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Literature summary for 2.5.1.9 extracted from

  • Meining, W.; Eberhardt, S.; Bacher, A.; Ladenstein, R.
    The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6 A resolution (2003), J. Mol. Biol., 331, 1053-1063.
    View publication on PubMed

Application

Application Comment Organism
additional information the enzyme is a target for development of antimicrobial drugs Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant homodimeric N-terminal enzyme domain in complex with riboflavin, 7 mg/ml protein in 70 mM sodium potassium phosphate, pH 7.0, and 100 mM sodium chloride, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular modeling Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6,7-dimethyl-8-(1-D-ribityl)lumazine Escherichia coli ultimate step in the biosynthesis of riboflavin, i.e. vitamin B2, the precursor of flavin cofactors riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AFU8
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-

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 active site structure and catalytic mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6,7-dimethyl-8-(1-D-ribityl)lumazine dismutation Escherichia coli riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione riboflavin binding site structure ?
6,7-dimethyl-8-(1-D-ribityl)lumazine ultimate step in the biosynthesis of riboflavin, i.e. vitamin B2, the precursor of flavin cofactors Escherichia coli riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione
-
?

Subunits

Subunits Comment Organism
trimer subunit fold and arrangement, beta-barrel capped by short alpha-helices on each side, overview Escherichia coli