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Literature summary for 2.6.1.11 extracted from
- The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli (2014), Mol. Microbiol., 94, 843-856.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
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General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | in Escherichia coli, the enzymes with N-acetylornithine aminotransferase (ACOAT) activity in arginine synthesis are ArgD, AstC, GabT and PuuE. The major anaerobic ACOAT is ArgD. Loss of ArgD derepresses arginine biosynthetic enzymes, and could result in higher levels of pathway intermediates that allows an alternate enzyme to catalyze the ACOAT reaction. An ArgD/AstC double mutant has a slower doubling time than an ArgD mutant in glucose-containing minimal medium without arginine. The ArgD mutant is not polyamine deficient during anaerobic growth, and the growth defects of the argD mutant are more severe anaerobically | Escherichia coli |
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