EC Number   |
Application |
Reference |
|---|
    2.7.2.4 | agriculture |
enzyme does not exist in animals, good target for conception of new pesticides controlling weeds, fungi and bacteria |
642340 |
| 2.7.2.4 | food industry |
L-lysine, one of the essential amino acids required for nutrition in animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase |
-, 747010 |
| 2.7.2.4 | medicine |
L-lysine, one of the essential amino acids required for nutrition in animals and humans, is widely used in the food industry, medical industry, etc. L-lysine has been mainly produced by microbial fermentation employing mutant strains of bacteria. An L-lysine high-yielding strain is developed by modification of aspartokinase III and dihydrodipicolinate synthetase |
-, 747010 |
| 2.7.2.4 | more |
AK DR1365 is not used for lysine biosynthesis but for threonine and methionine biosynteses, AK TTC0166 in Thermus thermophilus and AK DR1365 in Deinococcus radiodurans have different protein structure and evolutionary origins, but their functions are not different |
-, 678794 |
| 2.7.2.4 | more |
AK has biological importance, as a target candidate for developing new antifungal and antibacterial compounds, because mammals cannot biosynthesize lysine. |
681433 |
| 2.7.2.4 | more |
ASK1 and ASK2 share a high degree of identity with each other, there is one amino acid difference in the Ask2 enzymes of Oh545o2 and Oh51Ao2 |
681136 |
| 2.7.2.4 | more |
The absence of the aspartate biosynthetic pathway in humans makes it a good target for new pesticides and antibiotics. |
693065 |
| 2.7.2.4 | more |
upon binding to the inactive AK1-Lys complex, S-adenosyl-L-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1-Lys-S-adenosyl-L-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-L-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1-Lys towards the inactive form, S-adenosyl-L-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-L-methionine binding |
679764 |
| 2.7.2.4 | more |
upon binding to the inactive AK1Lys complex, S-adenosyl-l-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1LysS-adenosyl-l-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-l-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1Lys towards the inactive form, S-adenosyl-l-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-l-methionine binding |
679764 |
| 2.7.2.4 | nutrition |
enzyme mutants may be used to improve the nutritional quality of rice and other cereal grains |
762121 |
