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Literature summary for 2.7.2.4 extracted from

  • Xu, J.; Han, M.; Ren, X.; Zhang, W.
    Modification of aspartokinase III and dihydrodipicolinate synthetase increases the production of L-lysine in Escherichia coli (2016), Biochem. Eng. J., 114, 79-86 .
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Search for more literature for 2.7.2.4

Application

Application Comment Organism
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 Escherichia coli
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 Escherichia coli

Protein Variants

Protein Variants Comment Organism
M318I mutant enzyme T344M is more conducive to L-lysine production than mutant M318I Escherichia coli
T344M mutant enzyme T344M is more conducive to L-lysine production than mutant M318I Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P08660 strain LATR11 is derived from the wild-type strain Escherichia coli MG1655
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Escherichia coli LATR11 P08660 strain LATR11 is derived from the wild-type strain Escherichia coli MG1655
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Synonyms

Synonyms Comment Organism
AK III
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 Escherichia coli
aspartokinase III
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 Escherichia coli