EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    5.3.1.12 | D-Glucuronate |
- |
Pectobacterium carotovorum |
D-Fructuronate |
- |
? |
| 5.3.1.12 | D-Glucuronate |
- |
Pedobacter heparinus |
D-Fructuronate |
- |
? |
| 5.3.1.12 | D-Glucuronate |
- |
Halalkalibacterium halodurans |
D-Fructuronate |
- |
? |
| 5.3.1.12 | D-Glucuronate |
- |
Halalkalibacterium halodurans |
D-Fructuronate |
- |
r |
| 5.3.1.12 | D-Glucuronate |
- |
Escherichia coli |
D-Fructuronate |
- |
r |
| 5.3.1.12 | D-Glucuronate |
the mononuclear metal center in the active site is ligated to the C6 carboxylate and the C5 hydroxyl group of the substrate, this hydroxyl group is also hydrogen-bonded to Asp355. The C2 and C3 hydroxyl groups of the substrate are hydrogen bonded to Arg357 and the carbonyl group at C1 is hydrogen bonded to Tyr50 |
Halalkalibacterium halodurans |
D-Fructuronate |
- |
r |
| 5.3.1.12 | D-Glucuronate |
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism |
Escherichia coli |
? |
- |
? |
| 5.3.1.12 | D-Tagaturonate |
first step in the pathway of glucuronic acid metabolism and galacturonic acid metabolism |
Escherichia coli |
? |
- |
? |
| 5.3.1.12 | more |
the enzyme does not participate in the metabolism of heparin or chondroitin sulfate |
Pedobacter heparinus |
? |
- |
? |
| 5.3.1.12 | more |
active site structure and molecular reaction mechanism, proton transfer from C2 of D-glucuronate to C1 that is initiated by the combined actions of Asp-355 from the end of ?-strand 8 and the C-5 hydroxyl of the substrate that is bound to the metal ion. Formation of the proposed cis-enediol intermediate is further facilitated by the shuttling of the proton between the C2 and C1 oxygens by the conserved Tyr50 and/or Arg355 |
Halalkalibacterium halodurans |
? |
- |
? |
