Identification and Characterization of a MurA, UDP-N-Acetylglucosamine Enolpyruvyl Transferase from Cariogenic Streptococcus Mutans

Li, Huajun; Zhou, Yan; Wang, Ni; Xin, Yi; Tang, Li; Ma, Yufang

doi:10.2485/jhtb.21.17

Cited by 6 publications

(5 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several ions did not exhibit any significant effect on the enzyme activity except potassium which markedly enhanced it. The K m value of w Bm-MurA for the substrate UDPAG (0.03149 mM) was comparatively lower than that of other bacterial MurAs ( E. cloacae, 0.080 mM; S. pneumoniae, 0.244 mM; S. mutans, 0.12 mM and S. aureus, 0.168 mM) with the only exception being E. coli (0.015 mM) [56] , [57] . For PEP (0.009198 mM) the value was higher than that of E. coli (0.0004 mM) and E. cloacae (0.0083 mM), while lower than that of S. mutans (0.086 mM) and S. pneumoniae (0.037 mM) [56] , [57] .…”

Section: Discussionmentioning

confidence: 76%

“…The K m value of w Bm-MurA for the substrate UDPAG (0.03149 mM) was comparatively lower than that of other bacterial MurAs ( E. cloacae, 0.080 mM; S. pneumoniae, 0.244 mM; S. mutans, 0.12 mM and S. aureus, 0.168 mM) with the only exception being E. coli (0.015 mM) [56], [57]. For PEP (0.009198 mM) the value was higher than that of E. coli (0.0004 mM) and E. cloacae (0.0083 mM), while lower than that of S. mutans (0.086 mM) and S. pneumoniae (0.037 mM) [56], [57]. On the basis of these K m values, w Bm-MurA appears to have lower affinity for both the substrates (UDPAG & PEP) as compared to that of E. coli MurA.…”

Section: Discussionmentioning

confidence: 79%

See 1 more Smart Citation

Cloning, Expression and Characterization of UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) from Wolbachia Endosymbiont of Human Lymphatic Filarial Parasite Brugia malayi

et al. 2014

View full text Add to dashboard Cite

Wolbachia, an endosymbiont of filarial nematode, is considered a promising target for treatment of lymphatic filariasis. Although functional characterization of the Wolbachia peptidoglycan assembly has not been fully explored, the Wolbachia genome provides evidence for coding all of the genes involved in lipid II biosynthesis, a part of peptidoglycan biosynthesis pathway. UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is one of the lipid II biosynthesis pathway enzymes and it has inevitably been recognized as an antibiotic target. In view of the vital role of MurA in bacterial viability and survival, MurA ortholog from Wolbachia endosymbiont of Brugia malayi (wBm-MurA) was cloned, expressed and purified for further molecular characterization. The enzyme kinetics and inhibition studies were undertaken using fosfomycin. wBm-MurA was found to be expressed in all the major life stages of B. malayi and was immunolocalized in Wolbachia within the microfilariae and female adults by the confocal microscopy. Sequence analysis suggests that the amino acids crucial for enzymatic activity are conserved. The purified wBm-MurA was shown to possess the EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) like activity at a broad pH range with optimal activity at pH 7.5 and 37°C temperature. The apparent affinity constant (K m) for the substrate UDP-N-acetylglucosamine was found to be 0.03149 mM and for phosphoenolpyruvate 0.009198 mM. The relative enzymatic activity was inhibited ∼2 fold in presence of fosfomycin. Superimposition of the wBm-MurA homology model with the structural model of Haemophilus influenzae (Hi-MurA) suggests binding of fosfomycin at the same active site. The findings suggest wBm-MurA to be a putative antifilarial drug target for screening of novel compounds.

show abstract

Section: Discussionmentioning

confidence: 76%

Section: Discussionmentioning

confidence: 79%

Cloning, Expression and Characterization of UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) from Wolbachia Endosymbiont of Human Lymphatic Filarial Parasite Brugia malayi

et al. 2014

View full text Add to dashboard Cite

show abstract

“… 48 As well as caries-causing bacteria S. mutans synthesize peptidoglycan with the help of the enzyme Mur. 49 The enzymes MurA and MurB transfer PEP (phosphoenolvirupat) which converts UDP-GlcNac (uridine diphosphate- N -acetylglucosamine) into (uridine diphosphate- N -acetylmuramyl-pentapeptide) UDP-MurNAc. 50 UDP-MurNAc is then called the substrate to which the amino acids L-ala, D-Glu, L-Lys and D-Ala-D-Ala will be attached with the help of the enzymes MurC, MurD, MurE and MurF (shown in Figure 5 ).…”

Section: Biofilm Forming Gram-positive and Gram-negative Bacteriamentioning

confidence: 99%

Phytochemical Analysis and Anti-Biofilm Potential That Cause Dental Caries from Black Cumin Seeds (Nigella sativa Linn.)

