EC Number   |
General Information |
Reference |
|---|
   4.2.1.175 | metabolism |
phenylalanine catabolism in the hyperthermophilic archaeon Archaeoglobus fulgidus involves phenylalanine:2-oxoglutarate aminotransferase, phenyllactate dehydrogenase, radical iron-sulfur 3-phenyllactyl-CoA dehydratase, phenylpropionyl-CoA dehydrogenase, aryl pyruvate ferredoxin oxidoreductase, ADP-forming acetyl-CoA synthetase and family III CoA-transferase. The pathway is not fermentative but coupled to sulfate reduction |
-, 752604 |
| 4.2.1.175 | metabolism |
reaction may employ a ketyl radical intermediate |
754879 |
| 4.2.1.175 | metabolism |
the enzyme is involved in fermentation of phenylalanine |
-, 637243 |
| 4.2.1.175 | physiological function |
comparison of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans, Clostridium symbiosum and Fusobacterium nucleatum, 2-phenyllactate dehydratase from Clostridium sporogenes, 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile, and lactyl-CoA dehydratase from Clostridium propionicum. The 2-hydroxyacyl-CoA dehydratases are two-component systems composed of an extremely oxygen-sensitive component A, an activator, and component D, the actual dehydratase. Component A, a homodimer with one [4Fe-4S]cluster, transfers an electron to component D, a heterodimer with 1-2 [4Fe-4S] clusters and FMN, concomitant with hydrolysis of two ATP. From component D the electron is further transferred to the substrate, where it facilitates elimination of the hydroxyl group. In the resulting enoxyradical the beta-hydrogen is activated. After elimination the electron is handed-over to the next incoming substrate without further hydrolysis of ATP. The helix-cluster-helix architecture of component A forms an angle of 105°, which probably opens to 180° upon binding of ATP resembling an archer shooting arrows |
753594 |
| 4.2.1.175 | physiological function |
FldC is essential for the reductive metabolism of aromatic amino acids phenylalanine, tyrosine and tryptophan |
754892 |
| 4.2.1.175 | physiological function |
heterotrimeric phenyllactate dehydratase, FldABC, catalyses the reversible dehydration of (R)-phenyllactate to (E)-cinnamate in two steps: first CoA-transfer from the cofactor cinnamoyl-CoA to phenyllactate to yield phenyllactyl-CoA and the product cinnamate mediated by FldA, a (R)-phenyllactate CoA-transferase, second dehydration of phenyllactyl-CoA to cinnamoyl-CoA mediated by heterodimeric FldBC, a phenyllactyl-CoA dehydratase. Phenyllactate dehydratase requires initiation by ATP, MgCl2 and a reducing agent such as dithionite mediated by an extremely oxygen-sensitive initiator protein (FldI) present in the cell-free extract |
754768 |
