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Bioinspired Nanomaterials for Improving Sensing and Imaging Spectroscopy
Published in Kaushik Pal, Nanomaterials for Spectroscopic Applications, 2021
Janti Qar, Alaa A. A. Aljabali, Tasnim Al-Zanati, Mazhar S. Al Zoubi, Khalid M. Al-Batanyeh, Poonam Negi, Gaurav Gupta, Dinesh M. Pardhi, Kamal Dua, Murtaza M. Tambuwala
E2 is derived from the pyruvate-dehydrogenase-multienzyme complex’s E2 central domain (dihydrolipoamide acetyltransferase). The protein consists of 24 subunits in E. coli or 60 subunits Geobacillus stearothermophilus that self-assembly into a hollow system of a cubic central core, or an icosahedron with 12 pores of five nm openings [33]. Pyruvate decarboxylase (E1), dihydrolipoamide acetyltransferase (E2), and dihydrolipoamide dehydrogenase are the enzymes that are unique to pyruvate dehydrogenase (E3). Because the E1 and E3 are not separated, the latter shapes the systemic nucleus of inherent durability in the presence of the E2, which enables long-term survival under harsh environments. The modulation of the exterior surface with functional ligands does not inhibit the assembly of the core domain E2, as is the case with other nanocages, including viral capsids. This function is the same as its natural condition in which the E2 domain is linked to two distinct folding protein domains on its top [33]. E2 protein nanocage can be genetically or chemically engineered in a similar way to other natural protein (viruses) to enable multiple functions such as drug loading and precise delivery. Ren et al. have shown that
Hexavalent chromium bioremediation with insight into molecular aspect: an overview
Published in Bioremediation Journal, 2021
Sreejita Ghosh, Amrita Jasu, Rina Rani Ray
In bacterial respiratory chains, where cytochromes are involved Cr (VI) serves as an electron acceptor because of the presence of the membrane bound Cr (VI) reductase enzyme (Joutey et al. 2015). These membranes associated chromate reductases have been suggested to couple Cr (VI) reduction with NAD (P) H oxidation. Cr (VI) reduction is executed by a membrane bound chromate reductase which is a dihydrolipoamide dehydrogenase and is a fraction of the multi-subunit of the pyruvate dehydrogenase complex (Joutey et al. 2015).
Transcriptome analysis reveals that yeast extract inhibits synthesis of prodigiosin by Serratia marcescens SDSPY-136
Published in Preparative Biochemistry & Biotechnology, 2023
Junqing Wang, Tingting Zhang, Yang Liu, Shanshan Wang, Zerun Li, Ping Sun, Hui Xu
The majority of the enriched DEGs involved in the TCA cycle (ko00020), propanoate metabolism (ko00640), inositol phosphate metabolism (ko00562), pyruvate metabolism (ko00620), and butanoate metabolism (ko00650). TCA showed the greatest enrichment, and the majority of the genes associated in pyruvate metabolism were enriched (Table S1). Pyruvate and malonyl-CoA in the carbon metabolism pathway are important intermediates in prodigiosin synthesis.[13] Two key enzymes in the glycolysis pathway were downregulated: 6-phosphofructokinase (EC:2.7.1.11) and glyceraldehyde 3-phosphate dehydrogenase (phosphorylation) (EC:1.2.1.12). Changes in these enzymes affect pyruvate production. In the TCA cycle, we observed downregulation of pyruvate ferredoxin oxidoreductase (porA, B, C, D, G), which provides thiamin pyrophosphate and catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and CO2.[35] Notably, pyruvate dehydrogenase (aceE), pyruvate dehydrogenase E1 (PDHA, B), and dihydrolipoamide dehydrogenase (DLD) were slightly upregulated (Figure 5). These genes are critical for maintaining normal TCA cycle turnover and increasing pyruvate-to-acetyl-CoA flow.[36] Other genes in the citric acid cycle, such as isocitrate dehydrogenase (icd), 2-ketoglutarate dehydrogenase (OGDH; kgd; DLST), succinyl-CoA synthase (sucCD; LSC1, 2), fumarate hydration enzymes (fumA, B, C, D, E), malate dehydrogenase (mqo), and malate dehydrogenase (MDH1, 2) were also upregulated. The products of these genes are involved in providing energy and carbon skeletons for metabolism in S. marcescens. The expression of phosphoenol pyruvate carboxykinase, which is involved in carbon fixation via pyruvate metabolism, showed an increasing trend at the gene level. The conversion of malonyl-CoA to acetyl-CoA was enhanced, whereas the derivatization of pyruvate to formic and acetic acids was weakened. The regulation of other pyruvate genes is shown in Figure 5. The upregulation of these carbon metabolism genes suggests that S. marcescens carbon metabolism is regulated to compensate for the energy deficit. This may indirectly affect prodigiosin biosynthesis.