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Literature summary for 3.1.3.104 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
Search for more literature for 3.1.3.104

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Bacillus subtilis
-
-

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P42962
-
-
Bacillus subtilis P70947
-
-
Bacillus subtilis P96741
-
-
Bacillus subtilis 168 P42962
-
-
Bacillus subtilis 168 P70947
-
-
Bacillus subtilis 168 P96741
-
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
YcsE
-
 Bacillus subtilis
YitU
-
 Bacillus subtilis
YwtE
-
 Bacillus subtilis

General Information

General Information Comment Organism
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