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2.6.1.37 |
| Activity |
2.6.1.37 |
| Description |
(2-aminoethyl)phosphonate--pyruvate aminotransferase |
| Notes |
2-Aminoethylphosphonate (ciliatine) is the precursor of an array of phosphonated compounds (e.g., phosphonopolysaccharides), which are employed by some organisms for specialized functions such as chemical warfare, cell-cell communication, and host recognition. Enzymes in this family may be involved both in the synthesis and the degradation of ciliatine; their sequences are distantly related to those in the dhap aminotransferase family and to those of classic alanine-glyoxylate aminotransferases (family 2.6.1.44a).
Some biosynthetic enzymes (such as the enzyme from Treponema denticola) are part of bifunctional proteins containing also a N-terminal nucleotidyl transferase domain, which has been removed from the sequences included in the family. |
| PDB |
1M32; |
| PLP Fold Type |
I |
| PLP-dependent Domain |
|
| Number of sequences |
0 |
| Reference sequence |
T46947 |
| Domain interval |
6-335 |
| Catalytic site |
194 K |
| | |
|---|
| References |
Articles on 2.6.1.37 |
| last changed |
2019/08/26 09:15 |
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