Crystallization (Comment) | Organism |
---|---|
substrate binding site structure analysis of Aquifex aeolicus lumazine synthase in complex with the inhibitor 3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid | Aquifex aeolicus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | homotopical sequence insertion into icosahedral lumazine synthase resulting in large particles. Mutations at the phosphate binding site Arg127 perturb enzymatic activity and also capsid assembly. The central channel of the pentameric building blocks appear significantly widened, indicating that the mode of interaction between the pentamer units and the topology of the subunit interfaces must have undergone significant changes, overview | Aquifex aeolicus |
R127H | site-directed mutagenesis, the mutant shows 37% reduced activity compared to the wild-type enzyme | Aquifex aeolicus |
R127K | site-directed mutagenesis, the mutant shows 91% reduced activity compared to the wild-type enzyme | Aquifex aeolicus |
General Stability | Organism |
---|---|
role of electrostatic interactions for the stability of beta60 enzyme particles, pentamers of beta subunits have maximal stability at a pH of approximately pH 8.0 and are more stable than dimers or trimers | Aquifex aeolicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid | binding structure, overview | Aquifex aeolicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | Bacillus subtilis | - |
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? | |
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | Saccharomyces cerevisiae | - |
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? | |
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | Aquifex aeolicus | - |
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? | |
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | Brucella abortus | - |
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aquifex aeolicus | O66529 | gene ribH | - |
Bacillus subtilis | P11998 | gene ribH | - |
Brucella abortus | Q2YKV1 | gene ribH2; gene ribH2 | - |
Brucella abortus | Q2YNC6 | gene ribH1; gene ribH1 | - |
Saccharomyces cerevisiae | P50861 | gene Rib4 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | critical involvement of the active-site residues Phe22, His88 and Arg127 in substrate binding and catalysis | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | - |
Bacillus subtilis | 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? | |
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | - |
Saccharomyces cerevisiae | 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? | |
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | - |
Aquifex aeolicus | 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? | |
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil | - |
Brucella abortus | 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate | - |
? | |
additional information | critical involvement of the active-site residues Phe22, His88 and Arg127 in substrate binding and catalysis | Bacillus subtilis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
decamer | the d5-symmetric protein is a dimer of pentamers | Brucella abortus |
More | structure analysis and comparisons, overview | Bacillus subtilis |
More | structure analysis and comparisons, overview | Saccharomyces cerevisiae |
More | structure analysis and comparisons, overview | Aquifex aeolicus |
More | structure analysis and comparisons, overview | Brucella abortus |
pentamer | the lumazine protein folds into two closely similar domains | Bacillus subtilis |
pentamer | the lumazine protein folds into two closely similar domains, the enzyme forms a dodecamer of pentamers, electrostatic model calculations | Saccharomyces cerevisiae |
pentamer | the lumazine protein folds into two closely similar domains, the enzyme forms a dodecamer of pentamers, electrostatic model calculations | Aquifex aeolicus |
Synonyms | Comment | Organism |
---|---|---|
DMRL synthase | - |
Saccharomyces cerevisiae |
lumazine synthase | - |
Bacillus subtilis |
lumazine synthase | - |
Saccharomyces cerevisiae |
lumazine synthase | - |
Aquifex aeolicus |
lumazine synthase | - |
Brucella abortus |
RIB4 | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
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 | Bacillus subtilis |
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 | Aquifex aeolicus |
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 | Brucella abortus |
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 | Bacillus subtilis |
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 | Saccharomyces cerevisiae |
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 | Aquifex aeolicus |
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 | Brucella abortus |
additional information | modelling of the lumazine synthase/riboflavin synthase complex | Bacillus subtilis |
physiological function | the enzyme is a strong Brucella antigen | Brucella abortus |