Kurnia,

Padilah,

Apriyanti

et al. 2024

DDDT

View full text Add to dashboard Cite

The oral cavity is an excellent place for various microorganisms to grow. Spectrococcus mutans and Spectrococcus sanguinis are Gram-negative bacteria found in the oral cavity as pioneer biofilm formers on the tooth surface that cause caries. Caries treatment has been done with antibiotics and therapeutics, but the resistance level of S. mutans and S. sanguinis bacteria necessitates the exploration of new drug compounds. Black cumin (Nigella sativa Linn.) is known to contain secondary metabolites that have antioxidant, antibacterial, anti-biofilm, anti-inflammatory and antifungal activities. The purpose of this review article is to present data on the potential of Nigella sativa Linn seeds as anti-biofilm. This article will discuss biofilm-forming bacteria, the resistance mechanism of antibiotics, the bioactivity of N. sativa extracts and seed isolates together with the Structure Activity Relationship (SAR) review of N. sativa compound isolates. We collected data from reliable references that will illustrate the potential of N. sativa seeds as anti-biofilm drug.

show abstract

“…23 MurB catalyzes the conversion of enolpyruvate to D-lactate, resulting in the production of UD-N-acetylmuramate in the first step of cell wall biosynthesis. 24 PBP plays a role in the final step of cell wall biosynthesis by forming cross-links in peptidoglycan and defining bacterial cell walls. 25 Molecular docking is a computational method to visualize atomic interactions between small molecules and protein targets.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant and Antibacterial Activities of the Tropical Red Alga Eucheuma spinosum: In Silico Study

Damongilala

Dotulong

Apriyanti

et al. 2023

Natural Product Communications

View full text Add to dashboard Cite

Recently, numerous studies have focused on characterizing the biochemical activities of new natural marine resources as functional foods. Eucheuma spinosum J. Agardh., family Solieraceae, is a potential functional food that is widely used as a natural food source and contains bioactive components. This study aims to identify the bioactivity, drug-likeness, and pharmacokinetics of 3-(3-methoxyphenyl) propanal isolated from E. spinosum, and to discover the molecular interactions between the ligand, 3-(3-methoxyphenyl) propanal, and various antioxidant and antibacterial receptors. The bioactivity of 3-(3-methoxyphenyl) propanal was analyzed using computational Prediction of Activity Spectra for Substance (PASS) analysis. The drug-likeness was examined based on Lipinski's rule and other parameters. The pharmacokinetics of 3-(3-methoxyphenyl) propanal were predicted, and the molecular interactions between the receptors governing the antioxidant and antibacterial activity and 3-(3-methoxyphenyl) propanal were determined using the molecular docking method and molecular dynamics simulation. Based on the PASS analysis, 3-(3-methoxyphenyl) propanal was predicted to inhibit JAK2 expression, which contributes to apoptosis, with a probability of a molecule to be active (Pa) values of 0.733 and 0.508. Additionally, 3-(3-methoxyphenyl) propanal is an oxygen scavenger (Pa 0.408) and antimutagenic (Pa 0.419). Based on the drug-likeness and pharmacokinetic analyses, 3-(3-methoxyphenyl) propanal meets the requirements for an oral drug. Molecular docking revealed that binding affinity of 3-(3-methoxyphenyl) propanal for superoxide dismutase, tyrosinase, glutathione peroxidase, UDP-N-acetylmuramate, and penicillin-binding protein was −5.5, −6.1, −4.2, −6.2, and −4.9 kcal mol −1, respectively. Moreover, according to molecular dynamics simulation, propanal 3-(3-methoxyphenyl) propanal has stronger interaction with tyrosinase than the positive control. Based on PASS analysis and molecular docking results, 3-(3-methoxyphenyl) propanal exhibited promising potential as an antioxidant.

show abstract

Identification and Characterization of a MurA, UDP-N-Acetylglucosamine Enolpyruvyl Transferase from Cariogenic Streptococcus Mutans

Cited by 6 publications

References 22 publications

Cloning, Expression and Characterization of UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) from Wolbachia Endosymbiont of Human Lymphatic Filarial Parasite Brugia malayi

Cloning, Expression and Characterization of UDP-N-Acetylglucosamine Enolpyruvyl Transferase (MurA) from Wolbachia Endosymbiont of Human Lymphatic Filarial Parasite Brugia malayi

Phytochemical Analysis and Anti-Biofilm Potential That Cause Dental Caries from Black Cumin Seeds (Nigella sativa Linn.)

Antioxidant and Antibacterial Activities of the Tropical Red Alga Eucheuma spinosum: In Silico Study

Contact Info

Product

Resources

About