Enzymes
UniProtKB help_outline | 6,457 proteins |
GO Molecular Function help_outline |
|
Reaction participants Show >> << Hide
- Name help_outline β-D-fructose 6-phosphate Identifier CHEBI:57634 (Beilstein: 6422468) help_outline Charge -2 Formula C6H11O9P InChIKeyhelp_outline BGWGXPAPYGQALX-ARQDHWQXSA-L SMILEShelp_outline OC[C@@]1(O)O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-glyceraldehyde 3-phosphate Identifier CHEBI:59776 (Beilstein: 6139851) help_outline Charge -2 Formula C3H5O6P InChIKeyhelp_outline LXJXRIRHZLFYRP-VKHMYHEASA-L SMILEShelp_outline [H]C(=O)[C@H](O)COP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 33 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dihydroxyacetone Identifier CHEBI:16016 (Beilstein: 1740268; CAS: 96-26-4) help_outline Charge 0 Formula C3H6O3 InChIKeyhelp_outline RXKJFZQQPQGTFL-UHFFFAOYSA-N SMILEShelp_outline C(CO)(CO)=O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:28002 | RHEA:28003 | RHEA:28004 | RHEA:28005 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
|||
Gene Ontology help_outline | ||||
MetaCyc help_outline | ||||
EcoCyc help_outline |
Publications
-
Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases.
Schuermann M., Sprenger G.A.
We have cloned an open reading frame from the Escherichia coli K-12 chromosome that had been assumed earlier to be a transaldolase or a transaldolase-related protein, termed MipB. Here we show that instead a novel enzyme activity, fructose-6-phosphate aldolase, is encoded by this open reading fram ... >> More
We have cloned an open reading frame from the Escherichia coli K-12 chromosome that had been assumed earlier to be a transaldolase or a transaldolase-related protein, termed MipB. Here we show that instead a novel enzyme activity, fructose-6-phosphate aldolase, is encoded by this open reading frame, which is the first report of an enzyme that catalyzes an aldol cleavage of fructose 6-phosphate from any organism. We propose the name FSA (for fructose-six phosphate aldolase; gene name fsa). The recombinant protein was purified to apparent homogeneity by anion exchange and gel permeation chromatography with a yield of 40 mg of protein from 1 liter of culture. By using electrospray tandem mass spectroscopy, a molecular weight of 22,998 per subunit was determined. From gel filtration a size of 257,000 (+/-20,000) was calculated. The enzyme most likely forms either a decamer or dodecamer of identical subunits. The purified enzyme displayed a V(max) of 7 units mg(-)1 of protein for fructose 6-phosphate cleavage (at 30 degrees C, pH 8.5 in 50 mm glycylglycine buffer). For the aldolization reaction a V(max) of 45 units mg(-)1 of protein was found; K(m) values for the substrates were 9 mm for fructose 6-phosphate, 35 mm for dihydroxyacetone, and 0.8 mm for glyceraldehyde 3-phosphate. FSA did not utilize fructose, fructose 1-phosphate, fructose 1,6-bisphosphate, or dihydroxyacetone phosphate. FSA is not inhibited by EDTA which points to a metal-independent mode of action. The lysine 85 residue is essential for its action as its exchange to arginine (K85R) resulted in complete loss of activity in line with the assumption that the reaction mechanism involves a Schiff base formation through this lysine residue (class I aldolase). Another fsa-related gene, talC of Escherichia coli, was shown to also encode fructose-6-phosphate aldolase activity and not a transaldolase as proposed earlier. << Less