EC Number   |
General Information |
Reference |
|---|
    1.1.1.3 | evolution |
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants |
-, 760354 |
| 1.1.1.3 | evolution |
structure-function analysis and comparisons |
761404 |
| 1.1.1.3 | evolution |
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases |
-, 741408 |
| 1.1.1.3 | evolution |
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain |
-, 760736 |
| 1.1.1.3 | malfunction |
HOM6 deletions cause translational arrest in cells grown under amino acid starvation conditions. HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices. HOM6-homozygous mutants are hypersensitive to hygromycin B and cycloheximide as compared with wild-type, HOM6-heterozygous, and HOM6-reintegrated strains. HOM6 deletion affects translation and leads to the accumulation of free ribosomes |
-, 740860 |
| 1.1.1.3 | malfunction |
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production |
-, 762359 |
| 1.1.1.3 | metabolism |
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview |
-, 760736 |
| 1.1.1.3 | metabolism |
homoserine dehydrogenase (HSD) catalyzes the reversible conversion of L-aspartate-4-semialdehyde to L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine |
-, 761687 |
| 1.1.1.3 | metabolism |
homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine |
-, 739791 |
| 1.1.1.3 | metabolism |
homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine |
-, 739804 |
