2.5.1.78: 6,7-dimethyl-8-ribityllumazine synthase
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For detailed information about 6,7-dimethyl-8-ribityllumazine synthase, go to the full flat file.
Word Map on EC 2.5.1.78
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2.5.1.78
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brucella
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capsid
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icosahedral
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aquifex
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aeolicus
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brucellosis
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4-phosphate
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pentamer
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abortus
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3,4-dihydroxy-2-butanone
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5-amino-6-ribitylamino-2,41h,3h-pyrimidinedione
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medicine
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guest
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decameric
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supercharged
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homopentamer
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nanocompartments
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60-subunit
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biotechnology
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synthesis
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molecular biology
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analysis
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drug development
- 2.5.1.78
- brucella
-
capsid
-
icosahedral
-
aquifex
- aeolicus
- brucellosis
- 4-phosphate
-
pentamer
- abortus
- 3,4-dihydroxy-2-butanone
-
5-amino-6-ribitylamino-2,41h,3h-pyrimidinedione
- medicine
-
guest
-
decameric
-
supercharged
-
homopentamer
-
nanocompartments
-
60-subunit
- biotechnology
- synthesis
- molecular biology
- analysis
- drug development
Reaction
Synonyms
6,7-dimethyl-8-(d-ribityl)lumazine synthase, 6,7-dimethyl-8-ribityllumazine synthase, 6,7-dimethyl-8-ribityllumazine synthase 1, 6,7-dimethyl-8-ribityllumazine synthase 2, 6,7-dimethyl-8-ribityllumazine-synthase, AaLS, BLS, DMRL synthase, DMRL synthase 2, heavy riboflavin synthase, LcLS1, LcLS2, lumazine synthase, lumazine synthase 1, lumazine synthase 2, lumazine synthase/riboflavin synthase complex, lumazinesynthase/riboflavin synthase complex, lumazinesynthase/riboflavin synthase complex, icosahedral capsid of 60 beta subunits enclosing a triplet of alpha subunits, luminazine synthase, MbtLS, MJ0303, Pbls, RIB4, ribE, RibH, ribH1, RibH1 protein, RibH2, type I lumazine synthase, type II lumazine synthase
ECTree
2.5.1.78 6,7-dimethyl-8-ribityllumazine synthaseAdvanced search results
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Application on EC 2.5.1.78 - 6,7-dimethyl-8-ribityllumazine synthase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
development and characterization of an in vivo applicable magnetic resonance positive contrast agent by conjugating Gd(III)-chelating agent complexes to lumazine synthase isolated from Aquifex aeolicus (AaLS). The r1 relaxivity of Gd(III)-DOTA-AaLS-R108C is 16.49 mM/s and its r1/r2 ratio is 0.52 at the magnetic field strength of 7 T. The results of 3D MR angiography demonstrate the feasibility of vasculature imaging within 2 h of intravenous injection of the agent and a significant reduction in T1 values observed in the tumor region 7 h post-injection in the SCC-7 flank tumor model. Gd(III)-DOTA-AaLS-R108C can serve as a potential theranostic nanoplatform at high magnetic field strength
biotechnology
drug development
the enzyme is a potential drug target for the development of broad-spectrum antifungal drugs
medicine
molecular biology
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outside of the cell, the hollow spherical architecture of the enzyme capsid is used as a template for the encapsulation of cargo proteins, such as green fluorescent proteins, and HIV proteases, and fabrication of uniform layer-by-layer assemblies using non-covalent interactions between surface-displayed His6 and Ni-NTA of enzyme AaLS. The enzyme shows encapsulation capability and surface presentation of ligands, which represent the great potential of AaLS as a versatile delivery vehicle
synthesis
Bacillus subtilis is used for riboflavin production, also involving the enzyme RibH
additional information
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protection of mice against Shiga toxin 2 (Stx2)-associated damage by maternal immunization with a Brucella lumazine synthase-Stx2 B subunit chimera. The enzyme can be useful in vaccine development against enterohemorrhagic Shiga toxin (Stx)-producing Escherichia coli (EHEC), which causes a prodromal hemorrhagic enteritis, remaining the most common etiology of the typical or epidemic form of hemolytic-uremic syndrome. The EHEC challenge contributes to sustain a specific and protective immune response against Stx2
biotechnology
a circularly permuted variant of lumazine synthase affords versatile building blocks for the construction of nanocompartments that can be easily produced, tailored, and diversified. The topologically altered protein self-assembles into spherical and tubular cage structures with morphologies that can be controlled by the length of the linker connecting the native termini. Permutated lumazine synthase proteins integrate into wild-type and other engineered lumazine synthase assemblies by coproduction in Escherichia coli to form patchwork cages. This coassembly strategy enables encapsulation of guest proteins in the lumen, modification of the exterior through genetic fusion, and tuning of the size and electrostatics of the compartments
biotechnology
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the C-terminal tail of ribiflavin synthase can act as an encapsulation tag capable of targeting other proteins to the lumazine synthase capsid interior. Fusion of to either the last 11 or the last 32 amino acids of riboflavin synthase, yields variant GFP11 or GFP32, respectively. After purification, lumazine synthase capsids that have been coproduced in bacteria with GFP11 and GFP32 are 15- and 6fold more fluorescent, respectively. GFP11 is localized within the lumazine synthase capsid. Fusing the last 11 amino acids of riboflavin synthase to the C-terminus of the Abrin A chain also leads to its encapsulation by lumazine synthase at a level similar to that of GFP11. Mild changes in pH and buffer identity trigger dissociation of the GFP11 guest
