Exopolysaccharide Production from Marine Bacteria and Its Applications
Se-Kwon Kim in Marine Biochemistry, 2023
EPSs act as natural bioflocculant and well replace chemical flocculants. B. cereus SK has been reported for its significant bioflocculant activity (Busi et al., 2017). EPSs of Corynebacterium glutamicum and Bacillus sp. As-101 also exhibited noticeable flocculation activity (Salehizadeh et al., 2000; He et al., 2004). EPS-producing Pseudomonas and Staphylococcus spp. were found to possess bioflocculant properties, and a novel bioflocculant MM1 was reported from the EPSs produced by these bacteria. Similarly, a consortia of Rhizobium radiobacter F2 and B. sphaeicus F6 and of Oceanobacillus and Halobacillus spp. have been applied in the industrial wastewater and river water treatments due to the bioflocculant properties of EPSs produced by them (Zhang et al., 2007; Wang et al., 2011; Cosa et al., 2014; Vijayendra and Shamala, 2014).
Monoterpenes-Based Pharmaceuticals: A Review of Applications In Human Health and Drug Delivery Systems
Megh R. Goyal, Durgesh Nandini Chauhan in Plant- and Marine-Based Phytochemicals for Human Health, 2018
Sarria et al.117 did a combinatory screening of GPPS and PS enzymes from different species of coniferous trees to improve flux of pinene production in engineered E. coli.43 They constructed GPPS-PS protein fusions in order to reduce GPP inhibition of GPPS activity, and concluded that Abies grandis GPPS-PS fusion produced the highest amount of pinene (32 mg/L). Beside E. coli, other microorganisms such as Corynebacterium glutamicum were metabolically engineered to produce pinene.64
Structural Profiling of Bioactive Compounds with Medicinal Potential from Traditional Indian Medicinal Plants
Jayanta Kumar Patra, Gitishree Das, Sanjeet Kumar, Hrudayanath Thatoi in Ethnopharmacology and Biodiversity of Medicinal Plants, 2019
The killing effect of benzoic acid on Burkholderia xenovorans has been studied, and several targets were reported such as amidase, putative carbon-nitrogen hydrolase protein, 2-hydroxy-6-oxo-6-phenylhexa-2, 4-dienoate hydrolase (BphD), benzoate 1, 2-dioxygenase (BenA, BenB, and BenC), benzaldehyde dehydrogenase and benzoate-coenzyme A ligase. While amidase and putative carbon-nitrogen hydrolase protein affect virulence factor, others can block drug metabolism (Stitch 4.0.). Another virulence factor such as AmtR, a transcriptional regulator that present in Corynebacterium glutamicum can be inhibited by p-cymene. Kovac et al., studied the target action of α-pinene in Campylobacter jejuni and found it can bind to HrcA and HspR which are efflux pump proteins of the bacteria (Kovac et al., 2015). The most studied phytocompounds against E. coli are berberine, chlorogenic acid, cinnamaldehyde, EGCG, quercetin diacylglycoside, thymoquinone, curcumin, linoleic acid, and sabinene. Among them, curcumin, EGCG and quercetin diacylglycoside possess multiple targets in E. coli. The targets of curcumin are dihydropteridine reductase, FtsZ, predicted NADP-dependent, Zn-dependent oxidoreductase and tyrosine kinase which can block synthesis of nucleotides and amino acids, bacterial division, drug metabolism, extracellular polysaccharide, and colanic acid synthesis respectively (Stitch 4.0.). While EGCG has only two targets-Fab G and Fab I which function in fatty acid biosynthesis (Zhang and Rock, 2004). Like EGCG, linoleic acid also can target on Fab I. Quercetin diacylglycoside targets on DNA gyrase B (Suriyanarayanan et al., 2013) and topoisomerase IV (Hossion et al., 2011) which are responsible for negative supercoiling of DNA and resolution of chromosome dimers at DNA replication. Sabinene inhibits the adhesion of E. Coli to host cells by binding to YfcC, a predicted membrane protein.
Mycobacterial ethambutol responsive genes and implications in antibiotics resistance
Published in Journal of Drug Targeting, 2021
Xiaohong Xiang, Zhen Gong, Wanyan Deng, Qingyu Sun, Jianping Xie
The well-known target(s) of EMB are arabinosyl transferases associated with biosynthesis of AG and LAM, which are main component of mycobacterial cell wall [23,24]. EMB inhibited arabinan synthesis will abolish the mycolic acid anchoring site, thereby reducing the cell wall accumulation of mycolic acids and damaging the integrity of cell wall and culminating in cell death [25]. This mechanism is not limited to M. tuberculosis, emb mutant or EMB-treated wild-type Corynebacterium glutamicum (C. glutamicum) exhibiting morphological variation and slower growth, the AG structure in the cell wall is truncated, and mycolic acid is reduced [26]. EMB resistance is mainly caused by mutations in related genes that affect AG biosynthesis and bioactivity, and changes in EMB target genes. EMB enhances cell wall permeability by inhibiting the formation of mycolic acid–arabinoglycan peptidoglycan complex, which facilitates the other antituberculous drugs to reach their target. Hence, EMB and RFP have a synergistic effect when used in anti-TB treatment [24]. At the same time, bacterial resistance to EMB, INH and RFP often occurs simultaneously, and resistance pattern of INH and EMB in M. tuberculosis isolates is more common than INH, EMB and RMP [8].
Insights into structures of imidazo oxazines as potent polyketide synthase XIII inhibitors using molecular modeling techniques
Published in Journal of Receptors and Signal Transduction, 2020
Shanthakumar B., Kathiravan M. K.
It is proposed that fadD32 and the acyl CoA carboxylase gene accD4 of the fadD32-PKS13-accD4 core encodes the enzymes necessary for activation of 2 fatty acyl substrates for condensation reaction toward mycolic acid biosynthesis by PKS13. Mutational studies from Mycobacterium smegmatis and Corynebacterium glutamicum reveals that deletions or alterations in PKS13 results in improper cell wall formation with severe mycolic acid deficiency. fadD32 catalyzes the activation by adenylation and transfer of meromycolate chain on to PKS13. AccD4 is involved in activation of acyl Co A by carboxylation at C2 leading to the formation of 2-carboxy acyl CoA which ultimately serves as a real substrate for condensation reaction catalyzed by PKS13 [6,7].
Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production in Porphyromonas gingivalis
Published in Journal of Oral Microbiology, 2019
Yasuo Yoshida, Mitsunari Sato, Takamasa Nonaka, Yoshiaki Hasegawa, Yuichiro Kezuka
Bacterial genes are often organized in operons with regulatory units that control genes/proteins with associated functions. The RT-PCR analysis demonstrated that ack and pta genes constitute an operon in P. gingivalis (Figure 7), as has also been shown for homologous genes in several bacteria including E. coli [15] and Corynebacterium glutamicum [62]. Transcription of the PGN_1180 gene is independent from pta and ack. The PGN_1180 protein, the function of which has not been assigned, is therefore presumably not associated with ATP production.
Related Knowledge Centers
- Bacteria
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