EC Number   |
General Information |
Reference |
|---|
  4.1.1.116 | evolution |
the amino acid sequence of STM2360 shows significant similarity (about 30% identity) to diaminopimelate decarboxylase (DapDC), a fold III pyridoxal 5'-phosphate (PLP) dependent enzyme involved in L-lysine biosynthesis. Homologues of STM2360 with high sequence identity (over 80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio, and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas |
-, 746923 |
| 4.1.1.116 | evolution |
the amino acid sequence of STM2360 shows significant similarity (about 30% identity) to diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), a fold III pyridoxal-5'-phosphate (PLP) dependent enzyme involved in L-lysine biosynthesis. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the decarboxylase and the operon is ornithine. STM2360 is annotated as encoding a second DapDC in Salmonella typhimurium LT2, although it is unable to complement lysine auxotrophy in a lysA mutant |
-, 746923 |
| 4.1.1.116 | physiological function |
the physiological substrate of the decarboxylase (and the operon) is ornithine. No role of DOKDC in relief of acid stress, but the enzyme enzyme plays an important role in microbial metabolism |
-, 746923 |
