Protein Variants | Comment | Organism |
---|---|---|
Q443A | site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, asparate kinase activity is completely insensitive to inhibition by L-threonine, overview | Arabidopsis thaliana |
Q524A | site-directed mutagenesis, altered reaction kinetics for both activities and altered inhibition pattern by L-threonine compared to the wild-type enzyme, overview | Arabidopsis thaliana |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
L-threonine | the regulatory domain of the enzyme contains 2 binding sites, interaction with Gln443 leads to inhibition of the aspartate kinase activity and facilitates the binding of a second threonine on Gln524 leading to inhibition of the homoserine dehydrogenase activity, inhibition of the forward reactions | Arabidopsis thaliana |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required for aspartate kinase activity | Arabidopsis thaliana |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
320000 | - |
wild-type enzyme in presence of L-threonine, gel filtration | Arabidopsis thaliana |
470000 | - |
wild-type enzyme in absence of L-threonine, mutant enzymes Q443A and Q524A both in presence or absence of L-threonine, gel filtration | Arabidopsis thaliana |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ | bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activities | Arabidopsis thaliana |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-homoserine + NADP+ | - |
Arabidopsis thaliana | L-aspartate 4-semialdehyde + NADPH | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | primary and secondary structure comparison, the bifunctional enzyme contains 2 homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif, the enzymes' regulatory domain is composed of 2 subdomains, amino acid residues 414-453 and 495-534 | Arabidopsis thaliana |
Synonyms | Comment | Organism |
---|---|---|
AK-HSDH | - |
Arabidopsis thaliana |
aspartate kinase-homoserine dehydrogenase | - |
Arabidopsis thaliana |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Arabidopsis thaliana |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Arabidopsis thaliana |