EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.3 | gene akthr2, DNA sequence determination and analysis, located on chromosome 4, subcloning in Escherichia coli strain DH5alpha, functional complementation of the Saccharomyces cerevisiae homoserine dehydrogenase-deficient hom6 mutant strain and of the aspartate kinase-deficient hom3 mutant strain, conferring L-threonine and L-methionine prototrophy to the yeast cells | Arabidopsis thaliana |
2.7.2.4 | by functional complementation of a Saccharomyces cerevisiae strain mutated in its homoserine dehydrogenase gene (hom6), expression in Escherichia coli, two of the three isolated clones are also able to complement a mutant yeast aspartate kinase gene (hom3), expression of the AK-HSDH gene in Arabidopsis thaliana (meristematic cells, leaves and stamens) | Arabidopsis thaliana |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.3 | additional information | construction of transgenic Arabidopsis thaliana plants by transformation with gene akthr2 via Agrobacterium tumefaciens infection, determination of expression patterns of the gene akthr1 ans akthr2 in the transgenic plants | Arabidopsis thaliana |
1.1.1.3 | additional information | mutant strain M20-20D is deficient in gene HOM6 and shows no activity, the defect can be complemented by recombinant expression of the Arabidopsis thaliana gene akthr2 in the mutant yeast cells | Saccharomyces cerevisiae |
2.7.2.4 | S2207A | phenotype Thr- Met- Ura- | Arabidopsis thaliana |
2.7.2.4 | S2207A/pM1-1 | mutant S2207A complemented with plasmid pM1-1, phenotype Thr+ Met+ Ura+ | Arabidopsis thaliana |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.3 | L-threonine | - |
Arabidopsis thaliana | |
2.7.2.4 | L-alanine | no significant effect on AK activity at 5 and 20 mM | Arabidopsis thaliana | |
2.7.2.4 | L-isoleucine | no significant effect on AK activity at 5 and 20 mM | Arabidopsis thaliana | |
2.7.2.4 | L-lysine | no significant effect on AK activity at 5 and 20 mM | Arabidopsis thaliana | |
2.7.2.4 | L-threonine | inhibition at 0.5-1.0 mM in complemented S2207A cells is variable, it does not exceed 67% | Arabidopsis thaliana |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.7.2.4 | chloroplast | - |
Arabidopsis thaliana | 9507 | - |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.3 | Mg2+ | required for aspartate kinase activity | Arabidopsis thaliana |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.3 | L-homoserine + NADP+ | Saccharomyces cerevisiae | - |
L-aspartate 4-semialdehyde + NADPH | - |
? | |
1.1.1.3 | L-homoserine + NADP+ | Arabidopsis thaliana | - |
L-aspartate 4-semialdehyde + NADPH | - |
? | |
2.7.2.4 | ATP + L-aspartate | Arabidopsis thaliana | - |
ADP + phospho-L-aspartate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.3 | Arabidopsis thaliana | - |
var. Bensheim showing threonine and methionine prototrophy, bifunctional enzyme showing aspartate dehydrogenase and aspartate kinase activity, gene akthr2 | - |
1.1.1.3 | Saccharomyces cerevisiae | - |
mutant strain M20-20D and wild-type strain S2207A | - |
2.7.2.4 | Arabidopsis thaliana | - |
- |
- |
2.7.2.4 | Arabidopsis thaliana | - |
Saccharomyces cerevisiae M20-20D cells are transformed with A. thaliana cDNA, protein expressed and purified from Saccharomyces cerevisiae, all data refer to the recombinant yeast protein | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.7.2.4 | - |
Arabidopsis thaliana |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.1.1.3 | L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ | bifunctional enzyme showing aspartate kinase, 2.7.2.4, and homoserine dehydrogenase activities | Arabidopsis thaliana |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.1.1.3 | leaf | - |
Arabidopsis thaliana | - |
1.1.1.3 | meristem | - |
Arabidopsis thaliana | - |
1.1.1.3 | additional information | akthr2 is not or time-restricted expressed in stem, gynoecium, and during seed formation | Arabidopsis thaliana | - |
1.1.1.3 | stamen | - |
Arabidopsis thaliana | - |
2.7.2.4 | leaf | - |
Arabidopsis thaliana | - |
2.7.2.4 | meristem | - |
Arabidopsis thaliana | - |
2.7.2.4 | stamen | - |
Arabidopsis thaliana | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.7.2.4 | 0.0013 | - |
mutant S2207A | Arabidopsis thaliana |
2.7.2.4 | 0.0107 | - |
complemented mutant A2207A/pM1-1 | Arabidopsis thaliana |
2.7.2.4 | 0.0268 | - |
wild type X-2180-1A | Arabidopsis thaliana |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.3 | L-homoserine + NADP+ | - |
Saccharomyces cerevisiae | L-aspartate 4-semialdehyde + NADPH | - |
? | |
1.1.1.3 | L-homoserine + NADP+ | - |
Arabidopsis thaliana | L-aspartate 4-semialdehyde + NADPH | - |
? | |
1.1.1.3 | L-homoserine + NADP+ | - |
Arabidopsis thaliana | L-aspartate 4-semialdehyde + NADPH | - |
r | |
2.7.2.4 | ATP + L-aspartate | - |
Arabidopsis thaliana | ADP + phospho-L-aspartate | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.3 | AK-HSDH | - |
Arabidopsis thaliana |
1.1.1.3 | aspartate kinase-homoserine dehydrogenase | - |
Arabidopsis thaliana |
1.1.1.3 | HSDH | - |
Saccharomyces cerevisiae |
2.7.2.4 | AK | - |
Arabidopsis thaliana |
2.7.2.4 | aspartate kinase | - |
Arabidopsis thaliana |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.3 | NADP+ | - |
Saccharomyces cerevisiae | |
1.1.1.3 | NADP+ | - |
Arabidopsis thaliana | |
1.1.1.3 | NADPH | - |
Arabidopsis thaliana |