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Literature summary for 2.5.1.9 extracted from

  • Kim, R.R.; Illarionov, B.; Joshi, M.; Cushman, M.; Lee, C.Y.; Eisenreich, W.; Fischer, M.; Bacher, A.
    Mechanistic insights on riboflavin synthase inspired by selective binding of the 6,7-dimethyl-8-ribityllumazine exomethylene anion (2010), J. Am. Chem. Soc., 132, 2983-2990.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant N-terminal domain of riboflavin synthase is prepared Escherichia coli

Protein Variants

Protein Variants Comment Organism
T50A production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude Escherichia coli
T67A production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude 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 enzyme catalyzes the transfer of a four-carbon unit between 2 molecules of the substrate, 6,7-dimethyl-8-ribityllumazine riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6,7-dimethyl-8-(1-D-ribityl)lumazine enzyme catalyzes the transfer of a four-carbon unit between 2 molecules of the substrate, 6,7-dimethyl-8-ribityllumazine Escherichia coli riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
-
?

Synonyms

Synonyms Comment Organism
riboflavin synthase
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Escherichia coli