EC Number   |
General Information |
Reference  |
|---|
    1.1.1.3 | physiological function |
contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol |
-, 710978 |
| 1.1.1.3 | metabolism |
homoserine dehydrogenase is a key enzyme in the L-threonine pathway |
-, 738802 |
| 1.1.1.3 | physiological function |
the enzyme is naturally allosterically regulated by threonine and isoleucine |
739779 |
| 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 | more |
structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview |
-, 739791 |
| 1.1.1.3 | physiological function |
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine |
-, 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 |
| 1.1.1.3 | physiological function |
the enzyme is involved in cell-wall maintenance and essential amino acid biosynthesis. Homoserine dehydrogenase catalyzes a reaction at the branch point of the pathway leading to lysine biosynthesis. This pathway is also referred to as the diaminopimelate (dap) pathway |
-, 739804 |
| 1.1.1.3 | physiological function |
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway |
-, 739972 |
| 1.1.1.3 | more |
structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207 |
-, 740548 |
