EC Number |
General Information |
Reference |
---|
1.14.11.56 | evolution |
proline hydroxylases are representative members of the nonheme Fe2+/2-oxoglutarate-dependent dioxygenase family |
743931 |
1.14.11.56 | more |
I95, I97, and E114 are active site residues, the active site was composed of a distorted jelly roll beta-sheet core, which is sandwiched by the N-terminal and C-terminal alpha-helical domains |
743931 |
1.14.11.56 | more |
V95, V97, and G114 are active site residues, a structure homology model of the SmP4H triple mutant V97F/V95W/E114G is constructed based on the MlP4H crystal structure |
743931 |
1.14.11.56 | physiological function |
the enzyme catalyze the hydroxylation of L-proline, generating cis-4-hydroxy-L-proline, as well as the hydroxylation of L-pipecolic acid (L-Pip), generating two regioisomers, cis-5-hydroxypipecolate and cis-3-hydroxypipecolate in a 6:4 ratio |
743931 |