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Results 1 - 5 of 5
EC Number
General Information
Commentary
Reference
evolution
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
malfunction
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
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
more
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
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
Results 1 - 5 of 5