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Literature summary for 2.5.1.9 extracted from

  • Kis, K.; Bacher, A.
    Substrate channeling in the lumazine synthase/riboflavin synthase complex of Bacillus subtilis (1995), J. Biol. Chem., 270, 16788-16795.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information sigmoidal kinetics is observed with mixtures of artifactual beta 60 capsids and alpha subunit trimers. Km value for lumazine of the lumazine synthase/riboflavin synthase complex is about 10 times larger as compared to light riboflavin synthase consisting of alpha subunits, without lumazine synthase activity Bacillus subtilis
0.13
-
6,7-dimethyl-8-(1'-D-ribityl)lumazine pH 7.0, 37°C Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
lumazine synthase/riboflavin synthase complex, the alpha subunit carries riboflavin synthase activity
-

Reaction

Reaction Comment Organism Reaction ID
2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine formation of riboflavin by the lumazine synthase/riboflavin synthase complex follows a leaky channel model Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6,7-dimethyl-8-(1-D-ribityl)lumazine
-
Bacillus subtilis riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione catalysed by the alpha-subunit, which forms a trimer surrounded by an icosahedral capsid of 60 beta subunits producing substrate 6,7-dimethyl-8-(1-D-ribityl)lumazine ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.019
-
6,7-dimethyl-8-ribityllumazine pH 7.0, 37°C Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
both lumazine synthase and riboflavin synthase activity Bacillus subtilis