Cloned (Comment) | Organism |
---|---|
gene hom, recombinant expression of His-tagged wild-type and mutant enzymes in Echerichia coli strain Rosetta (DE3) pLysS | Staphylococcus aureus |
Crystallization (Comment) | Organism |
---|---|
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution | Staphylococcus aureus |
Protein Variants | Comment | Organism |
---|---|---|
K105A | site-directed double-primer PCR mutagenesis | Staphylococcus aureus |
K105R | site-directed double-primer PCR mutagenesis | Staphylococcus aureus |
K205A | site-directed double-primer PCR mutagenesis | Staphylococcus aureus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-serine | allosteric inhibitor | Staphylococcus aureus | |
L-threonine | allosteric inhibitor | Staphylococcus aureus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic profile | Staphylococcus aureus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-homoserine + NADP+ | Staphylococcus aureus | - |
L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
L-homoserine + NADP+ | Staphylococcus aureus COL | - |
L-aspartate 4-semialdehyde + NADPH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | A0A0H2WVX4 | - |
- |
Staphylococcus aureus COL | A0A0H2WVX4 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant enzymes from Echerichia coli strain Rosetta (DE3) pLysS by nickel affinty chromatography and gel filtration | Staphylococcus aureus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ | role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Lys105, which is located at the interface of the catalytic and cofactor-binding sites, mediates the hydride transfer step of the reaction mechanism of the enzyme. Potential reaction mechanisms for homoserine dehydrogenase, overview | Staphylococcus aureus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-homoserine + NADP+ | - |
Staphylococcus aureus | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r | |
L-homoserine + NADP+ | - |
Staphylococcus aureus COL | L-aspartate 4-semialdehyde + NADPH + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
homodimer | the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview | Staphylococcus aureus |
More | structural basis for the catalytic mechanism of homoserine dehydrogenase, overview | Staphylococcus aureus |
Synonyms | Comment | Organism |
---|---|---|
hom | - |
Staphylococcus aureus |
HSD | - |
Staphylococcus aureus |
SACOL1362 | - |
Staphylococcus aureus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
- |
Staphylococcus aureus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
the catalytic activity of the enzyme for the conversion of L-homoserine to L-aspartate 4-semialdehyde (the reverse reaction) is enhanced at basic pH | Staphylococcus aureus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Staphylococcus aureus | |
NADPH | - |
Staphylococcus aureus |
General Information | Comment | Organism |
---|---|---|
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 | Staphylococcus aureus |
additional information | 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 | Staphylococcus aureus |
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 | Staphylococcus aureus |