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N-羟化黄素蛋白单加氧酶的机理和结构研究。

Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases.

机构信息

Molecular Biosciences, University of Kansas, Lawrence, KS, United States.

出版信息

Bioorg Chem. 2011 Dec;39(5-6):171-7. doi: 10.1016/j.bioorg.2011.07.006. Epub 2011 Aug 5.

Abstract

The N-hydroxylating flavoprotein monooxygenases are siderophore biosynthetic enzymes that catalyze the hydroxylation of the sidechain amino-group of ornithine or lysine or the primary amino-group of putrescine. This hydroxylated product is subsequently formylated or acylated and incorporated into the siderophore. Importantly, the modified amino-group is a hydroxamate and serves as an iron chelating moiety in the siderophore. This review describes recent work to characterize the ornithine hydroxylases from Pseudomonas aeruginosa (PvdA) and Aspergillus fumigatus (SidA) and the lysine hydroxylase from Escherichia coli (IucD). This includes summaries of steady and transient state kinetic data for all three enzymes and the X-ray crystallographic structure of PvdA.

摘要

N-羟化黄素蛋白单加氧酶是一种铁载体生物合成酶,能够催化鸟氨酸或赖氨酸的侧链氨基基团或腐胺的伯氨基基团的羟化。该羟化产物随后甲酰化或酰化,并被整合到铁载体中。重要的是,修饰后的氨基基团是羟肟酸,并且在铁载体中充当铁螯合部分。本综述描述了最近对铜绿假单胞菌(PvdA)和烟曲霉(SidA)的鸟氨酸羟化酶以及大肠杆菌(IucD)的赖氨酸羟化酶进行的特征描述工作。这包括对所有三种酶的稳态和瞬态动力学数据以及 PvdA 的 X 射线晶体结构的总结。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f670/3188341/d9a0c2bcbfa0/nihms316803f1.jpg

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