EC Number   |
General Information |
Reference |
|---|
    2.5.1.78 | 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 |
738204 |
| 2.5.1.78 | metabolism |
enzyme AaLS catalyzes the penultimate step in riboflavin biosynthesis |
739639 |
| 2.5.1.78 | 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 |
759481 |
| 2.5.1.78 | 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 |
739125 |
| 2.5.1.78 | 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 |
737922 |
| 2.5.1.78 | 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 |
738204 |
| 2.5.1.78 | more |
modelling of the lumazine synthase/riboflavin synthase complex |
738204 |
| 2.5.1.78 | more |
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 |
738788 |
| 2.5.1.78 | more |
the enzyme carries an N-terminal extension typical for plant riboflavin biosynthetic proteins |
739125 |
| 2.5.1.78 | physiological function |
Brucella lumazine synthase (BLS) molecule is a favorable transport vector for antigenic protein |
737479 |
