Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.8.1.4 (diaphorase)
 2,754 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Manuka honey, derived from the New Zealand flowering plant Leptospermum scoparium, shows promise as a topical antibacterial agent and effective chronic wound dressing. The aim of this study was to determine the non-peroxide antibacterial effects of this honey on the proteome of the common wound pathogen Staphylococcus aureus. Proteomic analysis was performed on cells treated for a short time with manuka honey compared with the proteome of untreated cells as well as cells treated with a Leptospermum honey sample without antibacterial activity. Treatment with manuka honey resulted in a significant decrease in the bacterial cell growth rate as well as downregulation of ten and upregulation of two proteins. Nine of these proteins were also differentially expressed by cells treated with the inactive Leptospermum honey, but to a lesser degree, and the rate of bacterial growth was not affected. The differentially expressed proteins have roles in ribosomal function, protein synthesis, metabolic processes and transcription. Manuka honey uniquely caused downregulation of two proteins [dihydrolipoamide dehydrogenase (DLD) and elongation factor Tu (EF-Tu)] associated with two of these pathways as well as upregulation of one stress-related protein [cold shock protein C (CspC)]. The proteomic profile following treatment with manuka honey differed from the profiles of other antibacterial agents, indicating a unique mode of action and its potential value as a novel antimicrobial agent.
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PMID:Specific non-peroxide antibacterial effect of manuka honey on the Staphylococcus aureus proteome. 2258 31

Bacterial antioxidants play a vital role in the detoxification of exogenous peroxides. Several antioxidant defenses including low-molecular-weight thiols (LMWTs) and protective enzymes were developed to help the bacterium withstand the adverse stress. Although osmotically induced bacterial protein C (OsmC), classified as the organic hydroperoxide reductase (Ohr)/OsmC superfamily, has been demonstrated in some mycobacterial species, including M. tuberculosis and M. smegmatis, its physiological and biochemical functions in C. glutamicum remained elusive. Here we found the lack of C. glutamicum osmC gene resulted in decreased cell viability and increased intracellular reactive oxygen species accumulation under organic hydroperoxides (OHPs) stress conditions. The osmC expression was induced in the multiple antibiotic resistance regulator MarR-dependent manner by OHPs, and not by other oxidants or osmotic stress. Peroxide reductase activity showed that OsmC had a narrow range of substrates-only degrading OHPs, and detoxified OHPs mainly by linking the alkyl hydroperoxide reductase (AhpD) system (AhpD/dihydrolipoamide dehydrogenase (Lpd)/dihydrolipoamide acyltransferase (SucB)). Site-directed mutagenesis confirmed Cys48 was the peroxidatic cysteine, while Cys114 was the resolving Cys residue that formed an intramolecular disulfide bond with oxidized Cys48. Therefore, C. glutamicum OsmC was a thiol-dependent OHP reductase and played important role of protection against OHPs together with Ohr.
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PMID:OsmC in Corynebacterium glutamicum was a thiol-dependent organic hydroperoxide reductase. 3119 44