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Literature summary for 2.5.1.9 extracted from

  • Fischer, M.; Schott, A.K.; Kemter, K.; Feicht, R.; Richter, G.; Illarionov, B.; Eisenreich, W.; Gerhardt, S.; Cushman, M.; Steinbacher, S.; Huber, R.; Bacher, A.
    Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments (2003), BMC Biochem., 4, 18.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.9

Application

Application Comment Organism
pharmacology the enzyme is a target for development of antiinfective drugs Schizosaccharomyces pombe

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, subcloning and expression in Escherichia coli strains M15 and XL1-Blue, wild-type and mutant enzymes Schizosaccharomyces pombe

Protein Variants

Protein Variants Comment Organism
C48A site-directed mutagenesis, nearly inactive mutant Schizosaccharomyces pombe
C48M site-directed mutagenesis, nearly inactive mutant Schizosaccharomyces pombe
C48S site-directed mutagenesis, highly decreased activity compared to the wild-type enzyme Schizosaccharomyces pombe
S146A site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme Schizosaccharomyces pombe
S146C site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme Schizosaccharomyces pombe

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0057
-
 6,7-dimethyl-8-(1-D-ribityl)lumazine pH 7.2, 37°C, recombinant enzyme Schizosaccharomyces pombe

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23000
-
 3 * 23000, sedimentation equilibrium centrifugation Schizosaccharomyces pombe

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 Schizosaccharomyces pombe ultimate step in the biosynthesis of riboflavin, pathway overview riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione
-
 r

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe Q9Y7P0 alpha-chain; var. pombe, ATCC 16491
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli by ion exchange chromatography, ultrafiltration, gel filtration, and hydrophobic interaction chromatography Schizosaccharomyces pombe

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 detailed catalytic mechanism, Cys48 is involved Schizosaccharomyces pombe
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
27
-
 purified recombinant mutant C48S Schizosaccharomyces pombe
158
-
 purified recombinant wild-type enzyme Schizosaccharomyces pombe
179
-
 purified recombinant mutant S146C Schizosaccharomyces pombe
183
-
 purified recombinant mutant S146A Schizosaccharomyces pombe

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6,7-dimethyl-8-(1-D-ribityl)lumazine ultimate step in the biosynthesis of riboflavin, pathway overview Schizosaccharomyces pombe riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione
-
 r
6,7-dimethyl-8-(1-D-ribityl)lumazine mechanistically complex dismutation Schizosaccharomyces pombe riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione
-
 r
additional information substrate binding structure and catalytic mechanism by NMR analysis and protein perturbation studies using fluoro-substituted reaction intermediate analogues, i.e. 2 epimers of 6,7-bis(trifluoromethyl)-8-ribityllumazine hydrate, 6-trifluoromethyl-7-oxo-8-ribityllumazine, 6-carboxyethyl-7-oxo-8-ribityllumazine, and 5-nitro-6-ribitylamino-2,4-pyrimidinedione, overview Schizosaccharomyces pombe ?
-
 ?

Subunits

Subunits Comment Organism
More 2 similar folding domains per subunit Schizosaccharomyces pombe
trimer 3 * 23000, sedimentation equilibrium centrifugation Schizosaccharomyces pombe

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Schizosaccharomyces pombe

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Schizosaccharomyces pombe