1.14.11.3: pyrimidine-deoxynucleoside 2'-dioxygenase
This is an abbreviated version!
For detailed information about pyrimidine-deoxynucleoside 2'-dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.3
-
1.14.11.3
-
thymine
-
alpha-ketoglutarate
-
7-hydroxylase
-
ascorbate
-
rhodotorula
-
nidulans
-
co2
-
uracil
-
salvage
-
5-hydroxymethyluracil
-
crassa
-
neurospora
-
glutinis
- 1.14.11.3
- thymine
- alpha-ketoglutarate
-
7-hydroxylase
- ascorbate
-
rhodotorula
- nidulans
- co2
- uracil
-
salvage
- 5-hydroxymethyluracil
- crassa
- neurospora
- glutinis
Reaction
Synonyms
deoxyuridine 2'-dioxygenase, deoxyuridine 2'-hydroxylase, JBP1, JBP2, pyrimidine deoxyribonucleoside 2'-hydroxylase, thymidine 2'-dioxygenase, thymidine 2'-hydroxylase, thymidine 2-oxoglutarate dioxygenase, thymidine dioxygenase
ECTree
Advanced search results
General Information
General Information on EC 1.14.11.3 - pyrimidine-deoxynucleoside 2'-dioxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family
-
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
malfunction
-
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
malfunction
-
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
malfunction
-
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
malfunction
-
mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation
-
-
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
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
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
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
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
-
-
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
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
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
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
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
-
-
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
additional information
-
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
additional information
-
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
additional information
-
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
additional information
-
the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity
-