以被过氧化氢酶抑制，正如在P. luteoviolacea NCIMB T-1893中所描述的那样。这项工作阐明了这种大分子作为一种具有广泛底物特异性的新型l -氨基酸氧化酶（LAO）的性质。该酶对Met、Gln、Leu、Phe、Glu和Trp最活跃。在含有这些氨基酸的生长培养基中，由LAO催化反应产生的过氧化氢介导其抗菌活性。
Two purple pigmented bacterial strains, CPMOR-1 and CPMOR-2, have been newly isolated from the Mediterranean Sea. 16S RNA sequencing and phenotypic characteristics indicate that they belong to the species Pseudoalteromonas luteoviolacea. The synthesis of macromolecules with antimicrobial activity is a capacity described in many strains of this species although the nature of those macromolecules has not been reported up to now. The search for antimicrobial compounds in the two new strains described in this work shows that they synthesize a macromolecule with antimicrobial activity that can be inhibited by catalase, as it had been described in the type strain P. luteoviolacea NCIMB T-1893. This work elucidates the nature of such macromolecule as a novel L-amino acid oxidase (LAO) with broad substrate specificity. The enzyme is most active with Met, Gln, Leu, Phe, Glu, and Trp. In growth media containing those amino acids, the hydrogen peroxide generated by the reaction catalyzed by the LAO mediates its antimicrobial activity.