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Literature summary extracted from

  • Fischer, M.; Romisch, W.; Schiffmann, S.; Kelly, M.; Oschkinat, H.; Steinbacher, S.; Huber, R.; Eisenreich, W.; Richter, G.; Bacher, A.
    Biosynthesis of riboflavin in archaea studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii (2002), J. Biol. Chem., 277, 41410-41416.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.12 DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strains XL-1 Blue and M15 Methanocaldococcus jannaschii

Protein Variants

EC Number Protein Variants Comment Organism
4.1.99.12 D21E site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
4.1.99.12 D21N site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
4.1.99.12 D30E site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
4.1.99.12 E185D site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
4.1.99.12 E26D site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
4.1.99.12 E26Q site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
4.1.99.12 E28D site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii
4.1.99.12 H164N site-directed mutagenesis, inactive mutant Methanocaldococcus jannaschii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.99.12 Mg2+
-
 Methanocaldococcus jannaschii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.99.12 25799
-
 2 * 25799, recombinant enzyme, mass spectrometry and SDS-PAGE Methanocaldococcus jannaschii
4.1.99.12 51600
-
 recombinant enzyme, analytical ultrafiltration Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.12 D-ribulose 5-phosphate Methanocaldococcus jannaschii
-
 formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.12 Methanocaldococcus jannaschii
-
 orf MJ0055
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.12 recombinant wild-type and mutant enzymes from Escherichia coli by hydrophobic interaction and hydroxyapatite chromatography, and ultrafiltration Methanocaldococcus jannaschii

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.99.12 D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate reaction mechanism involving intramolecular skeletal rearrangement, a cluster of charged amino acid residues comprising Arg25, Glu26 and Glu28, Asp21 and Asp30 is essential for catalytic activity, as well as His164 and Glu185 Methanocaldococcus jannaschii
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.99.12 0.174
-
 purified enzyme Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.99.12 D-ribulose 5-phosphate
-
 Methanocaldococcus jannaschii formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
 ?
4.1.99.12 D-ribulose 5-phosphate the reaction involves an intramolecular skeletal rearrangement, NMR study Methanocaldococcus jannaschii formate + L-3,4-dihydroxy-2-butanone-4-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.99.12 dimer 2 * 25799, recombinant enzyme, mass spectrometry and SDS-PAGE Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.99.12 37
-
 assay at Methanocaldococcus jannaschii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.99.12 7.5 7.7 assay at Methanocaldococcus jannaschii