Literature summary extracted from
Steinbacher, S.; Schiffmann, S.; Richter, G.; Huber, R.; Bacher, A.; Fischer, M.
Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: implications for the catalytic mechanism (2003), J. Biol. Chem., 278, 42256-42265.
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.1.99.12 |
E185X |
site-directed mutagenesis, inactive mutant |
Methanocaldococcus jannaschii |
4.1.99.12 |
H147S |
site-directed mutagenesis, the mutant enzyme shows about 10% of the wild-type enzyme activity |
Methanocaldococcus jannaschii |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.1.99.12 |
Ca2+ |
binding structure, overview |
Methanocaldococcus jannaschii |
|
4.1.99.12 |
Mg2+ |
binding structure, overview |
Methanocaldococcus jannaschii |
|
4.1.99.12 |
additional information |
the enzyme depends on divalent metal ions, a dimetal center is involved in substrate binding |
Methanocaldococcus jannaschii |
|
4.1.99.12 |
Zn2+ |
binding structure, overview |
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 |
step in the biosynthesis of riboflavin, vitamin B2, ribulose 5-phosphate is converted into 3,4-dihydroxy-2-butanone 4-phosphate while its C4 atom is released as formate in a sequence of metal-dependent reactions |
formate + L-3,4-dihydroxy-2-butanone-4-phosphate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.99.12 |
Methanocaldococcus jannaschii |
Q60364 |
- |
- |
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 |
active site and reaction mechanism, structure-function relationship, structural coordination spheres are important, residues of the first coordination sphere involved in metal binding are indispensable for catalytic activity, Glu185 is essential for catalytic activity |
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 |
step in the biosynthesis of riboflavin, vitamin B2, ribulose 5-phosphate is converted into 3,4-dihydroxy-2-butanone 4-phosphate while its C4 atom is released as formate in a sequence of metal-dependent reactions |
Methanocaldococcus jannaschii |
formate + L-3,4-dihydroxy-2-butanone-4-phosphate |
- |
? |
|
4.1.99.12 |
D-ribulose 5-phosphate |
a dimetal center is involved in substrate binding, structure-function relationship, overview |
Methanocaldococcus jannaschii |
formate + L-3,4-dihydroxy-2-butanone-4-phosphate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.1.99.12 |
More |
structure-function relationship, overview |
Methanocaldococcus jannaschii |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.1.99.12 |
3,4-dihydroxy-2-butanone 4-phosphate synthase |
- |
Methanocaldococcus jannaschii |
4.1.99.12 |
DBPS |
- |
Methanocaldococcus jannaschii |