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Oliveira, R.F. & Almada, V.C. 1996. Dominance hierarchies and social structure in captive groups of the Mozambique tilapia Oreochromis mossambicus (Teleostei: Cichlidae). Ethology Ecology and Evolution 8(1): 39-55. PDF
Rs Salaria Data Structure Pdf 51
The reconstruction of heterologous BIA pathways into microbes is an exciting area of research, with significant progress being made in recent years: the in vivo BIA pathway in Escherichia coli and Saccharomyces cerevisiae have been reported with the production of natural BIAs13,14,15,16,17,18. Pathways to BIAs have also been achieved using enzyme cascade reactions in vitro in high yields19. The NCS Pictet-Spenglerase reaction is the key step to construct the BIA skeleton in such approaches13,19. Previous work has established the NCS mechanistic requirement for the arylethylamine meta-hydroxyl group, which binds into the NCS active site, and is deprotonated to enable ring formation20,21. We have reported a recombinant tyrosinase from Candidatus Nitrosopumilus salaria BD31 (CnTYR) able to effectively convert 4 to L-DOPA 5 without the requirement for expensive co-factors, generating the required meta-hydroxyl moeity19. Additionally a tyrosine decarboxylase from Enterococcus faecalis DC32 (EfTyrDC) was developed for the decarboxylation of 5 and these were used in cascades to generate BIAs (Fig. 1b). However, such cascades do not have to follow the natural pathway starting from L-tyrosine 4. They can be designed combining other enzymes in different orders, or other substrates, to enable the production of non-natural BIAs.
WT-CnTYR and the variant N201S (homology modelled) with L-tyrosine 4, meta-L-tyrosine 9 and halogenated tyrosines 11 and 12 using AutoDock Vina35. a Docking of L-tyrosine 4 with the wild-type (WT) CnTYR and CnTYR-N201S: L-tyrosine 1 fits well into the active sites of WT-CnTYR and CnTYR-N201S. b Docking of meta-L-tyrosine 9 with the WT-CnTYR: 9 can fit into the active site of WT-CnTYR but not in a productive orientation. c Docking of 9 with CnTYR-N201S: 9 fits well into the active site of CnTYR-N201S. d Docking of 3-F-L-tyrosine 11 with WT-CnTYR and CnTYR-N201S: 11 fits well into the active site of both. e Docking of 3-Cl-L-tyrosine 12 with WT-CnTYR: 12 can fit into the active sites WT-CnTYR but not in a productive orientation. f Docking of 12 with CnTYR-N201S: 12 fits well into the active sites of CnTYR-N201S. The functional histamine residues in the tyrosinase active sites and substrates are shown in stick and ribbon forms. Enzyme residues are shown in tan. Compounds 4, 9, 11, and 12 are shown in grey, rose, blue, and light blue, respectively. The model of WT-CnTYR was generated by homology modelling (SWISS-MODEL)37 using the crystal structure of BmTYR (PDB code: 3NPY)36 as a template. CnTYR variants were generated and homology modelled by Chimera38,39,40.
Modern memory devices may suffer from faults, where some bits may arbitrarily flip and corrupt the values of the affected memory cells. The appearance of such faults may seriously compromise the correctness and performance of computations. In recent years, many algorithms for computing in the presence of memory faults have been introduced in the literature: in particular, an algorithm or a data structure is called resilient if it is able to work correctly on the set of uncorrupted values. In this invited talk I will survey recent work on resilient algorithms and data structures. 2ff7e9595c
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