1.14.11.3	evolution	JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family	-, 725475	
1.14.11.3	malfunction	mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation	-, 725475	
1.14.11.3	metabolism	JBP1 and JBP2 utilize 2-oxoglutarate and O2 as co-substrate to hydroxylate T-residues in dsDNA, releasing succinate and CO2 as byproducts. The intermediate hmU is then glycosylated by an unknown glucosyltransferase forming base J, two-step base J-biosynthesis pathway of modifying T-residues in kinetoplastid DNA	-, 725475	
1.14.11.3	additional information	the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity	-, 725475	
1.14.11.3	physiological function	the enzyme regulating the hydroxylation of specific T-residues along the chromosome is critical for the control of trypanosome gene expression. JBP activity is regulated by oxygen levels in vivo	-, 725475