Structure based drug designing and discovery of promising lead molecules against UDP-N-acetylenolpyruvoylglucosamine reductase (MurB): A potential drug target in multi-drug resistant Acinetobacter baumannii

Amera, Gizachew Muluneh; Khan, Rameez Jabeer; Pathak, Abhishek; Jha, Rajat Kumar; Jain, Monika; Muthukumaran, Jayaraman; Singh, Amit Kumar

doi:10.1016/j.jmgm.2020.107675

Cited by 14 publications

(6 citation statements)

References 53 publications

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“…This list could be potential targets for the search for antimicrobials. Some of them are already being explored as targets of inhibitors in other bacteria, as for example, UDP-N-acetylmuramate dehydrogenase ( 102 , 103 ), riboflavin synthase ( 104 ), bifunctional riboflavin kinase/FAD synthase ( 25 , 26 ), or chorismate synthase ( 105 ). In agreement, a comparative metabolomics study in B. melitensis also pointed to synthase as an attractive target ( 106 ).…”

Section: Resultsmentioning

confidence: 99%

Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries

et al. 2022

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Section: Resultsmentioning

confidence: 99%

Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries

et al. 2022

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“…These proteins also provide protection against a myriad environmental toxins through active extrusion of the pernicious compounds [ 70 ]. Finally, UDP-N-acetylenol pyruvoyl glucosamine reductase (MurB) is the product of murB gene which catalyzes the terminal steps of the formation of UDP-N-acetylmuramic acid in the peptidoglycan biosynthesis pathway [ 71 ].…”

Section: Discussionmentioning

confidence: 99%

Subtractive proteomics approach to Unravel the druggable proteins of the emerging pathogen Waddlia chondrophila and drug repositioning on its MurB protein

Chowdhury

Saba

Sufi

et al. 2021

Heliyon

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“…The DrugBank database BLASTp shows that the alignment with flavin adenine dinucleotide drug resulted in E-value: 2.6683e-91, which is UDP-N acetyl enol pyruvoyl glucosamine reductase is encoded by the murB gene and involved in the catalysis of the final steps of the UDP-N-acetylmuramic acid formation [24]. This reaction is an NADPH-dependent reduction of enolpyruvyl-UDP-N-acetylglucosamine, releasing UDP-Nacetylmuramic acid as a product, to which three amino acids will subsequently be added sequentially by other enzymes in the pathway [25]. MurB is a flavoprotein and belongs to the superfamily category of FAD binding protein with a feature of flavin adenine dinucleotide binding fold [26].…”

Section: Udp-n-acetyl Enol Pyruvoyl Glucosamine Reductase (Murb) Udp-...mentioning

confidence: 99%

In Silico Identification and Characterization of Drug Targets in Streptococcus pneumoniae ATCC 700669 (Serotype 23F) by Subtractive Genomics

Duguma,

Dinka

2024

BioMed Research International

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Streptococcus pneumoniae (S. pneumoniae) is an important pathogen worldwide that causes pneumococcal infections which are related to high rates of morbidity and mortality especially in young children, older adults, and immune-compromised persons. Antibiotic resistance in S. pneumoniae is a serious problem across the world from time to time, resulting in treatment failure and diminished value of older medicines. Therefore, the objective of this study was to identify new putative drug targets against S. pneumoniae serotype 23F by using subtractive genomics. By using bioinformatics tools such as NCBI, UniProt KB, PDB, KEGG, DEG, PSORTb, CD hit, DrugBank database, and other softwares, proteins involved in unique metabolic pathways of S. pneumoniae serotype 23F were studied. The result indicates that this serotype consists of 97 metabolic pathways of which 74 are common with that of human, and 23 pathways are unique to the serotype 23F. After investigation and analysis of essentiality, nonhomology, subcellular localization, having drug targets, and enzymatic activity, four proteins were prioritized as druggable targets. These druggable proteins include UDP-N-acetylglucosamine 1-carboxyvinyltransferase, UDP-N-acetyl muramate dehydrogenase, D-alanine-D-alanine ligase, and alanine racemase that are found in S. pneumoniae serotype 23F. All these four proteins are essential, are nonhomologous with human proteins, have drug targets, and are located in cell cytoplasm. Therefore, the authors recommend these proteins to be used for efficient drug design against S. pneumoniae serotype 23F after experimental validation for essentiality and druggability.

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Structure based drug designing and discovery of promising lead molecules against UDP-N-acetylenolpyruvoylglucosamine reductase (MurB): A potential drug target in multi-drug resistant Acinetobacter baumannii

Cited by 14 publications

References 53 publications

Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries

Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries

Subtractive proteomics approach to Unravel the druggable proteins of the emerging pathogen Waddlia chondrophila and drug repositioning on its MurB protein

In Silico Identification and Characterization of Drug Targets in Streptococcus pneumoniae ATCC 700669 (Serotype 23F) by Subtractive Genomics

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