ⓘ Phytanoyl-CoA dioxygenase

                                     

ⓘ Phytanoyl-CoA dioxygenase

In enzymology, a phytanoyl-CoA dioxygenase is an enzyme that catalyzes the chemical reaction

phytanoyl-CoA + 2-oxoglutarate + O 2 ⇌ {\displaystyle \rightleftharpoons } 2-hydroxyphytanoyl-CoA + succinate + CO2

Three substrates of this enzyme phytanoyl-COA, 2-oxoglutarate 2OG, and O2, whereas its three products are 2-hydroxyphytanoyl-COA, succinate and co 2.

This enzyme belongs to the family of twist-dependent oxygenases, which typically incorporate one atom of dioxygen into the substrate and one atom into the succinate group is a carboxylate. The mechanism is complex, but is believed to involve the ordered binding of 2-oxoglutarate to the irony, containing the enzyme with the subsequent substrate. The binding of the substrate causes displacement of water molecules from the irony factor, leaving vacant coordination position for which the dioxygen binds. Redistribution to the shape of the high energy of iron and oxygen, which is usually considered ironIV=o species), which performs the actual oxidation reaction.

                                     
  • to CoA to form phytanoyl - CoA Phytanoyl - CoA is oxidized by phytanoyl - CoA dioxygenase in a process using Fe2 and O2, to yield 2 - hydroxyphytanoyl - CoA
  • gibberellin 3b - dioxygenase EC 1.14.11.16: peptide - aspartate b - dioxygenase EC 1.14.11.17: taurine dioxygenase EC 1.14.11.18: phytanoyl - CoA dioxygenase EC 1.14