medicine
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Brucella lumazine synthase can be used as both an antigen-carrier and as an adjuvant in the design of new oral subunit vaccines
medicine
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certain purinetriones bearing phosphate side chains can inhibit both lumazine synthase as well as riboflavin synthase, and molecular modeling with 3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate suggests possible binding modes to each enzyme. Antibiotics that would inhibit both lumazine synthase and riboflavin synthase would be less likely to suffer from the development of antibiotic resistance by the organisms that they are supposed to treat, since pathogenic microorganisms would have to simultaneously select for mutations in both enzymes in order to escape the cytotoxic effects of the antibiotics
medicine
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feasibility of using Brucella spp. lumazine synthase as a novel and effective delivery system to induce a protective immune response against rotavirus disease. In particular, previous results showing the plasticity of the Brucella spp. lumazine synthase scaffold for the production of polyvalent chimeras suggest that VP8 from different strains can be coupled to Brucella spp. lumazine synthase in order to elicit wide-protecting neutralizing antibodies against different field strains of rotavirus
medicine
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lumazine synthase is a potent delivery system for the improvement of subunit vaccines
medicine
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the fact that the enzymes of the riboflavin biosynthesis pathway are not present in the human or animal host makes them potential targets for anti-infective agents
medicine
this protein constitutes an interesting candidate for serological diagnosis and for the design of specific chemotherapeutic agents, and its polymeric characteristics could provide the basis for the development of an acellular vaccine
medicine
Brucella suis lumazine synthase (BLS) molecule is a favorable transport vector for antigenic protein, e.g. rL7/L12-BLS fusion protein, in vaccination, e.g. for antibody production in Oryctolagus cuniculus. The BLS molecule also has adjuvant property for improving immunity stimulation effects, when a foreign protein antigen is covalently attached to it
medicine
partially protective effect of enzyme BLS against B16 melanoma in mice generating a protective response at the first stages of tumor growth but not at later stages, therapeutic effect of BLS vaccination
medicine
the BLS scaffold is assessed for in plants for recombinant vaccine development by N-terminally fusing BLS to bovine rotavirus VP8d and expressing the resulting fusion (BLS-VP8d) in Nicotiana tabacum chloroplasts. BLS-VP8d remains soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature
medicine
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the striking feature of enterohemorrhagic Escherichia coli (EHEC) infections is the production of Shiga toxins (Stx) implicated in the development of the life-threatening hemolytic uremic syndrome. Immunization with a chimera consisting of the B subunit of Shiga toxin type 2 and Brucella sp. lumazine synthase confers total protection against Shiga toxins in mice, analysis of antibody efficacy against EHEC challenge. The enzyme can be used as transport vehhicle and antigen in vaccination against EHEC infections
medicine
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evalutation of the immunogenicity and protection ability of a recombinant adenovirus and plasmid DNA vaccine coexpressing P39 and lumazine synthase proteins. The immunization strategy of DNA priming followed by adenovirus boosting induces robust humoral and cellular immune responses, and it significantly reduces the numbers of Brucella abortus in a mouse model
medicine
generation of a chimeric protein (BLS-FliC131) by fusing flagellin from Salmonella typhimurium in the N-termini of BLS. The fusion protein is recognized by anti-flagellin and anti-BLS antibodies, keeps the oligomerization capacity of BLS, without affecting the folding of the monomeric protein components. The thermal stability of each fusion partner is conserved. BLS-FliC131 retains the capacity of triggering TLR5. The humoral response against BLS elicited by BLS-FliC131 is stronger than the one elicited by equimolar amounts of BLS1FliC
medicine
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use of lumazine synthase as a scaffold to present 60 copies of a linear B cell epitope (PB10) from the ricin toxin fused to the C-terminus of lumazine synthase via four different linkers. Fusion of the PB10 peptide onto lumazine synthase does not affect protein assembly, thermal stability or exposure of the epitope, but has a minor impact on protein conformation. Formaldehyde crosslinking considerably improves protein thermal stability with only minor impact on protein conformation. All lumazine synthase-PB10 constructs, when administered to mice by injection without adjuvant, elicites measurable anti-ricin serum IgG titers, although the titers are not sufficient to confer protection against a 10x lethal dose ricin challenge
medicine
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generation of a chimeric protein (BLS-FliC131) by fusing flagellin from Salmonella typhimurium in the N-termini of BLS. The fusion protein is recognized by anti-flagellin and anti-BLS antibodies, keeps the oligomerization capacity of BLS, without affecting the folding of the monomeric protein components. The thermal stability of each fusion partner is conserved. BLS-FliC131 retains the capacity of triggering TLR5. The humoral response against BLS elicited by BLS-FliC131 is stronger than the one elicited by equimolar amounts of BLS1FliC
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medicine
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the BLS scaffold is assessed for in plants for recombinant vaccine development by N-terminally fusing BLS to bovine rotavirus VP8d and expressing the resulting fusion (BLS-VP8d) in Nicotiana tabacum chloroplasts. BLS-VP8d remains soluble and stable during all stages of plant development and even in lyophilized leaves stored at room temperature
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