Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.3.3.7 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 .
No PubMed abstract available
Search for more literature for 4.3.3.7

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 nutritionin 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
H118Y mutant enzyme H56K is more conducive to L-lysine production than mutant H118Y Escherichia coli
H56K mutant enzyme H56K is more conducive to L-lysine production than mutant H118Y Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6L2 strain LATR11 is derived from the wild-type strain Escherichia coli MG1655
-
Escherichia coli LATR11 P0A6L2 strain LATR11 is derived from the wild-type strain Escherichia coli MG1655
-

Synonyms

Synonyms Comment Organism
DHDPS
-
 Escherichia coli