EC Number   |
General Information |
Reference |
|---|
    1.4.1.21 | evolution |
L-aspartate dehydrogenase is a rare member of amino acid dehydrogenase superfamily |
724055 |
| 1.4.1.21 | evolution |
L-AspDH members and other putative homologs share surprisingly low homology, below 10%, with the other amino acid dehydrogenases |
-, 724068 |
| 1.4.1.21 | metabolism |
proposed pathways of L-Asp metabolism, overview |
-, 724068 |
| 1.4.1.21 | more |
three-dimensional structure comparisons, overview |
-, 724068 |
| 1.4.1.21 | physiological function |
involvement of L-AspDH in NAD biosynthesis, overview |
-, 724068 |
| 1.4.1.21 | physiological function |
the amination activity of the enzyme may be important for the fixation of inorganic nitrogen |
723988 |
| 1.4.1.21 | physiological function |
the wild-type strain synthesizes 3-hydroxy-polybutyrate from fructose or L-Asp, while the enzyme knockout mutant strain does not. The AspDH cluster might be involved in the biosynthesis of poly-3-hydroxyalkanoates |
-, 724591 |
