<p>Therapeutic compounds targeting Lipid II for antibacterial purposes</p>

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The lantibiotic mersacidin inhibits peptidoglycan synthesis by targeting lipid II.

The lantibiotic mersacidin exerts its bactericidal action by inhibition of peptidoglycan biosynthesis. It interferes with the membrane-associated transglycosylation reaction; during this step the ultimate monomeric peptidoglycan precursor, undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)-GlcNAc (lipid II) is converted into polymeric nascent peptidoglycan. In the present study we demonstrate th...

متن کامل

Antibacterial compounds from Glycyrrhiza uralensis.

From the roots of Glycyrrhiza uralensis, two new pterocarpenes, glycyrrhizol A (1) and glycyrrhizol B (2), along with four known isoflavonoids, 5-O-methylglycryol (3), isoglycyrol (4), 6,8-diisoprenyl-5,7,4'-trihydroxyisoflavone (5), and gancaonin G (6), were isolated using a bioassay-guided fractionation method. The structures of the new compounds (1and 2) were elucidated by spectroscopic data...

متن کامل

Colicin M, a peptidoglycan lipid-II-degrading enzyme: potential use for antibacterial means?

Colicins are proteins produced by some strains of Escherichia coli to kill competitors belonging to the same species. Among them, ColM (colicin M) is the only one that blocks the biosynthesis of peptidoglycan, a specific bacterial cell-wall polymer essential for cell integrity. ColM acts in the periplasm by hydrolysing the phosphoester bond of the peptidoglycan lipid intermediate (lipid II). Co...

متن کامل

Dual targeting of GyrB and ParE by a novel aminobenzimidazole class of antibacterial compounds.

A structure-guided drug design approach was used to optimize a novel series of aminobenzimidazoles that inhibit the essential ATPase activities of bacterial DNA gyrase and topoisomerase IV and that show potent activities against a variety of bacterial pathogens. Two such compounds, VRT-125853 and VRT-752586, were characterized for their target specificities and preferences in bacteria. In metab...

متن کامل

Antibacterial Resistance via Gyrb24 Targeting

In Escherichia coli, the gyrase enzyme is composed of two subunits: A and B [1]. The A subunit (97 k Da) interacts and relieves DNA super coils through its active site (tyrosine) during DNA replication. The B subunit contains the ATP as active site required to release the energy in the attached ATP molecule and provides the free energy to the reaction (DNA super coiling) accomplished by the gyr...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Infection and Drug Resistance

سال: 2019

ISSN: 1178-6973

DOI: 10.2147/idr.s215070