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EC Number
General Information
Commentary
Reference
evolution
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
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
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
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; 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
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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
metabolism
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine
metabolism
homoserine dehydrogenase is a key enzyme in the L-threonine pathway
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
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
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
Results 1 - 10 of 15 > >>