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Literature summary extracted from

  • Sarge, S.; Haase, I.; Illarionov, B.; Laudert, D.; Hohmann, H.; Bacher, A.; Fischer, M.
    Catalysis of an essential step in vitamin B2 biosynthesis by a consortium of broad spectrum hydrolases (2015), ChemBioChem, 16, 2466-2469.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.104 expression in Escherichia coli Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.104 0.054
-
 5-amino-6-(5-phospho-D-ribitylamino)uracil pH not specified in the publication, temperature not specified in the publication Bacillus subtilis
3.1.3.104 0.135
-
 FMN pH not specified in the publication, temperature not specified in the publication Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.104 soluble
-
 Bacillus subtilis
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.104 Fe2+ about 50% of the activity with Mg2+ Bacillus subtilis
3.1.3.104 Mg2+ Mg2+ affords maximum catalytic activity over 1-5 mM, half-maximal velocity at 0.2 mM Bacillus subtilis
3.1.3.104 additional information presence of a divalent cation is absolutely required Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.104 30000
-
-
 Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.104 Bacillus subtilis P42962
-
-
3.1.3.104 Bacillus subtilis P70947
-
-
3.1.3.104 Bacillus subtilis P96741
-
-
3.1.3.104 Bacillus subtilis 168 P42962
-
-
3.1.3.104 Bacillus subtilis 168 P70947
-
-
3.1.3.104 Bacillus subtilis 168 P96741
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.104 0.0041
-
 substrate D-glucose 6-phosphate, pH not specified in the publication, temperature not specified in the publication Bacillus subtilis
3.1.3.104 0.0061
-
 substrate ribose 5-phosphate, pH not specified in the publication, temperature not specified in the publication Bacillus subtilis
3.1.3.104 0.0063
-
 substrate 6-phospho-D-gluconate, pH not specified in the publication, temperature not specified in the publication Bacillus subtilis
3.1.3.104 0.69
-
 pH not specified in the publication, temperature not specified in the publication Bacillus subtilis
3.1.3.104 1.7
-
 pH not specified in the publication, temperature not specified in the publication Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.104 5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O
-
 Bacillus subtilis 5-amino-6-(D-ribitylamino)uracil + phosphate
-
 ?
3.1.3.104 5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O
-
 Bacillus subtilis 168 5-amino-6-(D-ribitylamino)uracil + phosphate
-
 ?
3.1.3.104 6-phospho-D-gluconate + H2O
-
 Bacillus subtilis D-gluconate + phosphate
-
 ?
3.1.3.104 6-phospho-D-gluconate + H2O
-
 Bacillus subtilis 168 D-gluconate + phosphate
-
 ?
3.1.3.104 D-glucose 6-phosphate + H2O
-
 Bacillus subtilis D-glucose + phosphate
-
 ?
3.1.3.104 D-glucose 6-phosphate + H2O
-
 Bacillus subtilis 168 D-glucose + phosphate
-
 ?
3.1.3.104 D-ribose 5-phosphate + H2O
-
 Bacillus subtilis D-ribose + phosphate
-
 ?
3.1.3.104 D-ribose 5-phosphate + H2O
-
 Bacillus subtilis 168 D-ribose + phosphate
-
 ?
3.1.3.104 FMN + H2O
-
 Bacillus subtilis riboflavin + phosphate
-
 ?
3.1.3.104 FMN + H2O
-
 Bacillus subtilis 168 riboflavin + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.104 ? x * 30000, SDS-PAGE, recombinant protein with His-tag Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
3.1.3.104 YcsE
-
 Bacillus subtilis
3.1.3.104 YitU
-
 Bacillus subtilis
3.1.3.104 YwtE
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
3.1.3.104 physiological function a ycsE deletion mutant of Bacillus subtilis is not riboflavin dependent. Proteins YwtE and YitU additionally catalyse the hydrolysis of 5-amino-6-(5-phospho-D-ribitylamino)uracil at appreciable rates Bacillus subtilis