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Literature summary for 1.14.11.6 extracted from

  • Cliffe, L.J.; Kieft, R.; Southern, T.; Birkeland, S.R.; Marshall, M.; Sweeney, K.; Sabatini, R.
    JBP1 and JBP2 are two distinct thymidine hydroxylases involved in J biosynthesis in genomic DNA of African trypanosomes (2009), Nucleic Acids Res., 37, 1452-1462.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of either the wild type JBP2 or the mutant JBP2 proteins in insect stage trypanosomes, which do not contain the modified base J and determined the base J content of each cell line, mutations made within the key catalytic domain ablates the ability of JBP2 to initiate de novo base J synthesis Trypanosoma brucei

Protein Variants

Protein Variants Comment Organism
D393A site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2 inside the catalytic domain Trypanosoma brucei
H391A site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2, expression of the TH mutant H319A fails to stimulate base J formation Trypanosoma brucei
H441A site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2 inside the catalytic domain Trypanosoma brucei
R445A site-directed mutagenesis, mutation inside the catalytic domain, procyclic cells expressing mutant versions of JBP2 inside the catalytic domain Trypanosoma brucei
V459A site-directed mutagenesis, control substitution of a residue outside the catalytic domain Trypanosoma brucei

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Trypanosoma brucei 5634
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ 4 residues within this motif are critical for the coordination of Fe2+ and 2-oxoglutarate binding as well as functionality of this family of enzymes Trypanosoma brucei
Fe2+ acts as cofactor, 4 residues within this motif are critical for the coordination of Fe2+ and 2-oxoglutarate binding as well as functionality of this family of enzymes Trypanosoma brucei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
thymine + 2-oxoglutarate + O2 Trypanosoma brucei
-
5-hydroxymethyluracil + succinate + CO2
-
?

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei
-
-
-
Trypanosoma brucei Q57X81
-
-

Source Tissue

Source Tissue Comment Organism Textmining
29-13 cell insect stage Trypanosoma brucei
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thymine + 2-oxoglutarate + O2
-
Trypanosoma brucei 5-hydroxymethyluracil + succinate + CO2
-
?

Synonyms

Synonyms Comment Organism
Fe2+/2-oxoglutarate dependent hydroxylase
-
Trypanosoma brucei
J binding protein 1
-
Trypanosoma brucei
J binding protein 2
-
Trypanosoma brucei
JBP1
-
Trypanosoma brucei
JBP2
-
Trypanosoma brucei
thymidine hydroxylase
-
Trypanosoma brucei