EC Number | Cloned (Comment) | Organism |
---|---|---|
2.5.1.78 | expression in Escherichia coli | Brucella sp. |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
2.5.1.78 | - |
Brucella sp. |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.5.1.78 | 18000 | - |
10 * 18000, it is demonstrated by means of solution light scattering and X-ray structural analyses that the enzyme assembles as a very stable dimer of pentamers. A mechanism for dissociation/unfolding of this macromolecular assembly is postulated | Brucella sp. |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.78 | 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate | Brucella sp. | penultimate step of riboflavin biosynthesis | 6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O | - |
? |
EC Number | Organic Solvent | Comment | Organism |
---|---|---|---|
2.5.1.78 | guanidine-HCl | produces a cooperative and reversible change in the tertiary structure reflected by a decrease in tryptophan fluorescence emission. In addition, guanidine-HCl incubation produces a complete loss of secondary structure of BLS as monitored by CD spectra | Brucella sp. |
2.5.1.78 | urea | 8 M, the absence of structural changes indicates that the quaternary arrangement of the enzyme is very stable | Brucella sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.5.1.78 | Brucella sp. | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.5.1.78 | - |
Brucella sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.5.1.78 | 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate | penultimate step of riboflavin biosynthesis | Brucella sp. | 6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.5.1.78 | decamer | 10 * 18000, it is demonstrated by means of solution light scattering and X-ray structural analyses that the enzyme assembles as a very stable dimer of pentamers. A mechanism for dissociation/unfolding of this macromolecular assembly is postulated | Brucella sp. |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.5.1.78 | BLS | - |
Brucella sp. |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.5.1.78 | 20 | - |
the higher molecular order of the decameric enzyme increases its stability at 20°C compared with pentameric lumazine synthases | Brucella sp. |
2.5.1.78 | 88 | - |
melting temperature. The loss of secondary structure is not recovered after slow cooling of the samples, indicating that an irreversible unfolding takes place under these conditions | Brucella sp. |