EC Number   |
General Information |
Reference |
|---|
    1.1.1.3 | metabolism |
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine |
-, 740860 |
| 1.1.1.3 | metabolism |
homoserine dehydrogenase is a key enzyme in the L-threonine pathway |
-, 738802 |
| 1.1.1.3 | more |
binding of L-Hse and NADPH induces the conformational changes of TtHSD from an open to a closed form: the mobile loop containing Glu180 approaches to fix L-Hse and NADPH, and both Lys99 and Lys195 make hydrogen bonds with the hydroxy group of L-Hse. The ternary complex of TtHSDs in the closed form mimicks a Michaelis complex better than the previously reported open form structures from other species. Lys99 seems to be the acidx02base catalytic residue of HSD. The substrate L-Hse and the nicotinamide-ribose moiety of the cofactor NADPH are bound to a crevice formed at the interface between the substrate and nucleotide binding domains. In contrast, the adenosine group of NADPH is located at the surface of the enzyme. The open-closed conformational change may play an important role in the formation of the enzymex02substrate-cofactor complex and subsequent enzymatic catalysis |
761404 |
| 1.1.1.3 | more |
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling |
-, 762359 |
| 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 | more |
structure homology modeling of enzyme with bound substrate NAD+ and L-homoserine using the Saccharomyces cerevisiae enzyme (PDB ID 1EBU) as template, binding analysis, overview. The model with the best output is subjected to gradient minimization, redocking, and molecular dynamics simulation |
-, 760354 |
| 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 |
| 1.1.1.3 | more |
three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview |
-, 761687 |
| 1.1.1.3 | physiological function |
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK |
-, 760736 |
| 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 |
