EC Number   |
General Information |
Reference |
|---|
   1.1.1.272 | evolution |
the enzyme belongs to the family of D-isomer specific 2-hydroxyacid dehydrogenases (2HADHs) that contains a wide range of oxidoreductases with various metabolic roles as well as biotechnological applications. The family comprises 22 subfamilies, the enzyme from Haloferax mediterranei belongs to the DDH subfamily, phylogenetic analysis and tree, overview |
-, 762859 |
| 1.1.1.272 | more |
sequence-structure-function relationships, overview |
-, 762859 |
| 1.1.1.272 | more |
the amino acid residues Arg234, Glu263 and His 279 form the active site of enzyme HDH. Residues Arg234, Ala210, Thr211, and Arg212, which are located on top of the catalytic triad, act as a size filter to jointly determine the substrate specificity |
-, 742168 |
| 1.1.1.272 | physiological function |
the enzyme catalyzes the bioconversion of 2-dehydro-L-gulonic acid to L-idonate, which plays a negative role in the manufacture of vitamin C, cf. EC 1.1.1.215. The primary biochemical function of HDH from Ketogulonicigenium vulgare is C=O bond oxidation-reduction |
-, 742168 |
