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evolution
in Bacillaceae, lumazine synthase and riboflavin synthase form a structurally unique complex comprising an icosahedral shell of 60 lumazine synthase subunits and a core of three riboflavin synthase subunits, whereas many other bacteria have empty lumazine synthase capsids, fungi, Archaea and some eubacteria have pentameric lumazine synthases, and the riboflavin synthases of Archaea are paralogues of lumazine synthase. The quaternary structure of the icosahedral beta subunit capsids undergoes drastic changes, resulting in formation of large, quasi-spherical capsids
evolution
in Bacillaceae, lumazine synthase and riboflavin synthase form a structurally unique complex comprising an icosahedral shell of 60 lumazine synthase subunits and a core of three riboflavin synthase subunits, whereas many other bacteria have empty lumazine synthase capsids, fungi, Archaea and some eubacteria have pentameric lumazine synthases, and the riboflavin synthases of Archaea are paralogues of lumazine synthase. The quaternary structure of the icosahedral beta subunit capsids undergoes drastic changes, resulting in formation of large, quasi-spherical capsids
evolution
in Bacillaceae, lumazine synthase and riboflavin synthase form a structurally unique complex comprising an icosahedral shell of 60 lumazine synthase subunits and a core of three riboflavin synthase subunits, whereas many other bacteria have empty lumazine synthase capsids, fungi, Archaea and some eubacteria have pentameric lumazine synthases, and the riboflavin synthases of Archaea are paralogues of lumazine synthase. The quaternary structure of the icosahedral beta subunit capsids undergoes drastic changes, resulting in formation of large, quasi-spherical capsids
metabolism
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enzyme AaLS catalyzes the penultimate step in riboflavin biosynthesis
metabolism
lumazine synthase is involved in the riboflavin biosynthetic pathway and catalyzes the condensation of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione with 3,4-dihydroxy-2-butanone-4-phosphate, which is obtained from ribulose 5-phosphate by 3,4-dihydroxy-2-butanone-4-phosphate synthase (DHBPS), yielding 6,7-dimethyl-8-ribityllumazine. Proposd riboflavin biosynthetic pathway in plants, overview
metabolism
the enzyme is involved in the riboflavin biosynthesis pathway. The RibA protein is rate limiting in the pathway, reductase activity of RibG and lumazine synthase (RibH) might be the next most limiting steps. Computational minimization of the enzyme concentrations of the pathway suggests the need for a greater RibH enzyme concentration (0.251 mM) compared with the other enzymes (RibG 0.188 mM, RibB 0.023 mM). Kinetic modelling of the interaction of the single enzymes and identification of rate-limiting steps in the biosynthetic pathway. The potential order of enzyme limitation under increasing RibA concentration is as follows: the reductase activity of RibG and the lumazine synthase (RibH) are rather more limiting than riboflavin synthase (RibB) and the deaminase activity of RibG
metabolism
the xylene ring of riboflavin (vitamin B2) is assembled from two molecules of 3,4-dihydroxy-2-butanone 4-phosphate by a mechanistically complex process that is jointly catalyzed by lumazine synthase and riboflavin synthase as part of the riboflavin pathway, overview
metabolism
the xylene ring of riboflavin (vitamin B2) is assembled from two molecules of 3,4-dihydroxy-2-butanone 4-phosphate by a mechanistically complex process that is jointly catalyzed by lumazine synthase and riboflavin synthase as part of the riboflavin pathway, overview
metabolism
the xylene ring of riboflavin (vitamin B2) is assembled from two molecules of 3,4-dihydroxy-2-butanone 4-phosphate by a mechanistically complex process that is jointly catalyzed by lumazine synthase and riboflavin synthase as part of the riboflavin pathway, overview
metabolism
the xylene ring of riboflavin (vitamin B2) is assembled from two molecules of 3,4-dihydroxy-2-butanone 4-phosphate by a mechanistically complex process that is jointly catalyzed by lumazine synthase and riboflavin synthase as part of the riboflavin pathway, overview
metabolism
lumazine synthase forms specific inclusion complexes with riboflavin synthase when both proteins are co-expressed in a heterologous host. Encapsulation of specific enzymes in self-assembling protein cages is a hallmark of bacterial compartments that function as counterparts to eukaryotic organelles
physiological function
disruption mutants of either isform RibH1 or RibH2 obtained without any major difficulty, are not auxotrophic for riboflavin and grow at wild-type rates in both rich and minimal media. A double mutant lacking both RibH1 and RibH2 activity is not viable
physiological function
disruption mutants of either isform RibH1 or RibH2 obtained without any major difficulty, are not auxotrophic for riboflavin and grow at wild-type rates in both rich and minimal media. A double mutant lacking both RibH1 and RibH2 activity is not viable. For virulence, at least one isoform must be present for Brucella abortus survival and RibH2 and not RibH1 is essential for intracellular survival due to its luminazine synthase activity in vivo.
physiological function
Brucella lumazine synthase (BLS) molecule is a favorable transport vector for antigenic protein
physiological function
lumazine synthase (BLS) is a highly immunogenic decameric protein which can accept the fusion of foreign proteins at its ten N-termini. These chimeras are very efficient to elicit systemic and oral immunity without adjuvants. BLS signaling via Toll-like receptor 4 (TLR4) regulates innate and adaptive immune responses, inducing dendritic cell maturation and CD8+ T-cell cytotoxicity
physiological function
lumazine synthase from Brucella spp.is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity
physiological function
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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.Maternal immunization with BLSStx2B protein antigen as a possible approach for transferring anti-Stx2 protection to the offspring
physiological function
the enzyme 6,7-dimethyl-8-(d-ribityl)lumazine synthase is part of the riboflavin biosynthesis pathway essential to fungi and bacteria
physiological function
the enzyme is a strong Brucella antigen
physiological function
the enzyme is involved in the riboflavin biosynthesis pathway. Riboflavin or vitamin B2 is the precursor of the flavin cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), and is used commercially as an animal feed supplement and as a food colorant (E101)
physiological function
the lumazine synthase molecule from Brucella significantly promotes the immune-stimulation effects of antigenic proteins, e.g Omp31, overview
physiological function
lumazine synthase forms cage complexes with the cognate riboflavin synthase when both proteins are coproduced in the cytosol of Escherichia coli. A 12-amino acid-long peptide at the C terminus of riboflavin synthase serves as a specific localization sequence responsible for targeting the guest to the protein compartment
physiological function
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lumazine synthase from Brucella spp.is a highly immunogenic decameric protein which can accommodate foreign polypeptides or protein domains fused to its N-termini, markedly increasing their immunogenicity
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additional information
modelling of the lumazine synthase/riboflavin synthase complex
additional information
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molecular modelling of the recombinant BLS-Stx2B chimera fusing the C-terminal end of the structure of Stx2B, PDB ID IR4P, with the N-terminus of the crystallographic structure of enzyme BLS, PDB ID IDI0, through a decapeptide linker of sequence GSGSGSGSGS
additional information
the enzyme carries an N-terminal extension typical for plant riboflavin biosynthetic proteins
additional information
the enzyme carries an N-terminal extension typical for plant riboflavin biosynthetic proteins