EC Number   |
General Information |
Reference |
|---|
    2.7.2.4 | evolution |
the enzyme belongs to class II aspartate kinases |
-, 737545 |
| 2.7.2.4 | evolution |
the enzyme belongs to class III aspartate kinases |
739505 |
| 2.7.2.4 | evolution |
the enzyme from Corynebacterium pekinense belongs to the class II of aspartate kinases |
738419 |
| 2.7.2.4 | evolution |
the enzyme is composed of two domains: an N-terminal catalytic domain (kinase) domain and a C-terminal regulatory domain further comprised of two small domains belonging to the ACT domain family. The enzyme CaAK monomer from Clostridium acetobutylicum belongs to the class I type aspartate kinases which consists of one catalytic domain and two ACT domains |
737927 |
| 2.7.2.4 | evolution |
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain |
760736 |
| 2.7.2.4 | malfunction |
A 2fold increase in lysine production is observed by cloning of the ASK gene in Corynebacterium glutamicum rather than in Escherichia coli, due to the presence of lysine exporter channel which facilitates lysine extraction |
723793 |
| 2.7.2.4 | malfunction |
four-week-old loss-of-function Arabidopsis thaliana mutants in the AK-HSDH2 gene have increased amounts of Asp and Asp-derived amino acids, especially Thr, in leaves, phenotype, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Mutant plant phenotypes, overview |
739356 |
| 2.7.2.4 | malfunction |
the contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Mutant plant phenotypes, overview |
739356 |
| 2.7.2.4 | malfunction |
the contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Mutant plant phenotypes, overview |
739356 |
| 2.7.2.4 | metabolism |
aspartate kinase catalyzes the phosphorylation of aspartate to Asp-phosphate, the first step in the aspartate family biosynthesis pathway. The enzyme is feedback regulated |
739505 |
