在 Albachelin 生物合成中精氨酸羟化步骤的表征。
Characterization of the Ornithine Hydroxylation Step in Albachelin Biosynthesis.
机构信息
Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA.
Center for Drug Discovery, Virginia Tech, Blacksburg, VA 24061, USA.
出版信息
Molecules. 2017 Oct 1;22(10):1652. doi: 10.3390/molecules22101652.
-Hydroxylating monooxygenases (NMOs) are involved in siderophore biosynthesis. Siderophores are high affinity iron chelators composed of catechol and hydroxamate functional groups that are synthesized and secreted by microorganisms and plants. Recently, a new siderophore named albachelin was isolated from a culture of growing under iron-limiting conditions. This work focuses on the expression, purification, and characterization of the NMO, abachelin monooxygenase (AMO) from . This enzyme was purified and characterized in its holo (FAD-bound) and apo (FAD-free) forms. The apo-AMO could be reconstituted by addition of free FAD. The two forms of AMO hydroxylate ornithine, while lysine increases oxidase activity but is not hydroxylated and display low affinity for NADPH.
羟化单加氧酶（NMOs）参与了铁载体的生物合成。铁载体是由儿茶酚和羟肟酸官能团组成的高亲和力铁螯合剂，由微生物和植物合成和分泌。最近，一种新的铁载体名为 albachelin 从 在铁限制条件下生长的培养物中分离出来。本工作重点研究了 NMO 的表达、纯化和表征， albachelin 单加氧酶（AMO）。该酶以全酶（结合 FAD）和脱辅基酶（无 FAD）形式进行纯化和表征。apo-AMO 可通过添加游离 FAD 重新构成。两种形式的 AMO 羟化鸟氨酸，而赖氨酸增加氧化酶活性但不被羟化，并且对 NADPH 的亲和力低。
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