Structural and functional insights into UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) from Brucella ovis.

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Tác giả: Sergio Boneta, Víctor Correa-Pérez, Marta Martínez-Júlvez, Milagros Medina, Martha Minjárez-Sáenz, Víctor Polo, Maribel Rivero, Sheila J Sadeghi, Paula Suárez, Inmaculada Yruela

Ngôn ngữ: eng

Ký hiệu phân loại: 535.22 Intensity of light

Thông tin xuất bản: United States : Archives of biochemistry and biophysics , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 90104

The peptidoglycan biosynthetic pathway involves a series of enzymatic reactions in which UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) plays a crucial role in catalyzing the conversion of UDP-N-acetylglucosamine-enolpyruvate (UNAGEP) to UDP-N-acetylmuramic acid. This reaction relies on NADPH and FAD and, since MurB is not found in eukaryotes, it is an attractive target for the development of antimicrobials. MurB from Brucella ovis, the causative agent of brucellosis in sheep, is characterized here. The FAD cofactor in MurB of B. ovis is reduced to the hydroquinone state without semiquinone stabilization with an estimated E
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