EC Number   |
General Information |
Reference |
|---|
    1.2.1.11 | evolution |
the ASADH enzyme family shares the same substrate binding and active site catalytic groups, but the enzymes from representative bacterial and fungal species show different inhibition patterns when previously screened against low molecular weight inhibitors identified from fragment library screening |
742070 |
| 1.2.1.11 | malfunction |
deletion of the asdA gene precluded the growth of Edwardsiella ictaluri in absence of diaminopimelic acid |
-, 726268 |
| 1.2.1.11 | malfunction |
enzyme deficiency or inhibition of enzyme activity leads to 80% reduced cell wall materials compared to the wild-type, in addition to obvious morphological differences, phenotype, overview |
-, 742704 |
| 1.2.1.11 | malfunction |
the aspartate semialdehyde dehydrogenase (asd)-inactivated mutant exhibits significantly reduced growth in calf serum compared with the wild-type. The mutant also exhibits significantly reduced growth in medium, mimicking the concentrations of amino acids and glucose in calf serum, but can be recovered by addition of lysine and threonine |
-, 741702 |
| 1.2.1.11 | metabolism |
Asd is an essential enzyme for the biosynthesis of lysine, methionine, and threonine from aspartate |
-, 741702 |
| 1.2.1.11 | metabolism |
aspartate beta-semialdehyde dehydrogenase is a key enzyme in an essential amino acid biosynthetic pathway catalyzing the second reaction in the aspartate pathway |
725219 |
| 1.2.1.11 | metabolism |
aspartate-beta-semialdehyde dehydrogenase lies at the first branch point in the aspartate metabolic pathway which leads to the biosynthesis of several essential amino acids and some important metabolites. This pathway is crucial for many metabolic processes in plants and microbes like bacteria and fungi, but is absent in mammals |
742070 |
| 1.2.1.11 | metabolism |
aspartate-semialdehyde dehydrogenase catalyzes the reductive dephosphorylation of the substrate beta-aspartyl phosphate into aspartate semialdehyde, a key intermediate in the aspartate biosynthetic pathway and functions at a critical junction in the aspartate biosynthetic pathway |
-, 741535, 741540 |
| 1.2.1.11 | metabolism |
mathematical modeling of the lysine metabolism in Mycobacterium tuberculosis strain H37Rv involving the enzyme, overview |
-, 763308 |
| 1.2.1.11 | metabolism |
the enzyme has a rate-limiting key function in the biosynthesis of amino acids L-threonine, L-lysine, and L-isoleucine from L-aspartate via L-homoserine |
742287 |
