Literature summary for 1.14.11.3 extracted from

Cliffe, L.J.; Hirsch, G.; Wang, J.; Ekanayake, D.; Bullard, W.; Hu, M.; Wang, Y.; Sabatini, R.
JBP1 and JBP2 proteins are Fe2+/2-oxoglutarate-dependent dioxygenases regulating hydroxylation of thymidine residues in trypanosome DNA (2012), J. Biol. Chem., 287, 19886-19895.

Search for more literature for 1.14.11.3

Activating Compound

Activating Compound	Comment	Organism
ascorbate	-	Trypanosoma brucei
ascorbate	-	Trypanosoma cruzi
ascorbate	-	Leishmania tarentolae
ascorbate	-	Leishmania major

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged JBP1 in Escherichia coli strain BL21-DE3 T1R	Trypanosoma cruzi

Protein Variants

Protein Variants	Comment	Organism
additional information	mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine	Trypanosoma brucei
additional information	mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine	Trypanosoma cruzi
additional information	mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine	Leishmania tarentolae
additional information	mutation of the two conserved metal binding ligands of dioxygenases JBP1 and JBP2 results in the loss of Fe2+ binding and inability to hydroxylate thymidine	Leishmania major

Inhibitors

Inhibitors	Comment	Organism
2,4-pyridinedicarboxylic acid	competitive inhibition	Leishmania major
2,4-pyridinedicarboxylic acid	competitive inhibition	Leishmania tarentolae
2,4-pyridinedicarboxylic acid	competitive inhibition	Trypanosoma brucei
2,4-pyridinedicarboxylic acid	competitive inhibition	Trypanosoma cruzi
dimethyloxoglycine	competitive inhibition	Leishmania major
dimethyloxoglycine	competitive inhibition	Leishmania tarentolae
dimethyloxoglycine	competitive inhibition	Trypanosoma brucei
dimethyloxoglycine	competitive inhibition	Trypanosoma cruzi

Metals/Ions

Metals/Ions	Comment	Organism
Fe2+	dependent on	Trypanosoma brucei
Fe2+	dependent on	Trypanosoma cruzi
Fe2+	dependent on	Leishmania tarentolae
Fe2+	dependent on	Leishmania major

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
thymidine + 2-oxoglutarate + O2	Trypanosoma brucei	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	Trypanosoma cruzi	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	Leishmania tarentolae	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	Leishmania major	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	Trypanosoma brucei 427	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	5-hydroxymethyluridine + succinate + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Leishmania major	-	-	-
Leishmania tarentolae	-	-	-
Trypanosoma brucei	-	line 221a	-
Trypanosoma brucei 427	-	line 221a	-
Trypanosoma cruzi	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged JBP1 from Escherichia coli strain BL21-DE3 T1R by metal affinty chromatography	Trypanosoma cruzi

Source Tissue

Source Tissue	Comment	Organism	Textmining
bloodstream form	-	Trypanosoma brucei	-
metacyclic form	infective	Leishmania tarentolae	-
promastigote	-	Leishmania major	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated	Trypanosoma brucei	?	-	?
additional information	thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated	Trypanosoma cruzi	?	-	?
additional information	thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated	Leishmania tarentolae	?	-	?
additional information	thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated	Leishmania major	?	-	?
additional information	thymine in the context of single stranded DNA substrate, rather than duplex DNA, is not hydroxylated	Trypanosoma brucei 427	?	-	?
thymidine + 2-oxoglutarate + O2	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Trypanosoma brucei	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Trypanosoma cruzi	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Leishmania tarentolae	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Leishmania major	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Trypanosoma brucei	5-hydroxymethyluridine + succinate + CO2	mass spectrometric product determination	?
thymidine + 2-oxoglutarate + O2	telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Trypanosoma cruzi	5-hydroxymethyluridine + succinate + CO2	mass spectrometric product determination	?
thymidine + 2-oxoglutarate + O2	telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Leishmania tarentolae	5-hydroxymethyluridine + succinate + CO2	mass spectrometric product determination	?
thymidine + 2-oxoglutarate + O2	telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Leishmania major	5-hydroxymethyluridine + succinate + CO2	mass spectrometric product determination	?
thymidine + 2-oxoglutarate + O2	JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Trypanosoma brucei 427	5-hydroxymethyluridine + succinate + CO2	-	?
thymidine + 2-oxoglutarate + O2	telomeric duplex DNA substrate, JBP1 hydroxylates thymine specifically in the context of dsDNA in a Fe2+-, 2-oxoglutarate-, and O2-dependent manner	Trypanosoma brucei 427	5-hydroxymethyluridine + succinate + CO2	mass spectrometric product determination	?

Synonyms

Synonyms	Comment	Organism
JBP1	-	Trypanosoma brucei
JBP1	-	Trypanosoma cruzi
JBP1	-	Leishmania tarentolae
JBP1	-	Leishmania major
JBP2	-	Trypanosoma brucei
JBP2	-	Trypanosoma cruzi
JBP2	-	Leishmania tarentolae
JBP2	-	Leishmania major

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Trypanosoma brucei
37	-	assay at	Trypanosoma cruzi
37	-	assay at	Leishmania tarentolae
37	-	assay at	Leishmania major

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Trypanosoma brucei
8	-	assay at	Trypanosoma cruzi
8	-	assay at	Leishmania tarentolae
8	-	assay at	Leishmania major

General Information

General Information	Comment	Organism
evolution	JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family	Trypanosoma brucei
evolution	JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family	Trypanosoma cruzi
evolution	JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family	Leishmania tarentolae
evolution	JBP1 and JBP2 are members of the Fe2+/2-OG dioxygenase family	Leishmania major
malfunction	mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation	Trypanosoma brucei
malfunction	mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation	Trypanosoma cruzi
malfunction	mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation	Leishmania tarentolae
malfunction	mutation of residues involved in coordinating Fe2+ inhibit iron binding and thymidine hydroxylation	Leishmania major
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	Trypanosoma brucei
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	Trypanosoma cruzi
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	Leishmania tarentolae
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	Leishmania major
additional information	the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity	Trypanosoma brucei
additional information	the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity	Trypanosoma cruzi
additional information	the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity	Leishmania tarentolae
additional information	the N-terminal thymidine hydroxylase domain of JBP1 is sufficient for full activity	Leishmania major
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	Trypanosoma brucei
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	Trypanosoma cruzi
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	Leishmania tarentolae
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	Leishmania major