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Computational analysis of ethyl acetate extract of Nauclea subdita (Korth.) Steud. leaves as peptidoglycan glycosyltransferase inhibitor in Aeromonas hydrophila

IOP Conference Series: Earth and Environmental Science, 2020
Abstract Aeromonas hydrophila is a cause of Motile Aeromonad Septicemia (MAS) disease in freshwater fish, which is often endemic and causes significant losses in a freshwater fish farming business. Aeromonas hydrophila belongs to the group of gram-negative bacteria and has a complex cell wall consisting of three layers,
Wendy Alexander Tanod, Putut Har Riyadi
exaly   +2 more sources

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Peptidoglycan glycosyltransferase

1996
Dietmar Schomburg, Dörte Stephan
exaly   +2 more sources

Murgocil is a Highly Bioactive Staphylococcal-Specific Inhibitor of the Peptidoglycan Glycosyltransferase Enzyme MurG

ACS Chemical Biology, 2013
Modern medicine is founded on the discovery of penicillin and subsequent small molecules that inhibit bacterial peptidoglycan (PG) and cell wall synthesis. However, the discovery of new chemically and mechanistically distinct classes of PG inhibitors has become exceedingly rare, prompting speculation that intracellular enzymes involved in PG precursor ...
Anna Müller, Pedro M Pereira, Margarida Moreira Dos Santos   +2 more
exaly   +3 more sources

Continuous Fluorescence Assay for Peptidoglycan Glycosyltransferases

2016
Bacterial cell wall peptidoglycan is synthesized from its precursor lipid II by two enzymatic reactions. First, glycosyltransferases polymerize the glycan strands and second, DD-transpeptidases form cross-links between peptides of neighboring strands.
Egan AJF, Vollmer W
openaire   +5 more sources

Targeting Bacterial Cell Wall Peptidoglycan Synthesis by Inhibition of Glycosyltransferase Activity

Chemical Biology & Drug Design, 2015
Synthesis of bacterial cell wall peptidoglycan requires glycosyltransferase enzymes that transfer the disaccharide–peptide from lipid II onto the growing glycan chain. The polymerization of the glycan chain precedes cross‐linking by penicillin‐binding proteins and is essential for growth for key bacterial pathogens.
Mesleh, Michael F., Rajaratnam, Premraj, Conrad, Mary, Chandrasekaran, Vasu, Liu, Christopher M., Pandya, Bhaumik A., Hwang, You Seok, Rye, Peter T., Muldoon, Craig, Becker, Bernd, Zuegg, Johannes, Meutermans, Wim, Moy, Terence I.   +12 more
openaire   +5 more sources

The monofunctional glycosyltransferase ofEscherichia coliis a member of a new class of peptidoglycan-synthesising enzymes

FEBS Letters, 1996
Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacteria] species.
Dietrich Stüber, W Keck, D Stüber
exaly   +2 more sources

The molecular biology of moenomycins: towards novel antibiotics based on inhibition of bacterial peptidoglycan glycosyltransferases

Biological Chemistry, 2010
AbstractMoenomycins are phosphoglycolipid antibiotics and the only known natural product inhibitors of peptidoglycan glycosytransferases (PGTs). Techniques that would allow facile diversification of the moenomycin structure would facilitate the development of novel antibiotics, which are urgently needed in the wake of multidrug resistant bacterial ...
Bohdan, Ostash, Emma, Doud, Victor, Fedorenko   +2 more
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Identification of Peptidoglycan Glycosyltransferase FtsI as a Potential Drug Target against Salmonella Enteritidis and Salmonella Typhimurium Serovars Through Subtractive Genomics, Molecular Docking and Molecular Dynamics Simulation Approaches

Current Pharmaceutical Design
Introduction: Salmonella enterica serovar Enteritidis and Salmonella enterica serovar Typhimurium are among the main causative agents of nontyphoidal Salmonella infections, imposing a significant global health burden. The emergence of antibiotic resistance in these pathogens underscores the need for innovative therapeutic strategies.
Imran Gulzar, Asma Khalil, Usman Ali Ashfaq, Sadia Liaquat, Asma Haque   +4 more
openaire   +2 more sources

Studies towards a Solution Structure of the Peptidoglycan Glycosyltransferases

2012
Peptidoglycan glycosyltransferases (PGTs) are highly conserved bacterial enzymes that catalyze the polymerization of the lipidic disaccharide, Lipid II, to form individual peptidoglycan (PG) strands which are subsequently cross-linked to form mature PG, the major skeletal component of the bacterial cell wall.
openaire   +1 more source

Peptidoglycan Glycosyltransferase Inhibition: New Perspectives for An Old Target

Anti-Infective Agents in Medicinal Chemistry, 2008
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